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Journal articles on the topic 'LptC protein'

Author: Grafiati

Published: 9 March 2023

Last updated: 31 July 2025

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1

Sperandeo, Paola, Fion K. Lau, Andrea Carpentieri, et al. "Functional Analysis of the Protein Machinery Required for Transport of Lipopolysaccharide to the Outer Membrane of Escherichia coli." Journal of Bacteriology 190, no. 13 (2008): 4460–69. http://dx.doi.org/10.1128/jb.00270-08.

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ABSTRACT Lipopolysaccharide (LPS) is an essential component of the outer membrane (OM) in most gram-negative bacteria, and its structure and biosynthetic pathway are well known. Nevertheless, the mechanisms of transport and assembly of this molecule at the cell surface are poorly understood. The inner membrane (IM) transport protein MsbA is responsible for flipping LPS across the IM. Additional components of the LPS transport machinery downstream of MsbA have been identified, including the OM protein complex LptD/LptE (formerly Imp/RlpB), the periplasmic LptA protein, the IM-associated cytopla

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2

Martorana, Alessandra M., Mattia Benedet, Elisa A. Maccagni, et al. "Functional Interaction between the Cytoplasmic ABC Protein LptB and the Inner Membrane LptC Protein, Components of the Lipopolysaccharide Transport Machinery in Escherichia coli." Journal of Bacteriology 198, no. 16 (2016): 2192–203. http://dx.doi.org/10.1128/jb.00329-16.

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ABSTRACTThe assembly of lipopolysaccharide (LPS) in the outer leaflet of the outer membrane (OM) requires the transenvelope Lpt (lipopolysaccharide transport) complex, made inEscherichia coliof seven essential proteins located in the inner membrane (IM) (LptBCFG), periplasm (LptA), and OM (LptDE). At the IM, LptBFG constitute an unusual ATP binding cassette (ABC) transporter, composed by the transmembrane LptFG proteins and the cytoplasmic LptB ATPase, which is thought to extract LPS from the IM and to provide the energy for its export across the periplasm to the cell surface. LptC is a small

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3

Ren, Yixin, Wenting Dong, Yan Li, et al. "The Prediction of LptA and LptC Protein–Protein Interactions and Virtual Screening for Potential Inhibitors." Molecules 29, no. 8 (2024): 1827. http://dx.doi.org/10.3390/molecules29081827.

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Antibiotic resistance in Gram-negative bacteria remains one of the most pressing challenges to global public health. Blocking the transportation of lipopolysaccharides (LPS), a crucial component of the outer membrane of Gram-negative bacteria, is considered a promising strategy for drug discovery. In the transportation process of LPS, two components of the LPS transport (Lpt) complex, LptA and LptC, are responsible for shuttling LPS across the periplasm to the outer membrane, highlighting their potential as targets for antibacterial drug development. In the current study, a protein–protein int

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Lin, Yu-Ling, Li-Yi Chen, Chia-Hung Chen, et al. "A Soybean Oil-Based Liposome-Polymer Transfection Complex as a Codelivery System for DNA and Subunit Vaccines." Journal of Nanomaterials 2012 (2012): 1–12. http://dx.doi.org/10.1155/2012/427306.

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Inexpensive liposome-polymer transfection complexes (LPTCs) were developed and used as for DNA or protein delivery. The particle sizes of the LPTCs were in the range of 212.2 to 312.1 nm, and the zetapotential was +38.7 mV. LPTCs condensed DNA and protected DNA from DNase I digestion and efficiently delivered LPTC/DNA complexes in Balb/3T3 cells. LPTCs also enhanced the cellular uptake of antigen in mouse macrophage cells and stimulated TNF-αrelease in naïve mice splenocytes, both indicating the potential of LPTCs as adjuvants for vaccines.In vivostudies were performed usingH. pylorirelative h

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5

Dai, Xiaowei, Min Yuan, Yu Lu, et al. "Identification of a Small Molecule That Inhibits the Interaction of LPS Transporters LptA and LptC." Antibiotics 11, no. 10 (2022): 1385. http://dx.doi.org/10.3390/antibiotics11101385.

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The need for novel antibiotics has become imperative with the increasing prevalence of antibiotic resistance in Gram-negative bacteria in clinics. Acting as a permeability barrier, lipopolysaccharide (LPS) protects Gram-negative bacteria against drugs. LPS is synthesized in cells and transported to the outer membrane (OM) via seven lipopolysaccharide transport (Lpt) proteins (LptA–LptG). Of these seven Lpt proteins, LptC interacts with LptA to transfer LPS from the inner membrane (IM) to the OM, and assembly is aided by LptD/LptE. This interaction among the Lpt proteins is important for the bi

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6

Hicks, Greg, and Zongchao Jia. "Structural Basis for the Lipopolysaccharide Export Activity of the Bacterial Lipopolysaccharide Transport System." International Journal of Molecular Sciences 19, no. 9 (2018): 2680. http://dx.doi.org/10.3390/ijms19092680.

