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Journal articles on the topic 'Insect, protease, peptides'

Author: Grafiati
Published: 6 September 2023
Last updated: 31 July 2025

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1

COPLEY, S. Kathrin, M. Sheri ALM, A. David SCHOOLEY, and E. William COURCHESNE. "Expression, processing and secretion of a proteolytically-sensitive insect diuretic hormone by Saccharomyces cerevisiae requires the use of a yeast strain lacking genes encoding the Yap3 and Mkc7 endoproteases found in the secretory pathway." Biochemical Journal 330, no. 3 (1998): 1333–40. http://dx.doi.org/10.1042/bj3301333.

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A system is described for the heterologous expression of peptides in Saccharomyces cerevisiae. A synthetic gene encoding a precursor of the 41 amino acid Manduca sexta diuretic hormone (Mas-DH) was expressed at 0.8 mg/l purified peptide. A precursor of a mutant peptide of Mas-DH, Mas-DH[K22Q] was also expressed. The peptides were purified, then treated with peptidylglycine α-amidating enzyme to generate the α-amidated, mature, form of Mas-DH or Mas-DH[K22Q], which were biologically active. Successful expression of full-length Mas-DH+Gly depended upon the use of a protease-deficient yeast strai
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2

Deng, Yuping, James Gibbs, Igor Bačík, et al. "Assembly of MHC Class I Molecules with Biosynthesized Endoplasmic Reticulum-Targeted Peptides Is Inefficient in Insect Cells and Can Be Enhanced by Protease Inhibitors." Journal of Immunology 161, no. 4 (1998): 1677–85. http://dx.doi.org/10.4049/jimmunol.161.4.1677.

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Abstract To study the requirements for assembly of MHC class I molecules with antigenic peptides in the endoplasmic reticulum (ER), we studied Ag processing in insect cells. Insects lack a class I recognition system, and their cells therefore provide a “blank slate” for identifying the proteins that have evolved to facilitate assembly of class I molecules in vertebrate cells. H-2Kb heavy chain, mouse β2-microglobulin, and an ER-targeted version of a peptide corresponding to Ova257–264 were expressed in insect cells using recombinant vaccinia viruses. Cell surface expression of Kb-OVA257–264 co
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3

Liu, Huawei, Jiahui Xu, Luoling Wang, et al. "Serpin-1a and serpin-6 regulate the Toll pathway immune homeostasis by synergistically inhibiting the Spätzle-processing enzyme CLIP2 in silkworm, Bombyx mori." PLOS Pathogens 19, no. 10 (2023): e1011740. http://dx.doi.org/10.1371/journal.ppat.1011740.

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The Toll receptor signaling pathway is an important innate immune response of insects to pathogen infection; its extracellular signal transduction involves serine protease cascade activation. However, excessive or constitutive activation of the Toll pathway can be detrimental. Hence, the balance between activation and inhibition of the extracellular protease cascade must be tightly regulated to achieve favorable outcomes. Previous studies have shown that serpins—serine protease inhibitors—negatively regulate insect innate immunity by inhibiting extracellular protease cascade signaling. Althoug
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4

Caldas, C., A. Cherqui, A. Pereira, and N. Simões. "Purification and Characterization of an Extracellular Protease from Xenorhabdus nematophila Involved in Insect Immunosuppression." Applied and Environmental Microbiology 68, no. 3 (2002): 1297–304. http://dx.doi.org/10.1128/aem.68.3.1297-1304.2002.

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ABSTRACT Xenorhabdus nematophila, a bacterium pathogenic for insects associated with the nematode Steinernema carpocapsae, releases high quantities of proteases, which may participate in the virulence against insects. Zymogram assays and cross-reactions of antibodies suggested that two distinct proteases were present. The major one, protease II, was purified and shown to have a molecular mass of 60 kDa and an estimated isoelectric point of 8.5. Protease II digested the chromogenic substrate N-tosyl-Gly-Pro-Arg-paranitroanilide (pNA) with V max and Km values of 0.0551 μM/min and 234 μM, respect
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5

Pfrepper, Klaus-Ingmar, Hans-Richard Rackwitz, Martina Schnölzer, Hans Heid, Martin Löchelt, and Rolf M. Flügel. "Molecular Characterization of Proteolytic Processing of the Pol Proteins of Human Foamy Virus Reveals Novel Features of the Viral Protease." Journal of Virology 72, no. 9 (1998): 7648–52. http://dx.doi.org/10.1128/jvi.72.9.7648-7652.1998.

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ABSTRACT Spumaviruses, or foamy viruses, express a pol-specific transcript that codes for a Pol polyprotein that consists of the protease, reverse transcriptase, ribonuclease H, and the integrase domains. To delineate the proteolytic cleavage sites between the Pol subdomains, recombinant human foamy virus (HFV) Pol proteins were expressed, purified by affinity chromatography, and subjected to either HFV protease assays or autocatalytic processing. In control experiments, HFV protease-deficient mutant proteins in which the active site Asp was replaced by an Ala residue were used to rule out uns
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6

Lin, Ying-Chuan, Zachary Beck, Taekyu Lee, et al. "Alteration of Substrate and Inhibitor Specificity of Feline Immunodeficiency Virus Protease." Journal of Virology 74, no. 10 (2000): 4710–20. http://dx.doi.org/10.1128/jvi.74.10.4710-4720.2000.

