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Journal articles on the topic 'Cysteine-rich peptide'

Author: Grafiati

Published: 4 June 2021

Last updated: 7 February 2022

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1

Shahin-Kaleybar, Behzad, Ali Niazi, Alireza Afsharifar, Ghorbanali Nematzadeh, Reza Yousefi, Bernhard Retzl, Roland Hellinger, Edin Muratspahić, and Christian W. Gruber. "Isolation of Cysteine-Rich Peptides from Citrullus colocynthis." Biomolecules 10, no. 9 (September 16, 2020): 1326. http://dx.doi.org/10.3390/biom10091326.

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The plant Citrullus colocynthis, a member of the squash (Cucurbitaceae) family, has a long history in traditional medicine. Based on the ancient knowledge about the healing properties of herbal preparations, plant-derived small molecules, e.g., salicylic acid, or quinine, have been integral to modern drug discovery. Additionally, many plant families, such as Cucurbitaceae, are known as a rich source for cysteine-rich peptides, which are gaining importance as valuable pharmaceuticals. In this study, we characterized the C. colocynthis peptidome using chemical modification of cysteine residues, and mass shift analysis via matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry. We identified the presence of at least 23 cysteine-rich peptides in this plant, and eight novel peptides, named citcol-1 to -8, with a molecular weight between ~3650 and 4160 Da, were purified using reversed-phase high performance liquid chromatography (HPLC), and their amino acid sequences were determined by de novo assignment of b- and y-ion series of proteolytic peptide fragments. In silico analysis of citcol peptides revealed a high sequence similarity to trypsin inhibitor peptides from Cucumis sativus, Momordica cochinchinensis, Momordica macrophylla and Momordica sphaeroidea. Using genome/transcriptome mining it was possible to identify precursor sequences of this peptide family in related Cucurbitaceae species that cluster into trypsin inhibitor and antimicrobial peptides. Based on our analysis, the presence or absence of a crucial Arg/Lys residue at the putative P1 position may be used to classify these common cysteine-rich peptides by functional properties. Despite sequence homology and the common classification into the inhibitor cysteine knot family, these peptides appear to have diverse and additional bioactivities yet to be revealed.

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2

Ueberheide, Beatrix M., David Fenyö, Paul F. Alewood, and Brian T. Chait. "Rapid sensitive analysis of cysteine rich peptide venom components." Proceedings of the National Academy of Sciences 106, no. 17 (April 20, 2009): 6910–15. http://dx.doi.org/10.1073/pnas.0900745106.

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Disulfide-rich peptide venoms from animals such as snakes, spiders, scorpions, and certain marine snails represent one of nature's great diversity libraries of bioactive molecules. The various species of marine cone shells have alone been estimated to produce >50,000 distinct peptide venoms. These peptides have stimulated considerable interest because of their ability to potently alter the function of specific ion channels. To date, only a small fraction of this immense resource has been characterized because of the difficulty in elucidating their primary structures, which range in size between 10 and 80 aa, include up to 5 disulfide bonds, and can contain extensive posttranslational modifications. The extraordinary complexity of crude venoms and the lack of DNA databases for many of the organisms of interest present major analytical challenges. Here, we describe a strategy that uses mass spectrometry for the elucidation of the mature peptide toxin components of crude venom samples. Key to this strategy is our use of electron transfer dissociation (ETD), a mass spectrometric fragmentation technique that can produce sequence information across the entire peptide backbone. However, because ETD only yields comprehensive sequence coverage when the charge state of the precursor peptide ion is sufficiently high and the m/z ratio is low, we combined ETD with a targeted chemical derivatization strategy to increase the charge state of cysteine-containing peptide toxins. Using this strategy, we obtained full sequences for 31 peptide toxins, using just 7% of the crude venom from the venom gland of a single cone snail (Conus textile).

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3

Foden, Callum S., Saidul Islam, Christian Fernández-García, Leonardo Maugeri, Tom D. Sheppard, and Matthew W. Powner. "Prebiotic synthesis of cysteine peptides that catalyze peptide ligation in neutral water." Science 370, no. 6518 (November 12, 2020): 865–69. http://dx.doi.org/10.1126/science.abd5680.

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Peptide biosynthesis is performed by ribosomes and several other classes of enzymes, but a simple chemical synthesis may have created the first peptides at the origins of life. α-Aminonitriles—prebiotic α–amino acid precursors—are generally produced by Strecker reactions. However, cysteine’s aminothiol is incompatible with nitriles. Consequently, cysteine nitrile is not stable, and cysteine has been proposed to be a product of evolution, not prebiotic chemistry. We now report a high-yielding, prebiotic synthesis of cysteine peptides. Our biomimetic pathway converts serine to cysteine by nitrile-activated dehydroalanine synthesis. We also demonstrate that N-acylcysteines catalyze peptide ligation, directly coupling kinetically stable—but energy-rich—α-amidonitriles to proteinogenic amines. This rare example of selective and efficient organocatalysis in water implicates cysteine as both catalyst and precursor in prebiotic peptide synthesis.

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4

Chen, Shiyu, Inmaculada Rentero Rebollo, Sergey A. Buth, Julia Morales-Sanfrutos, Jeremy Touati, Petr G. Leiman, and Christian Heinis. "Bicyclic Peptide Ligands Pulled out of Cysteine-Rich Peptide Libraries." Journal of the American Chemical Society 135, no. 17 (April 17, 2013): 6562–69. http://dx.doi.org/10.1021/ja400461h.

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5

Braga, Maria Cristina Vianna, Arthur Andrade Nery, Henning Ulrich, Katsuhiro Konno, Juliana Mozer Sciani, and Daniel Carvalho Pimenta. "α-RgIB: A Novel Antagonist Peptide of Neuronal Acetylcholine Receptor Isolated from Conus regius Venom." International Journal of Peptides 2013 (February 27, 2013): 1–9. http://dx.doi.org/10.1155/2013/543028.

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Conus venoms are rich sources of biologically active peptides that act specifically on ionic channels and metabotropic receptors present at the neuromuscular junction, efficiently paralyzing the prey. Each species of Conus may have 50 to 200 uncharacterized bioactive peptides with pharmacological interest. Conus regius is a vermivorous species that inhabits Northeastern Brazilian tropical waters. In this work, we characterized one peptide with activity on neuronal acetylcholine receptor (nAChR). Crude venom was purified by reverse-phase HPLC and selected fractions were screened and sequenced by mass spectrometry, MALDI-ToF, and ESI-Q-ToF, respectively. A new peptide was identified, bearing two disulfide bridges. The novel 2,701 Da peptide belongs to the cysteine framework I, corresponding to the cysteine pattern CC-C-C. The biological activity of the purified peptide was tested by intracranial injection in mice, and it was observed that high concentrations induced hyperactivity in the animals, whereas lower doses caused breathing difficulty. The activity of this peptide was assayed in patch-clamp experiments, on nAChR-rich cells, in whole-cell configuration. The peptide blocked slow rise-time neuronal receptors, probably α3β4 and/or α3β4α5 subtype. According to the nomenclature, the new peptide was designated as α-RgIB.