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Gram-negative bacteria have a dense outer membrane (OM) coating of lipopolysaccharides, which is essential to their survival. This coating is assembled by the LPS (lipopolysaccharide) transport (Lpt) system, a coordinated seven-subunit protein complex that spans the cellular envelope. LPS transport is driven by an ATPase-dependent mechanism dubbed the “PEZ” model, whereby a continuous stream of LPS molecules is pushed from subunit to subunit. This review explores recent structural and functional findings that have elucidated the subunit-scale mechanisms of LPS transport, including the novel AB

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7

Xiang, Quanju, Haiyan Wang, Zhongshan Wang, Yizheng Zhang, and Changjiang Dong. "Characterization of lipopolysaccharide transport protein complex." Open Life Sciences 9, no. 2 (2014): 131–38. http://dx.doi.org/10.2478/s11535-013-0250-5.

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AbstractLipopolysaccharide (LPS) is an essential component of the outer membranes (OM) of most Gram-negative bacteria, which plays a crucial role in protection of the bacteria from toxic compounds and harsh conditions. The LPS is biosynthesized at the cytoplasmic side of inner membrane (IM), and then transported across the aqueous periplasmic compartment and assembled correctly at the outer membrane. This process is accomplished by seven LPS transport proteins (LptA-G), but the transport mechanism remains poorly understood. Here, we present findings by pull down assays in which the periplasmic

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8

Vetterli, Stefan U., Katja Zerbe, Maik Müller, et al. "Thanatin targets the intermembrane protein complex required for lipopolysaccharide transport inEscherichia coli." Science Advances 4, no. 11 (2018): eaau2634. http://dx.doi.org/10.1126/sciadv.aau2634.

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With the increasing resistance of many Gram-negative bacteria to existing classes of antibiotics, identifying new paradigms in antimicrobial discovery is an important research priority. Of special interest are the proteins required for the biogenesis of the asymmetric Gram-negative bacterial outer membrane (OM). Seven Lpt proteins (LptA to LptG) associate in most Gram-negative bacteria to form a macromolecular complex spanning the entire envelope, which transports lipopolysaccharide (LPS) molecules from their site of assembly at the inner membrane to the cell surface, powered by adenosine 5′-t

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Schultz, Kathryn M., and Candice S. Klug. "Characterization of and lipopolysaccharide binding to the E. coli LptC protein dimer." Protein Science 27, no. 2 (2017): 381–89. http://dx.doi.org/10.1002/pro.3322.

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10

Cina, Nicholas P., and Candice S. Klug. "Characterizing the interactions between the LPS transport protein LptC and the ABC transporter LptB2FG." Biophysical Journal 122, no. 3 (2023): 56a. http://dx.doi.org/10.1016/j.bpj.2022.11.511.

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11

Naclerio, George A., and Herman O. Sintim. "Multiple ways to kill bacteria via inhibiting novel cell wall or membrane targets." Future Medicinal Chemistry 12, no. 13 (2020): 1253–79. http://dx.doi.org/10.4155/fmc-2020-0046.

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The rise of antibiotic-resistant infections has been well documented and the need for novel antibiotics cannot be overemphasized. US FDA approved antibiotics target only a small fraction of bacterial cell wall or membrane components, well-validated antimicrobial targets. In this review, we highlight small molecules that inhibit relatively unexplored cell wall and membrane targets. Some of these targets include teichoic acids-related proteins (DltA, LtaS, TarG and TarO), lipid II, Mur family enzymes, components of LPS assembly (MsbA, LptA, LptB and LptD), penicillin-binding protein 2a in methic

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12

Lee, James, Mingyu Xue, Joseph S. Wzorek та ін. "Characterization of a stalled complex on the β-barrel assembly machine". Proceedings of the National Academy of Sciences 113, № 31 (2016): 8717–22. http://dx.doi.org/10.1073/pnas.1604100113.