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ABSTRACT Feline immunodeficiency virus (FIV) protease is structurally very similar to human immunodeficiency virus (HIV) protease but exhibits distinct substrate and inhibitor specificities. We performed mutagenesis of subsite residues of FIV protease in order to define interactions that dictate this specificity. The I37V, N55M, M56I, V59I, and Q99V mutants yielded full activity. The I37V, N55M, V59I, and Q99V mutants showed a significant increase in activity against the HIV-1 reverse transcriptase/integrase and P2/nucleocapsid junction peptides compared with wild-type (wt) FIV protease. The I
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7

Pfrepper, Klaus-Ingmar, Martin Löchelt, Hans-Richard Rackwitz, Martina Schnölzer, Hans Heid, and Rolf M. Flügel. "Molecular Characterization of Proteolytic Processing of the Gag Proteins of Human Spumavirus." Journal of Virology 73, no. 9 (1999): 7907–11. http://dx.doi.org/10.1128/jvi.73.9.7907-7911.1999.

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ABSTRACT Spumaviruses, or foamy viruses, express Gag proteins that are incompletely processed by the viral protease in cell cultures. To delineate the proteolytic cleavage sites between potential Gag subdomains, recombinant human spumaretrovirus (HSRV) Gag proteins of different lengths were expressed, purified by affinity chromatography, and subjected to HSRV protease assays. HSRV-specific proteolytic cleavage products were isolated and characterized by Western blotting. Peptides spanning potential cleavage sites, as deduced from the sizes of the proteolytic cleavage products, were chemically
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8

SIMONET, Gert, Bert BREUGELMANS, Paul PROOST, et al. "Characterization of two novel pacifastin-like peptide precursor isoforms in the desert locust (Schistocerca gregaria): cDNA cloning, functional analysis and real-time RT-PCR gene expression studies." Biochemical Journal 388, no. 1 (2005): 281–89. http://dx.doi.org/10.1042/bj20041414.

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In the last decade, a new serine protease inhibitor family has been described in arthropods. Eight members of the family were purified from locusts and share a conserved cysteine array (Cys-Xaa9–12-Cys-Asn-Xaa-Cys-Xaa-Cys-Xaa2–3-Gly-Xaa3–6-Cys-Thr-Xaa3-Cys) with nine inhibitory domains of the light chain of the crayfish protease inhibitor, pacifastin (PLDs; pacifastin light chain domains). Using cDNA cloning, several pacifastin-related precursors have been identified, encoding additional PLD-related peptides in different insect species. In the present study, two isoforms of a novel pacifastin-
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9

Beck, Zachary Q., Ying-Chuan Lin, and John H. Elder. "Molecular Basis for the Relative Substrate Specificity of Human Immunodeficiency Virus Type 1 and Feline Immunodeficiency Virus Proteases." Journal of Virology 75, no. 19 (2001): 9458–69. http://dx.doi.org/10.1128/jvi.75.19.9458-9469.2001.

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ABSTRACT We have used a random hexamer phage library to delineate similarities and differences between the substrate specificities of human immunodeficiency virus type 1 (HIV-1) and feline immunodeficiency virus (FIV) proteases (PRs). Peptide sequences were identified that were specifically cleaved by each protease, as well as sequences cleaved equally well by both enzymes. Based on amino acid distinctions within the P3-P3′ region of substrates that appeared to correlate with these cleavage specificities, we prepared a series of synthetic peptides within the framework of a peptide sequence cle
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10

Zhang, T. T., G. C. Zhang, F. F. Zeng, C. Y. Liu, and J. J. Mao. "Insulin-like peptides regulate vitellogenesis and oviposition in the green lacewing, Chrysopa septempunctata." Bulletin of Entomological Research 107, no. 2 (2016): 148–54. http://dx.doi.org/10.1017/s0007485316000742.

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AbstractInsulin-like peptides (ILPs) act through a conserved insulin signaling pathway and play crucial roles in insect metabolism, growth, reproduction, and aging. Application of bovine insulin is able to increase vitellogenin (Vg) mRNA and protein levels in female insects. Here, we first show that injection of bovine insulin into previtellogenic Chrysopa septempunctata female adults promoted ovarian growth, increased Vg protein abundance, elevated reproductive performance, and enhanced protease activity. These data suggested that ILPs play crucial roles in reproductive regulation of the gree
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11

You, Liwen, Daniel Garwicz, and Thorsteinn Rögnvaldsson. "Comprehensive Bioinformatic Analysis of the Specificity of Human Immunodeficiency Virus Type 1 Protease." Journal of Virology 79, no. 19 (2005): 12477–86. http://dx.doi.org/10.1128/jvi.79.19.12477-12486.2005.

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ABSTRACT Rapidly developing viral resistance to licensed human immunodeficiency virus type 1 (HIV-1) protease inhibitors is an increasing problem in the treatment of HIV-infected individuals and AIDS patients. A rational design of more effective protease inhibitors and discovery of potential biological substrates for the HIV-1 protease require accurate models for protease cleavage specificity. In this study, several popular bioinformatic machine learning methods, including support vector machines and artificial neural networks, were used to analyze the specificity of the HIV-1 protease. A new,
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12

Ueno, Takamasa, Satoru Misawa, Yoichi Ohba, et al. "Isolation and Characterization of Monoclonal Antibodies That Inhibit Hepatitis C Virus NS3 Protease." Journal of Virology 74, no. 14 (2000): 6300–6308. http://dx.doi.org/10.1128/jvi.74.14.6300-6308.2000.