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6

Čemažar, Maša, and David J. Craik. "Microwave-assisted Boc-solid phase peptide synthesis of cyclic cysteine-rich peptides." Journal of Peptide Science 14, no. 6 (2008): 683–89. http://dx.doi.org/10.1002/psc.972.

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7

Bortolini, Christian, and Mingdong Dong. "Cystine oligomers successfully attached to peptide cysteine-rich fibrils." Frontiers of Chemical Science and Engineering 10, no. 1 (January 25, 2016): 99–102. http://dx.doi.org/10.1007/s11705-016-1554-6.

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8

Kuhn-Nentwig, Lucia, Nicolas Langenegger, Manfred Heller, Dominique Koua, and Wolfgang Nentwig. "The Dual Prey-Inactivation Strategy of Spiders—In-Depth Venomic Analysis of Cupiennius salei." Toxins 11, no. 3 (March 19, 2019): 167. http://dx.doi.org/10.3390/toxins11030167.

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Most knowledge of spider venom concerns neurotoxins acting on ion channels, whereas proteins and their significance for the envenomation process are neglected. The here presented comprehensive analysis of the venom gland transcriptome and proteome of Cupiennius salei focusses on proteins and cysteine-containing peptides and offers new insight into the structure and function of spider venom, here described as the dual prey-inactivation strategy. After venom injection, many enzymes and proteins, dominated by α-amylase, angiotensin-converting enzyme, and cysteine-rich secretory proteins, interact with main metabolic pathways, leading to a major disturbance of the cellular homeostasis. Hyaluronidase and cytolytic peptides destroy tissue and membranes, thus supporting the spread of other venom compounds. We detected 81 transcripts of neurotoxins from 13 peptide families, whereof two families comprise 93.7% of all cysteine-containing peptides. This raises the question of the importance of the other low-expressed peptide families. The identification of a venom gland-specific defensin-like peptide and an aga-toxin-like peptide in the hemocytes offers an important clue on the recruitment and neofunctionalization of body proteins and peptides as the origin of toxins.

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9

Cociancich, S., A. Dupont, G. Hegy, R. Lanot, F. Holder, C. Hetru, J. A. Hoffmann, and P. Bulet. "Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus." Biochemical Journal 300, no. 2 (June 1, 1994): 567–75. http://dx.doi.org/10.1042/bj3000567.

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Insects belonging to the recent orders of the endopterygote clade (Lepidoptera, Diptera, Hymenoptera and Coleoptera) respond to bacterial challenge by the rapid and transient synthesis of a battery of potent antibacterial peptides which are secreted into their haemolymph. Here we present the first report on inducible antibacterial molecules in the sap-sucking bug Pyrrhocoris apterus, a representative species of the Hemiptera, which predated the Endoptergotes by at least 50 million years in evolution. We have isolated and characterized from immune blood of this species three novel peptides or polypeptides: (i) a 43-residue cysteine-rich anti-(Gram-positive bacteria) peptide which is a new member of the family of insect defensins; (ii) a 20-residue proline-rich peptide carrying an O-glycosylated substitution (N-acetylgalactosamine), active against Gram-negative bacteria; (iii) a 133-residue glycine-rich polypeptide also active against Gram-negative bacteria. The proline-rich peptide shows high sequence similarities with drosocin, an O-glycosylated antibacterial peptide from Drosophila, and also with the N-terminal domain of diptericin, an inducible 9 kDa antibacterial peptide from members of the order Diptera, whereas the glycine-rich peptide has similarities with the glycine-rich domain of diptericin. We discuss the evolutionary aspects of these findings.

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10

Cuthbertson, Brandon J., Yinshan Yang, Evelyne Bachère, Erika E. Büllesbach, Paul S. Gross, and André Aumelas. "Solution Structure of Synthetic Penaeidin-4 with Structural and Functional Comparisons with Penaeidin-3." Journal of Biological Chemistry 280, no. 16 (February 7, 2005): 16009–18. http://dx.doi.org/10.1074/jbc.m412420200.

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Antimicrobial peptide structure has direct implications for the complexity of functions and mechanisms of action. The penaeidin antimicrobial peptide family from shrimp is divided into multiple class designations based on primary structure. The penaeidin classes are not only characterized by variability in primary sequence but also by variation in target specificity and effectiveness. Whereas class 4 exhibits low isoform diversity within species and is highly conserved between species, the primary sequence of penaeidin class 3 is less conserved between species and exhibits considerable isoform diversity within species. All penaeidins, regardless of class or species, are composed of two dramatically different domains: an unconstrained proline-rich domain and a disulfide bond-stabilized cysteine-rich domain. The proline-rich domain varies in length and is generally less conserved, whereas the spacing and specific residue content of the cysteine-rich domain is more conserved. The structure of the synthetic penaeidin class 4 (PEN4-1) fromLitopenaeus setiferuswas analyzed using several approaches, including chemical mapping of disulfide bonds, circular dichroism analysis of secondary structural characteristics, and complete characterization of the solution structure of the peptide by proton NMR.L. setiferusPEN4-1 was then compared with the previously characterized structure of penaeidin class 3 fromLitopenaeus vannamei. Moreover, the specificity of these antimicrobial peptides was examined through direct comparison of activity against a panel of microbes. The penaeidin classes differ in microbial target specificity, which correlates to variability in specific domain sequence. However, the tertiary structure of the cysteine-rich domain and indeed the overall structure of penaeidins are conserved across classes.

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11

Terrier, Victor P., Agnès F. Delmas, and Vincent Aucagne. "Efficient synthesis of cysteine-rich cyclic peptides through intramolecular native chemical ligation of N-Hnb-Cys peptide crypto-thioesters." Organic & Biomolecular Chemistry 15, no. 2 (2017): 316–19. http://dx.doi.org/10.1039/c6ob02546c.