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The assembly of β-barrel proteins into membranes is mediated by an evolutionarily conserved machine. This process is poorly understood because no stable partially folded barrel substrates have been characterized. Here, we slowed the folding of the Escherichia coli β-barrel protein, LptD, with its lipoprotein plug, LptE. We identified a late-stage intermediate in which LptD is folded around LptE, and both components interact with the two essential β-barrel assembly machine (Bam) components, BamA and BamD. We propose a model in which BamA and BamD act in concert to catalyze folding, with the fin

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13

Marchesini, María Inés, Ansgar Poetsch, Leticia Soledad Guidolín, and Diego J. Comerci. "Brucella abortus Encodes an Active Rhomboid Protease: Proteome Response after Rhomboid Gene Deletion." Microorganisms 10, no. 1 (2022): 114. http://dx.doi.org/10.3390/microorganisms10010114.

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Rhomboids are intramembrane serine proteases highly conserved in the three domains of life. Their key roles in eukaryotes are well understood but their contribution to bacterial physiology is still poorly characterized. Here we demonstrate that Brucella abortus, the etiological agent of the zoonosis called brucellosis, encodes an active rhomboid protease capable of cleaving model heterologous substrates like Drosophila melanogaster Gurken and Providencia stuartii TatA. To address the impact of rhomboid deletion on B. abortus physiology, the proteomes of mutant and parental strains were compare

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14

Tran, An X., Changjiang Dong, and Chris Whitfield. "Structure and Functional Analysis of LptC, a Conserved Membrane Protein Involved in the Lipopolysaccharide Export Pathway inEscherichia coli." Journal of Biological Chemistry 285, no. 43 (2010): 33529–39. http://dx.doi.org/10.1074/jbc.m110.144709.

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15

Tran, An X., Changjiang Dong, and Chris Whitfield. "Structure and functional analysis of LptC, a conserved membrane protein involved in the lipopolysaccharide export pathway inEscherichia coli." Journal of Biological Chemistry 292, no. 45 (2017): 18731. http://dx.doi.org/10.1074/jbc.aac117.000510.

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16

Botos, Istvan, Nicholas Noinaj, and Susan K. Buchanan. "Insertion of proteins and lipopolysaccharide into the bacterial outer membrane." Philosophical Transactions of the Royal Society B: Biological Sciences 372, no. 1726 (2017): 20160224. http://dx.doi.org/10.1098/rstb.2016.0224.

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The bacterial outer membrane contains phospholipids in the inner leaflet and lipopolysaccharide (LPS) in the outer leaflet. Both proteins and LPS must be frequently inserted into the outer membrane to preserve its integrity. The protein complex that inserts LPS into the outer membrane is called LptDE, and consists of an integral membrane protein, LptD, with a separate globular lipoprotein, LptE, inserted in the barrel lumen. The protein complex that inserts newly synthesized outer-membrane proteins (OMPs) into the outer membrane is called the BAM complex, and consists of an integral membrane p

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17

Sperandeo, Paola, Rachele Cescutti, Riccardo Villa, et al. "Characterization of lptA and lptB, Two Essential Genes Implicated in Lipopolysaccharide Transport to the Outer Membrane of Escherichia coli." Journal of Bacteriology 189, no. 1 (2006): 244–53. http://dx.doi.org/10.1128/jb.01126-06.

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ABSTRACT The outer membrane (OM) of gram-negative bacteria is an asymmetric lipid bilayer that protects the cell from toxic molecules. Lipopolysaccharide (LPS) is an essential component of the OM in most gram-negative bacteria, and its structure and biosynthesis are well known. Nevertheless, the mechanisms of transport and assembly of this molecule in the OM are poorly understood. To date, the only proteins implicated in LPS transport are MsbA, responsible for LPS flipping across the inner membrane, and the Imp/RlpB complex, involved in LPS targeting to the OM. Here, we present evidence that t

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18

Benedet, Mattia, Federica A. Falchi, Simone Puccio, et al. "The Lack of the Essential LptC Protein in the Trans-Envelope Lipopolysaccharide Transport Machine Is Circumvented by Suppressor Mutations in LptF, an Inner Membrane Component of the Escherichia coli Transporter." PLOS ONE 11, no. 8 (2016): e0161354. http://dx.doi.org/10.1371/journal.pone.0161354.

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19

Wenzel, Cory Q., Frank St. Michael, Jacek Stupak, Jianjun Li, Andrew D. Cox, and James C. Richards. "Functional Characterization of Lpt3 and Lpt6, the Inner-Core Lipooligosaccharide Phosphoethanolamine Transferases from Neisseria meningitidis." Journal of Bacteriology 192, no. 1 (2009): 208–16. http://dx.doi.org/10.1128/jb.00558-09.