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ABSTRACT A series of mouse monoclonal antibodies (MAbs) to the nonstructural protein 3 (NS3) of hepatitis C virus was prepared. One of these MAbs, designated 8D4, was found to inhibit NS3 protease activity. This inhibition was competitive with respect to the substrate peptide (Ki = 39 nM) but was significantly decreased by the addition of the NS4A peptide, a coactivator of the NS3 protease. 8D4 also showed marked inhibition of the NS3-dependentcis processing of the NS3/4A polyprotein but had virtually no effect on the succeeding NS3/4A-dependent transprocessing of the NS5A/5B polyprotein in vi
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13

Shaikh, Faiyaz Khudaboddin, Sarwan W. Hamad, Saber W. Hamad, and Ashok A. Shinde. "In Vitro Screening of Seed Extracts of Medicinal Plants for Protease Inhibitory Activity." Cihan University-Erbil Scientific Journal 3, no. 1 (2019): 61–65. http://dx.doi.org/10.24086/cuesj.v3n1y2019.pp61-65.

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Protease inhibitors (PIs) are deployed in the plant kingdom as storage proteins or peptides, regulators of endogenous proteases, and plant protection agents against insect pests and pathogen attack. In humans, they are identified as chemopreventive agents against a range of cancers and have potential as drug to treat an array of disease associated with aberrant activity of proteases. The present investigation reports PIs activity data from 30 medicinal plants. The screening for PIs activity was done by dot blot assay using X-ray film coated with gelatin. Among screened seed extracts, Albizia l
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14

Oparin, Peter B., Konstantin S. Mineev, Yakov E. Dunaevsky, et al. "Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides." Biochemical Journal 446, no. 1 (2012): 69–77. http://dx.doi.org/10.1042/bj20120548.

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A new peptide trypsin inhibitor named BWI-2c was obtained from buckwheat (Fagopyrum esculentum) seeds by sequential affinity, ion exchange and reversed-phase chromatography. The peptide was sequenced and found to contain 41 amino acid residues, with four cysteine residues involved in two intramolecular disulfide bonds. Recombinant BWI-2c identical to the natural peptide was produced in Escherichia coli in a form of a cleavable fusion with thioredoxin. The 3D (three-dimensional) structure of the peptide in solution was determined by NMR spectroscopy, revealing two antiparallel α-helices stapled
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15

Robel, Ivonne, Julia Gebhardt, Jeroen R. Mesters, et al. "Functional Characterization of the Cleavage Specificity of the Sapovirus Chymotrypsin-Like Protease." Journal of Virology 82, no. 16 (2008): 8085–93. http://dx.doi.org/10.1128/jvi.00693-08.

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ABSTRACT Sapovirus is a positive-stranded RNA virus with a translational strategy based on processing of a polyprotein precursor by a chymotrypsin-like protease. So far, the molecular mechanisms regulating cleavage specificity of the viral protease are poorly understood. In this study, the catalytic activities and substrate specificities of the predicted forms of the viral protease, the 3C-like protease (NS6) and the 3CD-like protease-polymerase (NS6-7), were examined in vitro. The purified NS6 and NS6-7 were able to cleave synthetic peptides (15 to 17 residues) displaying the cleavage sites o
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16

Otvos, Laszlo, Krisztina Bokonyi, Istvan Varga, et al. "Insect peptides with improved protease-resistance protect mice against bacterial infection." Protein Science 9, no. 4 (2008): 742–49. http://dx.doi.org/10.1110/ps.9.4.742.

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17

Qie, Xingtao, Xizhong Yan, Wentao Wang, et al. "Serpin-4 Negatively Regulates Prophenoloxidase Activation and Antimicrobial Peptide Synthesis in the Silkworm, Bombyx mori." International Journal of Molecular Sciences 25, no. 1 (2023): 313. http://dx.doi.org/10.3390/ijms25010313.

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The prophenoloxidase (PPO) activation and Toll antimicrobial peptide synthesis pathways are two critical immune responses in the insect immune system. The activation of these pathways is mediated by the cascade of serine proteases, which is negatively regulated by serpins. In this study, we identified a typical serpin, BmSerpin-4, in silkworms, whose expression was dramatically up-regulated in the fat body and hemocytes after bacterial infections. The pre-injection of recombinant BmSerpin-4 remarkably decreased the antibacterial activity of the hemolymph and the expression of the antimicrobial
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18

Gallinari, Paola, Debra Brennan, Chiara Nardi, et al. "Multiple Enzymatic Activities Associated with Recombinant NS3 Protein of Hepatitis C Virus." Journal of Virology 72, no. 8 (1998): 6758–69. http://dx.doi.org/10.1128/jvi.72.8.6758-6769.1998.

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ABSTRACT The hepatitis C virus (HCV) nonstructural 3 protein (NS3) contains at least two domains associated with multiple enzymatic activities; a serine protease activity resides in the N-terminal one-third of the protein, whereas RNA helicase activity and RNA-stimulated nucleoside triphosphatase activity are associated with the C-terminal portion. To study the possible mutual influence of these enzymatic activities, a full-length NS3 polypeptide of 67 kDa was expressed as a nonfusion protein in Escherichia coli, purified to homogeneity, and shown to retain all three enzymatic activities. The
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19

Young, John K., Donghui Li, Matthew C. Abramowitz, and Trudy G. Morrison. "Interaction of Peptides with Sequences from the Newcastle Disease Virus Fusion Protein Heptad Repeat Regions." Journal of Virology 73, no. 7 (1999): 5945–56. http://dx.doi.org/10.1128/jvi.73.7.5945-5956.1999.