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We herein introduce a straightforward synthetic route to cysteine-containing cyclic peptides. It is based on the intramolecular native chemical ligation of thioesters generated in situ from N-Hnb-Cys crypto-thioesters. The strategy is applied to a representative range of natural cyclic disulfide-rich peptide sequences.

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12

Kam, Antony, Shining Loo, Bamaprasad Dutta, Siu Kwan Sze, and James P. Tam. "Plant-derived mitochondria-targeting cysteine-rich peptide modulates cellular bioenergetics." Journal of Biological Chemistry 294, no. 11 (January 23, 2019): 4000–4011. http://dx.doi.org/10.1074/jbc.ra118.006693.

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13

Shimony, Ethan, Tsoyue Sun, Ludmilla Kolmakova-Partensky, and Christopher Miller. "Engineering a uniquely reactive thiol into a cysteine-rich peptide." "Protein Engineering, Design and Selection" 7, no. 4 (1994): 503–7. http://dx.doi.org/10.1093/protein/7.4.503.

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14

Lee, Chul Won, Kazuki Sato, and Jae Il Kim. "Determination of Disulfide Bond Connectivity of Cysteine-rich Peptide IpTxa." Bulletin of the Korean Chemical Society 34, no. 6 (June 20, 2013): 1903–5. http://dx.doi.org/10.5012/bkcs.2013.34.6.1903.

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15

Gegenhuber, Thomas, Doris Abt, Alexander Welle, Suat Özbek, Anja S. Goldmann, and Christopher Barner-Kowollik. "Spatially resolved photochemical coding of reversibly anchored cysteine-rich domains." Journal of Materials Chemistry B 5, no. 25 (2017): 4993–5000. http://dx.doi.org/10.1039/c7tb00962c.

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16

Shelenkov, Andrey, Anna Slavokhotova, and Tatyana Odintsova. "Predicting Antimicrobial and Other Cysteine-Rich Peptides in 1267 Plant Transcriptomes." Antibiotics 9, no. 2 (February 4, 2020): 60. http://dx.doi.org/10.3390/antibiotics9020060.

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Antimicrobial peptides (AMPs) are a key component of innate immunity in various organisms including bacteria, insects, mammals, and plants. Their mode of action decreases the probability of developing resistance in pathogenic organisms, which makes them a promising object of study. However, molecular biology methods for searching for AMPs are laborious and expensive, especially for plants. Earlier, we developed a computational pipeline for identifying potential AMPs based on the cysteine motifs they usually possess. Since most motifs are too species-specific, a wide-scale screening of novel data is required to maintain the accuracy of searching algorithms. We have performed a search for potential AMPs in 1267 plant transcriptomes using our pipeline. On average, 50–150 peptides were revealed in each transcriptome. The data was verified by a BLASTp search in nr database to confirm peptide functions and by using random nucleotide sequences to estimate the fraction of erroneous predictions. The datasets obtained will be useful both for molecular biologists investigating AMPs in various organisms and for bioinformaticians developing novel algorithms of motif searching in transcriptomic and genomic sequences. The results obtained will represent a good reference point for future investigations in the fields mentioned above.

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17

Bortolini, Christian, Lei Liu, Zheshen Li, Karen Thomsen, Chen Wang, Flemming Besenbacher, and Mingdong Dong. "Identification of Cysteine-Rich Peptide-Fiber by Specific Cysteine-Au Nanoparticles Binding on Fiber Surface." Advanced Materials Interfaces 1, no. 9 (July 9, 2014): 1400133. http://dx.doi.org/10.1002/admi.201400133.

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18

Shabab, Mohammed, Markus F. F. Arnold, Jon Penterman, Andrew J. Wommack, Hartmut T. Bocker, Paul A. Price, Joel S. Griffitts, Elizabeth M. Nolan, and Graham C. Walker. "Disulfide cross-linking influences symbiotic activities of nodule peptide NCR247." Proceedings of the National Academy of Sciences 113, no. 36 (August 22, 2016): 10157–62. http://dx.doi.org/10.1073/pnas.1610724113.

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Interactions of rhizobia with legumes establish the chronic intracellular infection that underlies symbiosis. Within nodules of inverted repeat-lacking clade (IRLC) legumes, rhizobia differentiate into nitrogen-fixing bacteroids. This terminal differentiation is driven by host nodule-specific cysteine-rich (NCR) peptides that orchestrate the adaptation of free-living bacteria into intracellular residents. Medicago truncatula encodes a family of >700 NCR peptides that have conserved cysteine motifs. NCR247 is a cationic peptide with four cysteines that can form two intramolecular disulfide bonds in the oxidized forms. This peptide affects Sinorhizobium meliloti transcription, translation, and cell division at low concentrations and is antimicrobial at higher concentrations. By preparing the three possible disulfide–cross-linked NCR247 regioisomers, the reduced peptide, and a variant lacking cysteines, we performed a systematic study of the effects of intramolecular disulfide cross-linking and cysteines on the activities of an NCR peptide. The relative activities of the five NCR247 variants differed strikingly among the various bioassays, suggesting that the NCR peptide-based language used by plants to control the development of their bacterial partners during symbiosis is even greater than previously recognized. These patterns indicate that certain NCR bioactivities require cysteines whereas others do not. The results also suggest that NCR247 may exert some of its effects within the cell envelope whereas other activities occur in the cytoplasm. BacA, a membrane protein that is critical for symbiosis, provides protection against all bactericidal forms of NCR247. Oxidative folding protects NCR247 from degradation by the symbiotically relevant metalloprotease HrrP (host range restriction peptidase), suggesting that disulfide bond formation may additionally stabilize NCR peptides during symbiosis.

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Kumari, Geeta, Aida Serra, Joon Shin, Phuong Q. T. Nguyen, Siu Kwan Sze, Ho Sup Yoon, and James P. Tam. "Cysteine-Rich Peptide Family with Unusual Disulfide Connectivity from Jasminum sambac." Journal of Natural Products 78, no. 11 (November 10, 2015): 2791–99. http://dx.doi.org/10.1021/acs.jnatprod.5b00762.

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20

Góngora-Benítez, Miriam, Judit Tulla-Puche, Marta Paradís-Bas, Oleg Werbitzky, Matthieu Giraud, and Fernando Albericio. "Optimized Fmoc solid-phase synthesis of the cysteine-rich peptide linaclotide." Biopolymers 96, no. 1 (August 21, 2010): 69–80. http://dx.doi.org/10.1002/bip.21480.

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21

Couto, M. A., S. S. Harwig, J. S. Cullor, J. P. Hughes, and R. I. Lehrer. "eNAP-2, a novel cysteine-rich bactericidal peptide from equine leukocytes." Infection and Immunity 60, no. 12 (1992): 5042–47. http://dx.doi.org/10.1128/iai.60.12.5042-5047.1992.