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ABSTRACT The lipooligosaccharide (LOS) of Neisseria meningitidis contains heptose (Hep) residues that are modified with phosphoethanolamine (PEtn) at the 3 (3-PEtn) and/or 6 (6-PEtn) position. The lpt3 (NMB2010) and lpt6 (NMA0408) genes of N. meningitidis, which are proposed to encode the required HepII 3- and 6-PEtn transferases, respectively, were cloned and overexpressed as C-terminally polyhistidine-tagged fusion proteins in Escherichia coli and found to localize to the inner membrane, based on sucrose density gradient centrifugation. Lpt3-His6 and Lpt6-His6 were purified from Triton X-100

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20

Schultz, Kathryn M., and Candice S. Klug. "High-Pressure EPR Spectroscopy Studies of the E. coli Lipopolysaccharide Transport Proteins LptA and LptC." Applied Magnetic Resonance 48, no. 11-12 (2017): 1341–53. http://dx.doi.org/10.1007/s00723-017-0948-z.

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21

Hsueh, Yi-Ching, Eva-M. Brouwer, Julian Marzi, Oliver Mirus, and Enrico Schleiff. "Functional properties of LptA and LptD in Anabaena sp. PCC 7120." Biological Chemistry 396, no. 9-10 (2015): 1151–62. http://dx.doi.org/10.1515/hsz-2014-0322.

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Abstract Lipopolysaccharides (LPS) are central components of the outer membrane and consist of Lipid A, the core polysaccharide, and the O-antigen. The synthesis of LPS is initiated at the cytosolic face of the cytoplasmic membrane. The subsequent transport to and across the outer membrane involves multiple lipopolysaccharide transport (Lpt) proteins. Among those proteins, the periplasmic-localized LptA and the outer membrane-embedded LptD participate in the last steps of transfer and insertion of LPS into the outer membrane. While the process is described for proteobacterial model systems, no

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22

Svanberg Frisinger, Frida, Bimal Jana, Stefano Donadio, and Luca Guardabassi. "In silico Prediction and Prioritization of Novel Selective Antimicrobial Drug Targets in Escherichia coli." Antibiotics 10, no. 6 (2021): 632. http://dx.doi.org/10.3390/antibiotics10060632.

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Novel antimicrobials interfering with pathogen-specific targets can minimize the risk of perturbations of the gut microbiota (dysbiosis) during therapy. We employed an in silico approach to identify essential proteins in Escherichia coli that are either absent or have low sequence identity in seven beneficial taxa of the gut microbiota: Faecalibacterium, Prevotella, Ruminococcus, Bacteroides, Lactobacillus, Lachnospiraceae and Bifidobacterium. We identified 36 essential proteins that are present in hyper-virulent E. coli ST131 and have low similarity (bitscore < 50 or identity < 30% and

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23

Tusi, Solaleh Khoramian, Lien Nguyen, Kiruphagaran Thangaraju, et al. "The alternative initiation factor eIF2A plays key role in RAN translation of myotonic dystrophy type 2 CCUG•CAGG repeats." Human Molecular Genetics 30, no. 11 (2021): 1020–29. http://dx.doi.org/10.1093/hmg/ddab098.

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Abstract Repeat-associated non-ATG (RAN) proteins have been reported in 11 microsatellite expansion disorders but the factors that allow RAN translation to occur and the effects of different repeat motifs and alternative AUG-like initiation codons are unclear. We studied the mechanisms of RAN translation across myotonic dystrophy type 2 (DM2) expansion transcripts with (CCUG) or without (CAGG) efficient alternative AUG-like codons. To better understand how DM2 LPAC and QAGR RAN proteins are expressed, we generated a series of CRISPR/Cas9-edited HEK293T cell lines. We show that LPAC and QAGR RA

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Batistela, Emanuele, Mayara Peron Pereira, Juliany Torres Siqueira, et al. "Decreased rate of protein synthesis, caspase-3 activity, and ubiquitin–proteasome proteolysis in soleus muscles from growing rats fed a low-protein, high-carbohydrate diet." Canadian Journal of Physiology and Pharmacology 92, no. 6 (2014): 445–54. http://dx.doi.org/10.1139/cjpp-2013-0290.

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The aim of this study was to investigate the changes in the rates of both protein synthesis and breakdown, and the activation of intracellular effectors that control these processes in soleus muscles from growing rats fed a low-protein, high-carbohydrate (LPHC) diet for 15 days. The mass and the protein content, as well as the rate of protein synthesis, were decreased in the soleus from LPHC-fed rats. The availability of amino acids was diminished, since the levels of various essential amino acids were decreased in the plasma of LPHC-fed rats. Overall rate of proteolysis was also decreased, ex

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Damron, F. Heath, Jennifer Napper, M. Allison Teter, and Hongwei D. Yu. "Lipotoxin F of Pseudomonas aeruginosa is an AlgU-dependent and alginate-independent outer membrane protein involved in resistance to oxidative stress and adhesion to A549 human lung epithelia." Microbiology 155, no. 4 (2009): 1028–38. http://dx.doi.org/10.1099/mic.0.025833-0.