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ABSTRACT Typical of many viral fusion proteins, the sequence of the Newcastle disease virus (NDV) fusion protein has several heptad repeat regions. One, HR1, is located just carboxyl terminal to the fusion peptide, while the other, HR2, is located adjacent to the transmembrane domain. The structure and function of a synthetic peptide with a sequence from the region of the NDV HR1 region (amino acids 150 to 173) were characterized. The peptide inhibited fusion with a half-maximal concentration of approximately 2 μM; however, inhibition was observed only if the peptide was added prior to proteas
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20

Mitpuangchon, Natrada, Kwan Nualcharoen, Singtoe Boonrotpong, and Patamarerk Engsontia. "Identification of Novel Toxin Genes from the Stinging Nettle Caterpillar Parasa lepida (Cramer, 1799): Insights into the Evolution of Lepidoptera Toxins." Insects 12, no. 5 (2021): 396. http://dx.doi.org/10.3390/insects12050396.

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Many animal species can produce venom for defense, predation, and competition. The venom usually contains diverse peptide and protein toxins, including neurotoxins, proteolytic enzymes, protease inhibitors, and allergens. Some drugs for cancer, neurological disorders, and analgesics were developed based on animal toxin structures and functions. Several caterpillar species possess venoms that cause varying effects on humans both locally and systemically. However, toxins from only a few species have been investigated, limiting the full understanding of the Lepidoptera toxin diversity and evoluti
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21

Welch, Brett D., J. Nicholas Francis, Joseph S. Redman, et al. "Design of a Potent d-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to Resistance." Journal of Virology 84, no. 21 (2010): 11235–44. http://dx.doi.org/10.1128/jvi.01339-10.

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ABSTRACT The HIV gp41 N-trimer pocket region is an ideal viral target because it is extracellular, highly conserved, and essential for viral entry. Here, we report on the design of a pocket-specific d-peptide, PIE12-trimer, that is extraordinarily elusive to resistance and characterize its inhibitory and structural properties. d-Peptides (peptides composed of d-amino acids) are promising therapeutic agents due to their insensitivity to protease degradation. PIE12-trimer was designed using structure-guided mirror-image phage display and linker optimization and is the first d-peptide HIV entry i
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22

Krishnan, Manigandan, Joonhyeok Choi, Ahjin Jang, and Yangmee Kim. "A Novel Peptide Antibiotic, Pro10-1D, Designed from Insect Defensin Shows Antibacterial and Anti-Inflammatory Activities in Sepsis Models." International Journal of Molecular Sciences 21, no. 17 (2020): 6216. http://dx.doi.org/10.3390/ijms21176216.

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Owing to the challenges faced by conventional therapeutics, novel peptide antibiotics against multidrug-resistant (MDR) gram-negative bacteria need to be urgently developed. We had previously designed Pro9-3 and Pro9-3D from the defensin of beetle Protaetia brevitarsis; they showed high antimicrobial activity with cytotoxicity. Here, we aimed to develop peptide antibiotics with bacterial cell selectivity and potent antibacterial activity against gram-negative bacteria. We designed 10-meric peptides with increased cationicity by adding Arg to the N-terminus of Pro9-3 (Pro10-1) and its D-enantio
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23

Cabral, C. M., A. Cherqui, A. Pereira, and N. Simões. "Purification and Characterization of Two Distinct Metalloproteases Secreted by the Entomopathogenic Bacterium Photorhabdus sp. Strain Az29." Applied and Environmental Microbiology 70, no. 7 (2004): 3831–38. http://dx.doi.org/10.1128/aem.70.7.3831-3838.2004.

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ABSTRACT Photorhabdus sp. strain Az29 is symbiotic with an Azorean nematode of the genus Heterorhabditis in a complex that is highly virulent to insects even at low temperatures. The virulence of the bacteria is mainly attributed to toxins and bacterial enzymes secreted during parasitism. The bacteria secrete proteases during growth, with a peak at the end of the exponential growth phase. Protease secretion was higher in cultures growing at lower temperatures. At 10°C the activity was highest and remained constant for over 7 days, whereas at 23 and 28°C it showed a steady decrease. Two proteas
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24

Leni, G., L. Soetemans, J. Jacobs, et al. "Protein hydrolysates from Alphitobius diaperinus and Hermetia illucens larvae treated with commercial proteases." Journal of Insects as Food and Feed 6, no. 4 (2020): 393–404. http://dx.doi.org/10.3920/jiff2019.0037.

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Insect proteins have been proposed as a promising alternative for feed and food formulations. In the present work protease-assisted extraction was studied as a way to separate and extract proteins from two different insect species: Alphitobius diaperinus (AD) and Hermetia illucens (HI). The proteolytic activity of seven enzymes (papain, pancreatin, dispase I, pepsin, protease from Bacillus licheniformis, bromelain and trypsin) was evaluated determining the protein extraction yield, the degree of hydrolysis (DH) and the released free amino acids (FAA). Both insects represent an interesting sour
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25

Chabry, Joëlle, Suzette A. Priola, Kathy Wehrly, Jane Nishio, James Hope, and Bruce Chesebro. "Species-Independent Inhibition of Abnormal Prion Protein (PrP) Formation by a Peptide Containing a Conserved PrP Sequence." Journal of Virology 73, no. 8 (1999): 6245–50. http://dx.doi.org/10.1128/jvi.73.8.6245-6250.1999.