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22

Yuan, Liu, Meng Guo-Quan, Zhou Jian-Ping, Zhang Teng, Feng Juan, and Ren Zheng-long. "Expression, purification and identification of gibberellin-induced cysteine-rich protein ofGymanadenia conopsea." Chinese Journal of Agricultural Biotechnology 6, no. 3 (December 2009): 271–76. http://dx.doi.org/10.1017/s1479236209990155.

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AbstractPrimers bearing restriction enzyme sites forEcoR I andHind III were designed according to the known partial cDNA sequence for gibberellin-induced cysteine-rich protein and were then used to amplify the full-length open reading frame (ORF) and signal peptide-truncated fragment of thegcgasagene. Two fragments with lengths 319 and 238 bp were obtained and were further cloned into plasmid pET-32(a). Following transformation intoEscherichia coliBL21(DE3), the fusion proteins were observed to appear at ~26.0 and 25.2 kDa after induction from 1 mmol/l isopropyl-beta-D-thiogalactopyronoside (IPTG). The results of sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and transmission electron microscopy (TEM) of an ultra-thin section revealed that the presence of signal peptide gave rise to the formation of an inclusion body located in the periplasmic space; however, the absence of signal peptide greatly enhanced the solubility of the target protein. The expressed soluble protein was further purified by Ni2+-NTA affinity chromatography and gel filtration methods.

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23

Dang, Xiangli, and Guangshun Wang. "Spotlight on the Selected New Antimicrobial Innate Immune Peptides Discovered During 2015-2019." Current Topics in Medicinal Chemistry 20, no. 32 (December 3, 2020): 2984–98. http://dx.doi.org/10.2174/1568026620666201022143625.

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Background: Antibiotic resistance is a global issue and new anti-microbials are required. Introduction: Anti-microbial peptides are important players of host innate immune systems that prevent infections. Due to their ability to eliminate drug-resistant pathogens, AMPs are promising candidates for developing the next generation of anti-microbials. Methods: The anti-microbial peptide database provides a useful tool for searching, predicting, and designing new AMPs. In the period from 2015-2019, ~500 new natural peptides have been registered. Results: This article highlights a select set of new AMP members with interesting properties. Teixobactin is a cell wall inhibiting peptide antibiotic, while darobactin inhibits a chaperone and translocator for outer membrane proteins. Remarkably, cOB1, a sex pheromone from commensal enterococci, restricts the growth of multidrug-resistant Enterococcus faecalis in the gut at a picomolar concentration. A novel proline-rich AMP has been found in a plant Brassica napus. A shrimp peptide MjPen-II comprises three different sequence domains: serine-rich, proline-rich, and cysteine-rich regions. Surprisingly, an amphibian peptide urumin specifically inhibits H1 hemagglutinin-bearing influenza A virus. Defensins are abundant and typically consist of three pairs of intramolecular disulfide bonds. However, rat rattusin dimerizes via forming five pairs of intermolecular disulfide bonds. While human LL-37 can be induced by vitamin D, vitamin A induces the expression of resistin-like molecule alpha (RELMα) in mice. The isolation and characterization of an alternative human cathelicidin peptide, TLN-58, substantiates the concept of one gene multiple peptides. The involvement of a fly AMP nemuri in sleep induction may promote the research on the relationship between sleep and infection control. Conclusion: The functional roles of AMPs continue to grow and the general term “innate immune peptides” becomes useful. These discoveries widen our view on antimicrobial peptides and may open new opportunities for developing novel peptide therapeutics for different applications.

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Oho, Takahiko, Floris J. Bikker, Arie V. Nieuw Amerongen, and Jasper Groenink. "A Peptide Domain of Bovine Milk Lactoferrin Inhibits the Interaction between Streptococcal Surface Protein Antigen and a Salivary Agglutinin Peptide Domain." Infection and Immunity 72, no. 10 (October 2004): 6181–84. http://dx.doi.org/10.1128/iai.72.10.6181-6184.2004.

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ABSTRACT The peptide domain of salivary agglutinin responsible for its interaction with cell surface protein antigen (PAc) of Streptococcus mutans or bovine lactoferrin was found in the same peptide, scavenger receptor cysteine-rich domain peptide 2 (SRCRP2). Inhibition studies suggest that PAc and lactoferrin, of which residues 480 to 492 seem important, competitively bind to the SRCRP2 domain of salivary agglutinin.

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McKIE, Norman, Donna J. DALLAS, Tracy EDWARDS, Jane F. APPERLEY, Graham G. RUSSELL, and Peter I. CROUCHER. "Cloning of a novel membrane-linked metalloproteinase from human myeloma cells." Biochemical Journal 318, no. 2 (September 1, 1996): 459–62. http://dx.doi.org/10.1042/bj3180459.

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We have isolated a novel cDNA from human myeloma cells encoding a member of the reprolysin family of metalloproteinases. Derived amino acid sequence predicts a protein of approx. 76 kDa. The open reading frame predicts the presence of a leader peptide, a pro-peptide with a ‘cysteine switch’, a metalloproteinase domain, a disintegrin-like domain, a cysteine-rich domain, an epidermal growth factor-like domain and a putative transmembrane sequence. Expression of the mRNA for this metalloproteinase has been demonstrated in human myeloma cells.

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Diamond, G., M. Zasloff, H. Eck, M. Brasseur, W. L. Maloy, and C. L. Bevins. "Tracheal antimicrobial peptide, a cysteine-rich peptide from mammalian tracheal mucosa: peptide isolation and cloning of a cDNA." Proceedings of the National Academy of Sciences 88, no. 9 (May 1, 1991): 3952–56. http://dx.doi.org/10.1073/pnas.88.9.3952.

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27

Lavergne, Vincent, Ivon Harliwong, Alun Jones, David Miller, Ryan J. Taft, and Paul F. Alewood. "Optimized deep-targeted proteotranscriptomic profiling reveals unexplored Conus toxin diversity and novel cysteine frameworks." Proceedings of the National Academy of Sciences 112, no. 29 (July 6, 2015): E3782—E3791. http://dx.doi.org/10.1073/pnas.1501334112.