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ABSTRACT Conversion of the normal protease-sensitive prion protein (PrP) to its abnormal protease-resistant isoform (PrP-res) is a major feature of the pathogenesis associated with transmissible spongiform encephalopathy (TSE) diseases. In previous experiments, PrP conversion was inhibited by a peptide composed of hamster PrP residues 109 to 141, suggesting that this region of the PrP molecule plays a crucial role in the conversion process. In this study, we used PrP-res derived from animals infected with two different mouse scrapie strains and one hamster scrapie strain to investigate the spe
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26

Freimoser, Florian M., Steven Screen, Gang Hu, and Raymond St. Leger. "EST analysis of genes expressed by the zygomycete pathogen Conidiobolus coronatus during growth on insect cuticle." Microbiology 149, no. 7 (2003): 1893–900. http://dx.doi.org/10.1099/mic.0.26252-0.

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Conidiobolus coronatus (Zygomycota) is a facultative saprobe that is a pathogen of many insect species. Almost 2000 expressed sequence tag (EST) cDNA clones were sequenced to analyse gene expression during growth on insect cuticle. Sixty percent of the ESTs that could be clustered into functional groups (E⩽10−5) had their best blast hits among fungal sequences. These included chitinases and multiple subtilisins, trypsin, metalloprotease and aspartyl protease activities with the potential to degrade host tissues and disable anti-microbial peptides. Otherwise, compared to the ascomycete entomopa
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27

Stratov, Ivan, C. Jane Dale, Socheata Chea, James McCluskey, and Stephen J. Kent. "Induction of T-Cell Immunity to Antiretroviral Drug-Resistant Human Immunodeficiency Virus Type 1." Journal of Virology 79, no. 12 (2005): 7728–37. http://dx.doi.org/10.1128/jvi.79.12.7728-7737.2005.

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ABSTRACT Antiretroviral drug-resistant human immunodeficiency virus type 1 (HIV-1) is a major, growing, public health problem. Immune responses targeting epitopes spanning drug resistance sites could ameliorate development of drug resistance. We studied 25 individuals harboring multidrug-resistant HIV-1 for T-cell immunity to HIV-1 proteins and peptides spanning all common drug resistance mutations. CD8 T cells targeting epitopes spanning drug-induced mutations were detected but only in the 3 individuals with robust HIV-specific T-cell activity. Novel CD8 T-cell responses were detected against
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28

Vincent, Martin J., Angela J. Sanchez, Bobbie R. Erickson, et al. "Crimean-Congo Hemorrhagic Fever Virus Glycoprotein Proteolytic Processing by Subtilase SKI-1." Journal of Virology 77, no. 16 (2003): 8640–49. http://dx.doi.org/10.1128/jvi.77.16.8640-8649.2003.

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ABSTRACT Crimean-Congo hemorrhagic fever (CCHF) virus is a tick-borne member of the genus Nairovirus, family Bunyaviridae. The mature virus glycoproteins, Gn and Gc (previously referred to as G2 and G1), are generated by proteolytic cleavage from precursor proteins. The amino termini of Gn and Gc are immediately preceded by tetrapeptides RRLL and RKPL, respectively, leading to the hypothesis that SKI-1 or related proteases may be involved (A. J. Sanchez, M. J. Vincent, and S. T. Nichol, J. Virol. 76:7263-7275, 2002). In vitro peptide cleavage data show that an RRLL peptide representing the Gn
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29

St. Leger, Raymond J. "The role of cuticle-degrading proteases in fungal pathogenesis of insects." Canadian Journal of Botany 73, S1 (1995): 1119–25. http://dx.doi.org/10.1139/b95-367.

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The proteinaceous outer integument of insects forms an effective barrier against most microbes. Only the 700 known species of entomopathogenic fungi effect entry into their hosts by breaching the cuticle. There is accumulating evidence that the ability of fungi to degrade protein may aid their invasion of and growth in this orderly complex structure. Evidence for the particular importance of proteinases derives largely from studies of their production in infected cuticles associated with cuticle degradation, the effects of proteinase inhibitors on pathogen behavior, and by the analysis of prot
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30

Da Costa, Bruno, Stéphanie Soignier, Christophe Chevalier, et al. "Blotched Snakehead Virus Is a New Aquatic Birnavirus That Is Slightly More Related to Avibirnavirus Than to Aquabirnavirus." Journal of Virology 77, no. 1 (2003): 719–25. http://dx.doi.org/10.1128/jvi.77.1.719-725.2003.

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ABSTRACT By different approaches, we characterized the birnavirus blotched snakehead virus (BSNV). The sequence of genomic segment A revealed the presence of two open reading frames (ORFs): a large ORF with a 3,207-bp-long nucleotide sequence and a 417-nucleotide-long small ORF located within the N-terminal half of the large ORF, but in a different reading frame. The large ORF was found to encode a polyprotein cotranslationally processed by the viral protease VP4 to generate pVP2 (the VP2 precursor), a 71-amino-acid-long peptide ([X]), VP4, and VP3. The two cleavage sites at the [X]-VP4 and VP
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31

Gordon, M. M., T. Howard, M. J. Becich, and D. H. Alpers. "Cathepsin L mediates intracellular ileal digestion of gastric intrinsic factor." American Journal of Physiology-Gastrointestinal and Liver Physiology 268, no. 1 (1995): G33—G40. http://dx.doi.org/10.1152/ajpgi.1995.268.1.g33.

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Although acidic proteases of lysosomal origin are implicated in the degradation of intrinsic factor (IF) during cobalamin (cbl) transport across enterocytes and proximal renal tubule cell lines, the enzyme(s) involved in this process is not known. Recombinant (baculovirus-produced) rat 125I-labeled IF (125I-rIF), 43 kDa, added in vivo to the lumen of rat ileum was converted intracellularly to peptides of 33 and 26 kDa. In vitro rat 125I-rIF was degraded to peptides of 33 and 31 kDa by addition of cathepsin L; this conversion was fully inhibited by leupeptin. Western blot analysis using antiser
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32

Ujike, Makoto, Hiroki Nishikawa, Akira Otaka, et al. "Heptad Repeat-Derived Peptides Block Protease-Mediated Direct Entry from the Cell Surface of Severe Acute Respiratory Syndrome Coronavirus but Not Entry via the Endosomal Pathway." Journal of Virology 82, no. 1 (2007): 588–92. http://dx.doi.org/10.1128/jvi.01697-07.

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ABSTRACT The peptides derived from the heptad repeat (HRP) of severe acute respiratory syndrome coronavirus (SCoV) spike protein (sHRPs) are known to inhibit SCoV infection, yet their efficacies are fairly low. Recently our research showed that some proteases facilitated SCoV's direct entry from the cell surface, resulting in a more efficient infection than the previously known infection via endosomal entry. To compare the inhibitory effect of the sHRP in each pathway, we selected two sHRPs, which showed a strong inhibitory effect on the interaction of two heptad repeats in a rapid and virus-f
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SACRAMENTO, R. S., R. M. MARTINS, A. MIRANDA та ін. "Differential effects of α-helical and β-hairpin antimicrobial peptides against Acanthamoeba castellanii". Parasitology 136, № 8 (2009): 813–21. http://dx.doi.org/10.1017/s0031182009006283.

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SUMMARYIn this work we evaluated the ability of different types of antimicrobial peptides to promote permeabilization and growth inhibition of Acanthamoeba castellanii trophozoites, which cause eye keratitis. We used cationic α-helical peptides P5 and P6, corresponding to the N-terminus of the pore-forming protein from Triatoma infestans, a blood-sucking insect, and a β-hairpin amphipathic molecule (gomesin), of the spider Acanthoscurria gomesiana haemocytes. A. castellanii permeabilization was obtained after 1 h incubation with micromolar concentrations of both types of peptides. While permea
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Crim, Roberta L., Susette A. Audet, Steven A. Feldman, Howard S. Mostowski, and Judy A. Beeler. "Identification of Linear Heparin-Binding Peptides Derived from Human Respiratory Syncytial Virus Fusion Glycoprotein That Inhibit Infectivity." Journal of Virology 81, no. 1 (2006): 261–71. http://dx.doi.org/10.1128/jvi.01226-06.

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ABSTRACT It has been shown previously that the fusion glycoprotein of human respiratory syncytial virus (RSV-F) interacts with cellular heparan sulfate. Synthetic overlapping peptides derived from the F-protein sequence of RSV subtype A (strain A2) were tested for their ability to bind heparin using heparin-agarose affinity chromatography (HAAC). This evaluation identified 15 peptides representing eight linear heparin-binding domains (HBDs) located within F1 and F2 and spanning the protease cleavage activation site. All peptides bound to Vero and A549 cells, and binding was inhibited by solubl
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Mason, R. D., M. I. Bowmer, C. M. Howley, and M. D. Grant. "Cross-Reactive Cytotoxic T Lymphocytes against Human Immunodeficiency Virus Type 1 Protease and Gamma Interferon-Inducible Protein 30." Journal of Virology 79, no. 9 (2005): 5529–36. http://dx.doi.org/10.1128/jvi.79.9.5529-5536.2005.

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ABSTRACT The gamma interferon (IFN-γ)-inducible protein 30 (IP-30) signal peptide −11 to −3 (LLDVPTAAV) is a prominent self peptide expressed with the class I human histocompatibility leukocyte antigen A2 (HLA-A2). Stimulation of peripheral blood mononuclear cells (PBMC) from HLA-A2 human immunodeficiency virus type 1 (HIV-1)-infected individuals with an HLA-A2-restricted HIV protease (PR) peptide 76-84 (LVGPTPVNI) activated cytotoxic T lymphocytes (CTL) against the IP-30 signal peptide. Since HIV-1 PR 76-84 stimulated CD8+ T cells from these individuals to secrete IFN-γ, we tested whether the
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Nelson, Christian D. S., Eveliina Minkkinen, Magnus Bergkvist, et al. "Detecting Small Changes and Additional Peptides in the Canine Parvovirus Capsid Structure." Journal of Virology 82, no. 21 (2008): 10397–407. http://dx.doi.org/10.1128/jvi.00972-08.