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Cone snails are predatory marine gastropods characterized by a sophisticated venom apparatus responsible for the biosynthesis and delivery of complex mixtures of cysteine-rich toxin peptides. These conotoxins fold into small highly structured frameworks, allowing them to potently and selectively interact with heterologous ion channels and receptors. Approximately 2,000 toxins from an estimated number of >70,000 bioactive peptides have been identified in the genus Conus to date. Here, we describe a high-resolution interrogation of the transcriptomes (available at www.ddbj.nig.ac.jp) and proteomes of the diverse compartments of the Conus episcopatus venom apparatus. Using biochemical and bioinformatic tools, we found the highest number of conopeptides yet discovered in a single Conus specimen, with 3,305 novel precursor toxin sequences classified into 9 known superfamilies (A, I1, I2, M, O1, O2, S, T, Z), and identified 16 new superfamilies showing unique signal peptide signatures. We were also able to depict the largest population of venom peptides containing the pharmacologically active C-C-CC-C-C inhibitor cystine knot and CC-C-C motifs (168 and 44 toxins, respectively), as well as 208 new conotoxins displaying odd numbers of cysteine residues derived from known conotoxin motifs. Importantly, six novel cysteine-rich frameworks were revealed which may have novel pharmacology. Finally, analyses of codon usage bias and RNA-editing processes of the conotoxin transcripts demonstrate a specific conservation of the cysteine skeleton at the nucleic acid level and provide new insights about the origin of sequence hypervariablity in mature toxin regions.

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Chua, Victor M., Joanna Gajewiak, Maren Watkins, Samuel S. Espino, Iris Bea L. Ramiro, Carla A. Omaga, Julita S. Imperial, et al. "Purification and Characterization of the Pink-Floyd Drillipeptide, a Bioactive Venom Peptide from Clavus davidgilmouri (Gastropoda: Conoidea: Drilliidae)." Toxins 12, no. 8 (August 7, 2020): 508. http://dx.doi.org/10.3390/toxins12080508.

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The cone snails (family Conidae) are the best known and most intensively studied venomous marine gastropods. However, of the total biodiversity of venomous marine mollusks (superfamily Conoidea, >20,000 species), cone snails comprise a minor fraction. The venoms of the family Drilliidae, a highly diversified family in Conoidea, have not previously been investigated. In this report, we provide the first biochemical characterization of a component in a Drilliidae venom and define a gene superfamily of venom peptides. A bioactive peptide, cdg14a, was purified from the venom of Clavus davidgilmouri Fedosov and Puillandre, 2020. The peptide is small (23 amino acids), disulfide-rich (4 cysteine residues) and belongs to the J-like drillipeptide gene superfamily. Other members of this superfamily share a conserved signal sequence and the same arrangement of cysteine residues in their predicted mature peptide sequences. The cdg14a peptide was chemically synthesized in its bioactive form. It elicited scratching and hyperactivity, followed by a paw-thumping phenotype in mice. Using the Constellation Pharmacology platform, the cdg14a drillipeptide was shown to cause increased excitability in a majority of non-peptidergic nociceptors, but did not affect other subclasses of dorsal root ganglion (DRG) neurons. This suggests that the cdg14a drillipeptide may be blocking a specific molecular isoform of potassium channels. The potency and selectivity of this biochemically characterized drillipeptide suggest that the venoms of the Drilliidae are a rich source of novel and selective ligands for ion channels and other important signaling molecules in the nervous system.

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Coulon, Alexandre, Emir Berkane, Anne-Marie Sautereau, Konrad Urech, Pierre Rougé, and André Lopez. "Modes of membrane interaction of a natural cysteine-rich peptide: viscotoxin A3." Biochimica et Biophysica Acta (BBA) - Biomembranes 1559, no. 2 (February 2002): 145–59. http://dx.doi.org/10.1016/s0005-2736(01)00446-1.

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Astafieva, A. A., Eugene A. Rogozhin, Yaroslav A. Andreev, T. I. Odintsova, S. A. Kozlov, Eugene V. Grishin, and Tsezi A. Egorov. "A novel cysteine-rich antifungal peptide ToAMP4 from Taraxacum officinale Wigg. flowers." Plant Physiology and Biochemistry 70 (September 2013): 93–99. http://dx.doi.org/10.1016/j.plaphy.2013.05.022.

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Kato, Yusuke, and Setsuko Komatsu. "ASABF, a Novel Cysteine-rich Antibacterial Peptide Isolated from the NematodeAscaris suum." Journal of Biological Chemistry 271, no. 48 (November 29, 1996): 30493–98. http://dx.doi.org/10.1074/jbc.271.48.30493.

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Bortolini, Christian, Lei Liu, Zheshen Li, Karen Thomsen, Chen Wang, Flemming Besenbacher, and Mingdong Dong. "Peptide-Fibers: Identification of Cysteine-Rich Peptide-Fiber by Specific Cysteine-Au Nanoparticles Binding on Fiber Surface (Adv. Mater. Interfaces 9/2014)." Advanced Materials Interfaces 1, no. 9 (December 2014): n/a. http://dx.doi.org/10.1002/admi.201470055.

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Tiricz, Hilda, Attila Szűcs, Attila Farkas, Bernadett Pap, Rui M. Lima, Gergely Maróti, Éva Kondorosi, and Attila Kereszt. "Antimicrobial Nodule-Specific Cysteine-Rich Peptides Induce Membrane Depolarization-Associated Changes in the Transcriptome of Sinorhizobium meliloti." Applied and Environmental Microbiology 79, no. 21 (August 30, 2013): 6737–46. http://dx.doi.org/10.1128/aem.01791-13.

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ABSTRACTLeguminous plants establish symbiosis with nitrogen-fixing alpha- and betaproteobacteria, collectively called rhizobia, which provide combined nitrogen to support plant growth. Members of the inverted repeat-lacking clade of legumes impose terminal differentiation on their endosymbiotic bacterium partners with the help of the nodule-specific cysteine-rich (NCR) peptide family composed of close to 600 members. Among the few tested NCR peptides, cationic ones had antirhizobial activity measured by reduction or elimination of the CFU and uptake of the membrane-impermeable dye propidium iodide. Here, the antimicrobial spectrum of two of these peptides, NCR247 and NCR335, was investigated, and their effect on the transcriptome of the natural targetSinorhizobium melilotiwas characterized. Both peptides were able to kill quickly a wide range of Gram-negative and Gram-positive bacteria; however, their spectra were only partially overlapping, and differences were found also in their efficacy on given strains, indicating that the actions of NCR247 and NCR335 might be similar though not identical. Treatment ofS. meliloticultures with either peptide resulted in a quick downregulation of genes involved in basic cellular functions, such as transcription-translation and energy production, as well as upregulation of genes involved in stress and oxidative stress responses and membrane transport. Similar changes provoked mainly in Gram-positive bacteria by antimicrobial agents were coupled with the destruction of membrane potential, indicating that it might also be a common step in the bactericidal actions of NCR247 and NCR335.

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Jiang, Hongbing, Yidong Xu, Li Li, Leiyun Weng, Qiang Wang, Shijian Zhang, Baosen Jia, et al. "Inhibition of Influenza Virus Replication by Constrained Peptides Targeting Nucleoprotein." Antiviral Chemistry and Chemotherapy 22, no. 3 (December 2011): 119–30. http://dx.doi.org/10.3851/imp1902.

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Background: Because of high mutation rates, new drug-resistant viruses are rapidly evolving, thus making the necessary control of influenza virus infection difficult. Methods: We screened a constrained cysteine-rich peptide library mimicking μ-conotoxins from Conus geographus and a proline-rich peptide library mimicking lebocin 1 and 2 from Bombyx mori by using influenza virus RNA polymerase (PB1, PB2 and PA) and nucleoprotein (NP) as baits. Results: Among the 22 peptides selected from the libraries, we found that the NP-binding proline-rich peptide, PPWCCCSPMKRASPPPAQSDLPATPKCPP, inhibited influenza replicon activity to mean ±SD 40.7% ±15.8% when expressed as a GFP fusion peptide in replicon cells. Moreover, when the GFP fusion peptide was transduced into cells by an HIV-TAT protein transduction domain sequence, the replication of influenza virus A/WSN/33 (WSN) at a multiplicity of infection of 0.01 was inhibited to 20% and 69% at 12 and 24 h post-infection, respectively. In addition, the TAT-GFP fusion peptide was able to slightly protect Balb/c mice from WSN infection when administrated prior to the infection. Conclusions: These results suggest the potential of this peptide as the seed of an anti-influenza drug and reveal the usefulness of the constrained peptide strategy for generating inhibitors of influenza infection. The results also suggest that influenza NP, which is conserved among the influenza A viruses, is a good target for influenza inhibition, despite being the most abundant protein in infected cells.

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Horváth, Beatrix, Ágota Domonkos, Attila Kereszt, Attila Szűcs, Edit Ábrahám, Ferhan Ayaydin, Károly Bóka, et al. "Loss of the nodule-specific cysteine rich peptide, NCR169, abolishes symbiotic nitrogen fixation in the Medicago truncatula dnf7 mutant." Proceedings of the National Academy of Sciences 112, no. 49 (September 23, 2015): 15232–37. http://dx.doi.org/10.1073/pnas.1500777112.

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Host compatible rhizobia induce the formation of legume root nodules, symbiotic organs within which intracellular bacteria are present in plant-derived membrane compartments termed symbiosomes. In Medicago truncatula nodules, the Sinorhizobium microsymbionts undergo an irreversible differentiation process leading to the development of elongated polyploid noncultivable nitrogen fixing bacteroids that convert atmospheric dinitrogen into ammonia. This terminal differentiation is directed by the host plant and involves hundreds of nodule specific cysteine-rich peptides (NCRs). Except for certain in vitro activities of cationic peptides, the functional roles of individual NCR peptides in planta are not known. In this study, we demonstrate that the inability of M. truncatula dnf7 mutants to fix nitrogen is due to inactivation of a single NCR peptide, NCR169. In the absence of NCR169, bacterial differentiation was impaired and was associated with early senescence of the symbiotic cells. Introduction of the NCR169 gene into the dnf7-2/NCR169 deletion mutant restored symbiotic nitrogen fixation. Replacement of any of the cysteine residues in the NCR169 peptide with serine rendered it incapable of complementation, demonstrating an absolute requirement for all cysteines in planta. NCR169 was induced in the cell layers in which bacteroid elongation was most pronounced, and high expression persisted throughout the nitrogen-fixing nodule zone. Our results provide evidence for an essential role of NCR169 in the differentiation and persistence of nitrogen fixing bacteroids in M. truncatula.

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Velivelli, Siva L. S., Kirk J. Czymmek, Hui Li, Jared B. Shaw, Garry W. Buchko, and Dilip M. Shah. "Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection." Proceedings of the National Academy of Sciences 117, no. 27 (June 22, 2020): 16043–54. http://dx.doi.org/10.1073/pnas.2003526117.

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In the indeterminate nodules of a model legumeMedicago truncatula, ∼700 nodule-specific cysteine-rich (NCR) peptides with conserved cysteine signature are expressed. NCR peptides are highly diverse in sequence, and some of these cationic peptides exhibit antimicrobial activity in vitro and in vivo. However, there is a lack of knowledge regarding their structural architecture, antifungal activity, and modes of action against plant fungal pathogens. Here, the three-dimensional NMR structure of the 36-amino acid NCR044 peptide was solved. This unique structure was largely disordered and highly dynamic with one four-residue α-helix and one three-residue antiparallel β-sheet stabilized by two disulfide bonds. NCR044 peptide also exhibited potent fungicidal activity against multiple plant fungal pathogens, includingBotrytis cinereaand threeFusariumspp. It inhibited germination in quiescent spores ofB. cinerea. In germlings, it breached the fungal plasma membrane and induced reactive oxygen species. It bound to multiple bioactive phosphoinositides in vitro. Time-lapse confocal and superresolution microscopy revealed strong fungal cell wall binding, penetration of the cell membrane at discrete foci, followed by gradual loss of turgor, subsequent accumulation in the cytoplasm, and elevated levels in nucleoli of germlings. Spray-applied NCR044 significantly reduced gray mold disease symptoms caused by the fungal pathogenB. cinereain tomato and tobacco plants, and postharvest products. Our work illustrates the antifungal activity of a structurally unique NCR peptide against plant fungal pathogens and paves the way for future development of this class of peptides as a spray-on fungistat/fungicide.

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Guyonnet Duperat, V., J. P. Audie, V. Debailleul, A. Laine, M. P. Buisine, S. Galiegue-Zouitina, P. Pigny, P. Degand, J. P. Aubert, and N. Porchet. "Characterization of the human mucin gene MUC5AC: a consensus cysteine-rich domain for 11p15 mucin genes?" Biochemical Journal 305, no. 1 (January 1, 1995): 211–19. http://dx.doi.org/10.1042/bj3050211.