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ABSTRACT Parvovirus capsids are assembled from multiple forms of a single protein and are quite stable structurally. However, in order to infect cells, conformational plasticity of the capsid is required and this likely involves the exposure of structures that are buried within the structural models. The presence of functional asymmetry in the otherwise icosahedral capsid has also been proposed. Here we examined the protein composition of canine parvovirus capsids and evaluated their structural variation and permeability by protease sensitivity, spectrofluorometry, and negative staining electr
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Prabu-Jeyabalan, Moses, Ellen A. Nalivaika, Nancy M. King, and Celia A. Schiffer. "Viability of a Drug-Resistant Human Immunodeficiency Virus Type 1 Protease Variant: Structural Insights for Better Antiviral Therapy." Journal of Virology 77, no. 2 (2003): 1306–15. http://dx.doi.org/10.1128/jvi.77.2.1306-1315.2003.

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ABSTRACT Under the selective pressure of protease inhibitor therapy, patients infected with human immunodeficiency virus (HIV) often develop drug-resistant HIV strains. One of the first drug-resistant mutations to arise in the protease, particularly in patients receiving indinavir or ritonavir treatment, is V82A, which compromises the binding of these and other inhibitors but allows the virus to remain viable. To probe this drug resistance, we solved the crystal structures of three natural substrates and two commercial drugs in complex with an inactive drug-resistant mutant (D25N/V82A) HIV-1 p
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Rahman, Khalidur, Mohd Amir F. Abdullah, Suresh Ambati, Milton D. Taylor, and Michael J. Adang. "Differential Protection of Cry1Fa Toxin against Spodoptera frugiperda Larval Gut Proteases by Cadherin Orthologs Correlates with Increased Synergism." Applied and Environmental Microbiology 78, no. 2 (2011): 354–62. http://dx.doi.org/10.1128/aem.06212-11.

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ABSTRACTThe Cry proteins produced byBacillus thuringiensis(Bt) are the most widely used biopesticides effective against a range of crop pests and disease vectors. Like chemical pesticides, development of resistance is the primary threat to the long-term efficacy of Bt toxins. Recently discovered cadherin-based Bt Cry synergists showed the potential to augment resistance management by improving efficacy of Cry toxins. However, the mode of action of Bt Cry synergists is thus far unclear. Here we elucidate the mechanism of cadherin-based Cry toxin synergism utilizing two cadherin peptides,Spodopt
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Kellenberger, Christine, Christian Boudier, Isabel Bermudez, Joseph G. Bieth, Bang Luu та Hélène Hietter. "Serine Protease Inhibition by Insect Peptides Containing a Cysteine Knot and a Triple-stranded β-Sheet". Journal of Biological Chemistry 270, № 43 (1995): 25514–19. http://dx.doi.org/10.1074/jbc.270.43.25514.

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Darsouei, Reyhaneh, Javad Karimi, and Gary B. Dunphy. "Functional Characterization of Outer Membrane Proteins (OMPs) in Xenorhabdus nematophila and Photorhabdus luminescens through Insect Immune Defense Reactions." Insects 10, no. 10 (2019): 352. http://dx.doi.org/10.3390/insects10100352.

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Xenorhabdus nematophila and Photorhabdus luminescens are entomopathogenic bacterial symbionts that produce toxic proteins that can interfere with the immune system of insects. Herein, we show that outer membrane proteins (OMPs) could be involved as bacterial virulence factors. Purified totals OMPs of both bacterial species were injected into fifth instar larvae of Spodoptera exigua Hübner. Larvae were surveyed for cellular defenses fluctuations in total haemocyte counts (THC) and granulocyte percentage and for the humoral defenses protease, phospholipase A2 (PLA2), and phenoloxidase (PO) activ
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Khan, Selina, Albert Zimmermann, Michael Basler, Marcus Groettrup, and Hartmut Hengel. "A Cytomegalovirus Inhibitor of Gamma Interferon Signaling Controls Immunoproteasome Induction." Journal of Virology 78, no. 4 (2004): 1831–42. http://dx.doi.org/10.1128/jvi.78.4.1831-1842.2004.

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ABSTRACT Both human and mouse cytomegaloviruses (HCMV and MCMV) avoid peptide presentation through the major histocompatibility complex (MHC) class I pathway to CD8+ T cells. Within the MHC class I pathway, the vast majority of antigenic peptides are generated by the proteasome system, a multicatalytic protease complex consisting of constitutive subunits, three of which can be replaced by enzymatically active gamma interferon (IFN-γ)-inducible subunits, i.e., LMP2, LMP7, and MECL1, to form the so-called immunoproteasomes. Here, we show that steady-state levels of immunoproteasomes are readily
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42

Maroto, Beatriz, Juan C. Ramı́rez, and José M. Almendral. "Phosphorylation Status of the Parvovirus Minute Virus of Mice Particle: Mapping and Biological Relevance of the Major Phosphorylation Sites." Journal of Virology 74, no. 23 (2000): 10892–902. http://dx.doi.org/10.1128/jvi.74.23.10892-10902.2000.

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ABSTRACT The core of the VP-1 and VP-2 proteins forming the T=1 icosahedral capsid of the prototype strain of the parvovirus minute virus of mice (MVMp) share amino acids sequence and a common three-dimensional structure; however, the roles of these polypeptides in the virus infection cycle differ. To gain insights into this paradox, the nature, distribution, and biological significance of MVMp particle phosphorylation was investigated. The VP-1 and VP-2 proteins isolated from purified empty capsids and from virions containing DNA harbored phosphoserine and phosphothreonine amino acids, which
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Merkulov, Gennady V., Joseph F. Lawler, Yolanda Eby, and Jef D. Boeke. "Ty1 Proteolytic Cleavage Sites Are Required for Transposition: All Sites Are Not Created Equal." Journal of Virology 75, no. 2 (2001): 638–44. http://dx.doi.org/10.1128/jvi.75.2.638-644.2001.