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To date five human mucin cDNAs (MUC2, 5A, 5B, 5C and 6) mapped to 11p15.3-15.5, so it appears that this chromosome region might contain several distinct gene loci for mucins. Three of these cDNAs, MUC5A, B and C, were cloned in our laboratory and previously published. A common number, 5, was recommended by the Human Gene Mapping Nomenclature Committee to designate them because of their common provenance from human tracheobronchial mucosa. In order to define whether they are products of the same gene locus or distinct loci, we describe in this paper physical mapping of these cDNAs using the strategy of analysis of CpG islands by pulse-field gel electrophoresis. The data suggest that MUC5A and MUC5C are part of the same gene (called MUC5AC) which is distinct from MUC5B. In the second part of this work, complete sequences of the inserts corresponding to previously described (JER47, JER58) and novel (JER62, JUL32, MAR2, MAR10 and MAR11) cDNAs of the so-called MUC5AC gene are presented and analysed. The data show that in this mucin gene, the tandem repeat domain is interrupted several times with a subdomain encoding a 130 amino acid cysteine-rich peptide in which the TR3A and TR3B peptides previously isolated by Rose et al. [Rose, Kaufman and Martin (1989) J. Biol. Chem., 264, 8193-8199] from airway mucins are found. A consensus peptide sequence for these subdomains involving invariant positions of most of the cysteines is proposed. The consensus nucleotide sequence of this subdomain is also found in the MUC2 gene and in the MUC5B gene, two other mucin genes mapped to 11p15. The functional significance for secreted mucins of these cysteine-rich subdomains and the modular organization of mucin peptides are discussed.

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Rey-Campos, Magalí, Beatriz Novoa, Alberto Pallavicini, Marco Gerdol, and Antonio Figueras. "Comparative Genomics Reveals a Significant Sequence Variability of Myticin Genes in Mytilus galloprovincialis." Biomolecules 10, no. 6 (June 22, 2020): 943. http://dx.doi.org/10.3390/biom10060943.

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Myticins are cysteine-rich antimicrobial peptides highly expressed in hemocytes of Mytilus galloprovincialis. Along with other antimicrobial peptides (AMPs), myticins are potent effectors in the mussel immune response to pathogenic infections. As intertidal filter-feeders, mussels are constantly exposed to mutable environmental conditions, as well as to the presence of many pathogens, and myticins may be key players in the great ability of these organisms to withstand these conditions. These AMPs are known to be characterized by a remarkable sequence diversity, which was further explored in this work, thanks to the analysis of the recently released genome sequencing data from 16 specimens. Altogether, we collected 120 different sequence variants, evidencing the important impact of presence/absence variation and positive selection in shaping the repertoire of myticin genes of each individual. From a functional point of view, both the isoelectric point (pI) and the predicted charge of the mature peptide show unusually low values compared with other cysteine-rich AMPs, reinforcing previous observations that myticins may have accessory functions not directly linked with microbe killing. Finally, we report the presence of highly conserved regulatory elements in the promoter region of myticin genes, which might explain their strong hemocyte-specific expression.

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Zheng, Lin, Yi-da Yang, Guo-cai Lu, and Maria S. Salvato. "Extracellular HIV Tat and Tat cysteine rich peptide increase CCR5 expression in monocytes." Journal of Zhejiang University SCIENCE 6B, no. 7 (July 2005): 668–72. http://dx.doi.org/10.1631/jzus.2005.b0668.

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Potocki, Slawomir, Magdalena Rowinska-Zyrek, Daniela Valensin, Karolina Krzywoszynska, Danuta Witkowska, Marek Luczkowski, and Henryk Kozlowski. "Metal Binding Ability of Cysteine-Rich Peptide Domain of ZIP13 Zn2+Ions Transporter." Inorganic Chemistry 50, no. 13 (July 4, 2011): 6135–45. http://dx.doi.org/10.1021/ic200270p.

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Juskowiak, Gary L., Christopher J. McGee, John Greaves, and David L. Van Vranken. "Synthesis, Screening, and Sequencing of Cysteine-Rich One-Bead One-Compound Peptide Libraries." Journal of Combinatorial Chemistry 10, no. 5 (September 8, 2008): 726–31. http://dx.doi.org/10.1021/cc800087y.

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Mandard, Nicolas, Philippe Bulet, Anita Caille, Sirlei Daffre, and Françoise Vovelle. "The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider." European Journal of Biochemistry 269, no. 4 (February 15, 2002): 1190–98. http://dx.doi.org/10.1046/j.0014-2956.2002.02760.x.

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Washburn, Catherine A., Allan L. Bieber, Kemmons A. Tubbs, and Douglas E. Chandler. "Mammalian Sperm Chemotaxis Is Elicited by Peptide Mimics of Cysteine Rich Secretory Proteins." Biology of Reproduction 85, Suppl_1 (July 1, 2011): 534. http://dx.doi.org/10.1093/biolreprod/85.s1.534.

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Zimmerman, C. U., and R. Herrmann. "Synthesis of a small, cysteine-rich, 29 amino acids long peptide inMycoplasma pneumoniae." FEMS Microbiology Letters 253, no. 2 (December 2005): 315–21. http://dx.doi.org/10.1016/j.femsle.2005.09.054.

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Dalas, E., A. Chalias, D. Gatos, and K. Barlos. "The inhibition of calcium carbonate crystal growth by the cysteine-rich Mdm2 peptide." Journal of Colloid and Interface Science 300, no. 2 (August 2006): 536–42. http://dx.doi.org/10.1016/j.jcis.2006.04.003.

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Durkin, M. E., S. Chakravarti, B. B. Bartos, S. H. Liu, R. L. Friedman, and A. E. Chung. "Amino acid sequence and domain structure of entactin. Homology with epidermal growth factor precursor and low density lipoprotein receptor." Journal of Cell Biology 107, no. 6 (December 1, 1988): 2749–56. http://dx.doi.org/10.1083/jcb.107.6.2749.

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Entactin (nidogen), a 150-kD sulfated glycoprotein, is a major component of basement membranes and forms a highly stable noncovalent complex with laminin. The complete amino acid sequence of mouse entactin has been derived from sequencing of cDNA clones. The 5.9-kb cDNA contains a 3,735-bp open reading frame followed by a 3'-untranslated region of 2.2 kb. The open reading frame encodes a 1,245-residue polypeptide with an unglycosylated Mr of 136,500, a 28-residue signal peptide, two Asn-linked glycosylation sites, and two potential Ca2+-binding sites. Analysis of the deduced amino acid sequence predicts that the molecule consists of two globular domains of 70 and 36 kD separated by a cysteine-rich domain of 28 kD. The COOH-terminal globular domain shows homology to the EGF precursor and the low density lipoprotein receptor. Entactin contains six EGF-type cysteine-rich repeat units and one copy of a cysteine-repeat motif found in thyroglobulin. The Arg-Gly-Asp cell recognition sequence is present in one of the EGF-type repeats, and a synthetic peptide from the putative cell-binding site of entactin was found to promote the attachment of mouse mammary tumor cells.

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Hansen, Ida K. Ø., Johan Isaksson, Aaron G. Poth, Kine Ø. Hansen, Aaron J. C. Andersen, Céline S. M. Richard, Hans-Matti Blencke, Klara Stensvåg, David J. Craik, and Tor Haug. "Isolation and Characterization of Antimicrobial Peptides with Unusual Disulfide Connectivity from the Colonial Ascidian Synoicum turgens." Marine Drugs 18, no. 1 (January 12, 2020): 51. http://dx.doi.org/10.3390/md18010051.

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This study reports the isolation of two novel cysteine-rich antibacterial peptides, turgencin A and turgencin B, along with their oxidized derivatives, from the Arctic marine colonial ascidian Synoicum turgens. The peptides are post-translationally modified, containing six cysteines with an unusual disulfide connectivity of Cys1-Cys6, Cys2-Cys5, and Cys3-Cys4 and an amidated C-terminus. Furthermore, the peptides contain methionine residues resulting in the isolation of peptides with different degrees of oxidation. The most potent peptide, turgencin AMox1 with one oxidized methionine, displayed antimicrobial activity against both Gram-negative and Gram-positive bacteria with a minimum inhibitory concentration (MIC) as low as 0.4 µM against selected bacterial strains. In addition, the peptide inhibited the growth of the melanoma cancer cell line A2058 (IC50 = 1.4 µM) and the human fibroblast cell line MRC-5 (IC50 = 4.8 µM). The results from this study show that natural peptides isolated from marine tunicates have the potential to be promising drug leads.

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Yamaguchi, Yusuke, Takanori Moriki, Hideo Wada, Masanori Matsumoto, Yoshihiro Fujimura, Terumichi Nakagawa, Atsuko Igari, Yasuo Ikeda, and Mitsuru Murata. "Identification of ADAMTS13 Peptide Sequences Recognized by Autoantibodies in Patients with Acquired Thrombotic Thrombocytopenic Purpura." Blood 112, no. 11 (November 16, 2008): 2286. http://dx.doi.org/10.1182/blood.v112.11.2286.2286.

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Abstract Anti-ADAMTS13 autoantibodies are considered to play pivotal roles in the pathophysiology of acquired thrombotic thrombocytopenic purpura (TTP). They inhibit the ADAMTS13 function resulting in the appearance of ultra-large von Willebrand factor (VWF) multimers. Major binding sites of the autoantibodies were reported to be in the cysteine-rich/spacer domains. To clarify the precise peptide sequences recognized by anti-ADAMTS13 IgG autoantibodies, we constructed a random cDNA fragment library expressing various peptides of ADAMTS13 on the surface of lambda phage and screened the library using purified IgG from 13 TTP patients. Diverse peptide sequences were obtained from almost entire ADAMTS13 domains such as metalloprotease, disintegrin, TSP1-1, cysteine-rich, spacer, TSP1- 2, 3, 4, 5, 7, 8 and CUB1. In particular, we detected an identical 26 amino-acid epitope sequence in the C-terminus of spacer domain from Gly662 to Val687 (sp662–687) shared by 5 TTP patients. Moreover, the peptide sequence was exactly included in one of the VWF binding epitope sites that we previously determined (Blood110 (11), 795a, 2007). We then assessed the impact of specific autoantibody to ADAMTS13 activity measured by FRETS-VWF73 or EIA and ADAMTS13 inhibitor titer in each of TTP patient plasma. However, both of the ADAMTS13 activity and inhibitor titer seemed not correlated with the existence of specific sp662–687 IgG autoantibody. These observations suggest that the autoantibody to sp662–687 may be one specific feature of TTP, although other epitopes are also involved in the pathogenesis of the disorder.

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Haag, Andreas F., Bernhard Kerscher, Sergio Dall'Angelo, Monica Sani, Renato Longhi, Mikhail Baloban, Heather M. Wilson, Peter Mergaert, Matteo Zanda, and Gail P. Ferguson. "Role of Cysteine Residues and Disulfide Bonds in the Activity of a Legume Root Nodule-specific, Cysteine-rich Peptide." Journal of Biological Chemistry 287, no. 14 (February 17, 2012): 10791–98. http://dx.doi.org/10.1074/jbc.m111.311316.

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Taylor, Karen, Bryan McCullough, David J. Clarke, Ross J. Langley, Tali Pechenick, Adrian Hill, Dominic J. Campopiano, Perdita E. Barran, Julia R. Dorin, and John R. W. Govan. "Covalent Dimer Species of β-Defensin Defr1 Display Potent Antimicrobial Activity against Multidrug-Resistant Bacterial Pathogens." Antimicrobial Agents and Chemotherapy 51, no. 5 (March 12, 2007): 1719–24. http://dx.doi.org/10.1128/aac.01531-06.

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ABSTRACT Beta defensins comprise a family of cationic, cysteine-rich antimicrobial peptides, predominantly expressed at epithelial surfaces. Previously we identified a unique five-cysteine defensin-related peptide (Defr1) that, when synthesized, is a mixture of dimeric isoforms and exhibits potent antimicrobial activity against Escherichia coli and Pseudomonas aeruginosa. Here we report that Defr1 displays antimicrobial activity against an extended panel of multidrug-resistant nosocomial pathogens for which antimicrobial treatment is limited or nonexistent. Defr1 fractions were collected by high-pressure liquid chromatography and analyzed by gel electrophoresis and mass spectrometry. Antimicrobial activity was initially investigated with the type strain Pseudomonas aeruginosa PAO1. All fractions tested displayed equivalent, potent antimicrobial activity levels comparable with that of the unfractionated Defr1. However, use of an oxidized, monomeric six-cysteine analogue (Defr1 Y5C), or of reduced Defr1, gave diminished antimicrobial activity. These results suggest that the covalent dimer structure of Defr1 is crucial to antimicrobial activity; this hypothesis was confirmed by investigation of a synthetic one-cysteine variant (Defr1-1cys). This gave an activity profile similar to that of synthetic Defr1 but only in an oxidized, dimeric form. Thus, we have shown that covalent, dimeric molecules based on the Defr1 β-defensin sequence demonstrate antimicrobial activity even in the absence of the canonical cysteine motif.

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