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ABSTRACT The retroviral protease is a key enzyme in a viral multienzyme complex that initiates an ordered sequence of events leading to virus assembly and propagation. Viral peptides are initially synthesized as polyprotein precursors; these precursors undergo a number of proteolytic cleavages executed by the protease in a specific and presumably ordered manner. To determine the role of individual protease cleavage sites in Ty1, a retrotransposon from Saccharomyces cerevisiae, the cleavage sites were systematically mutagenized. Altering the cleavage sites of the yeast Ty1 retrotransposon produ
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44

Fodor, Sharon K., and Volker M. Vogt. "Characterization of the Protease of a Fish Retrovirus, Walleye Dermal Sarcoma Virus." Journal of Virology 76, no. 9 (2002): 4341–49. http://dx.doi.org/10.1128/jvi.76.9.4341-4349.2002.

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ABSTRACT Three fish retroviruses infecting walleyes constitute the recently recognized genus called epsilonretrovirus. The founding member of this group, walleye dermal sarcoma virus (WDSV), induces benign skin tumors in the infected fish and replicates near 4°C. While the viral genomic sequence is known, biochemical characterization of the virus has been limited to the identification of the mature structural and envelope proteins present in virions. We undertook this study to determine the cleavage sites in the WDSV Pro and Pol proteins and to characterize the viral protease (PR) in vitro. A
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Zhang, R., J. Durkin, W. T. Windsor, C. McNemar, L. Ramanathan, and H. V. Le. "Probing the substrate specificity of hepatitis C virus NS3 serine protease by using synthetic peptides." Journal of virology 71, no. 8 (1997): 6208–13. http://dx.doi.org/10.1128/jvi.71.8.6208-6213.1997.

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46

Esram, Poornima, and Premkumar Arumugam. "Comprehensive Investigation of Recombinant Human TMPRSS4 Expression and Purification Across Diverse Expression Platforms: Bacterial, Insect (BVES), and Mammalian Systems." Journal of Advanced Zoology 44, no. 3 (2023): 232–46. http://dx.doi.org/10.17762/jaz.v44i3.583.

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TMPRSS4, an essential transmembrane protease serine 4, holds significant relevance in diverse biological contexts, making it a molecule of interest across various fields. This transmembrane serine protease, TMPRSS4, plays a pivotal role in multiple areas, including cancer research, disease processes, and potentially in the spread of viral infections. In light of its multifaceted significance, the research and production of active TMPRSS4 protein serve as a critical foundation for in-depth structural and functional studies, ultimately leading to the identification of potential inhibitors. Withi
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47

Lindemann, Dirk, Thomas Pietschmann, Marcus Picard-Maureau, et al. "A Particle-Associated Glycoprotein Signal Peptide Essential for Virus Maturation and Infectivity." Journal of Virology 75, no. 13 (2001): 5762–71. http://dx.doi.org/10.1128/jvi.75.13.5762-5771.2001.

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ABSTRACT Signal peptides (SP) are key determinants for targeting glycoproteins to the secretory pathway. Here we describe the involvement in particle maturation as an additional function of a viral glycoprotein SP. The SP of foamy virus (FV) envelope glycoprotein is predicted to be unusually long. Using an SP-specific antiserum, we demonstrate that its proteolytic removal occurs posttranslationally by a cellular protease and that the major N-terminal cleavage product, gp18, is found in purified viral particles. Analysis of mutants in proposed signal peptidase cleavage positions and N-glycosyla
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48

Stączek, Sylwia, Agnieszka Zdybicka-Barabas, Iwona Wojda та ін. "Fungal α-1,3-Glucan as a New Pathogen-Associated Molecular Pattern in the Insect Model Host Galleria mellonella". Molecules 26, № 16 (2021): 5097. http://dx.doi.org/10.3390/molecules26165097.

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Recognition of pathogen-associated molecular patterns (PAMPs) by appropriate pattern recognition receptors (PRRs) is a key step in activating the host immune response. The role of a fungal PAMP is attributed to β-1,3-glucan. The role of α-1,3-glucan, another fungal cell wall polysaccharide, in modulating the host immune response is not clear. This work investigates the potential of α-1,3-glucan as a fungal PAMP by analyzing the humoral immune response of the greater wax moth Galleria mellonella to Aspergillus niger α-1,3-glucan. We demonstrated that 57-kDa and 61-kDa hemolymph proteins, identi
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Ray, L. Bryan. "How Flies Find Fungal Foes." Science's STKE 2007, no. 369 (2007): tw21. http://dx.doi.org/10.1126/stke.3692007tw21.

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Responses of the immune systems of plants and animals show what appears to be evidence of ancient attacks and counterattacks by pathogens and their hosts in the battle for survival. Drosophila have developed receptors that recognize constituents of bacterial cell walls and mount an immune response that causes proteolytic cleavage of the cytokine Spätzle. The Spätzle fragment then activates Toll receptors and leads to production of antimicrobial peptides. Gottar et al. explored the response of Drosophila to fungal infections and found a similar defense mechanism but also unveiled a second signa
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Cordingley, M. G., R. B. Register, P. L. Callahan, V. M. Garsky, and R. J. Colonno. "Cleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli." Journal of Virology 63, no. 12 (1989): 5037–45. http://dx.doi.org/10.1128/jvi.63.12.5037-5045.1989.

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