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Chronic lung infection with P. aeruginosa and excessive neutrophil-associated inflammation are major causes of morbidity and mortality in patients with cystic fibrosis (CF). Overproduction of an exopolysaccharide known as alginate leads to the formation of mucoid biofilms that are resistant to antibiotics and host defences. Alginate overproduction or mucoidy is controlled by a stress-related ECF sigma factor AlgU/T. Mutation in the anti-sigma factor MucA is a known mechanism for conversion to mucoidy. Recently, we showed that inactivation of a kinase (KinB) in nonmucoid strain PAO1 results in

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Wahl, Devin, David Raubenheimer, Rafael de Cabo, et al. "Comparing the Effects of Low-Protein and High-Carbohydrate Diets and Caloric Restriction on Brain Aging in Mice." Innovation in Aging 4, Supplement_1 (2020): 846. http://dx.doi.org/10.1093/geroni/igaa057.3103.

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Abstract The Geometric Framework for Nutrition (GFN) has revealed that ad-libitum low-protein, high-carbohydrate (LPHC) diets improve cardiometabolic health and extend lifespan in rodents, but it is not known whether these diets are also beneficial for brain health. Here, we utilized previous results from GFN studies and compared hippocampus biology and memory in mice subjected to 20% calorie restriction (CR) or provided ad-libitum access to several LPHC diets. RNA expression in the hippocampus of 15-month-old mice were similar between mice fed CR and LPHC diets. Nutrient-sensing proteins, inc

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Chang, Kai-Fu, Jinghua Tsai Chang, Xiao-Fan Huang, et al. "Antitumor Effects of N-Butylidenephthalide Encapsulated in Lipopolyplexs in Colorectal Cancer Cells." Molecules 25, no. 10 (2020): 2394. http://dx.doi.org/10.3390/molecules25102394.

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Colorectal cancer (CRC) is the third most common type of cancer and the second most common cause of cancer-related death in the world. N-Butylidenephthalide (BP), a natural compound, inhibits several cancers, such as hepatoma, brain tumor and colon cancer. However, due to the unstable structure, the activity of BP is quickly lost after dissolution in an aqueous solution. A polycationic liposomal polyethylenimine and polyethylene glycol complex (LPPC), a new drug carrier, encapsulates both hydrophobic and hydrophilic compounds, maintains the activity of the compound, and increases uptake of can

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O'Connor, Ellen T., Andrzej Piekarowicz, Karen V. Swanson, J. McLeod Griffiss, and Daniel C. Stein. "Biochemical Analysis of Lpt3, a Protein Responsible forPhosphoethanolamine Addition to Lipooligosaccharide ofPathogenic Neisseria." Journal of Bacteriology 188, no. 3 (2006): 1039–48. http://dx.doi.org/10.1128/jb.188.3.1039-1048.2006.

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ABSTRACT The inner core of neisserial lipooligosaccharide (LOS) contains heptose residues that can be decorated by phosphoethanolamine (PEA). PEA modification of heptose II (HepII) can occur at the 3, 6, or 7 position(s). We used a genomic DNA sequence of lpt3, derived from Neisseria meningitidis MC58, to search the genomic sequence of N. gonorrhoeae FA1090 and identified a homolog of lpt3 in N. gonorrhoeae. A PCR amplicon containing lpt3 was amplified from F62ΔLgtA, cloned, mutagenized, and inserted into the chromosome of N. gonorrhoeae strain F62ΔLgtA, producing strain F62ΔLgtAlpt3::Tn5. LOS

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Franco, Juliana Gastão, Egberto Gaspar de Moura, Josely Correa Koury, et al. "Resveratrol reduces lipid peroxidation and increases sirtuin 1 expression in adult animals programed by neonatal protein restriction." Journal of Endocrinology 207, no. 3 (2010): 319–28. http://dx.doi.org/10.1677/joe-10-0124.

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Resveratrol (Res) has been associated with protective effects against oxidative stress. This study evaluated the effect of Res over lipid peroxidation, antioxidant defense, hepatic sirtuin 1 (SIRT1), which up-regulates antioxidant enzymes, and copper/zinc superoxide dismutase (Cu/Zn SOD) in adult offspring whose mothers were protein restricted during lactation. Lactating Wistar rats were divided into control (C) group, which were fed a normal diet (23% protein), and low-protein and high-carbohydrate (LPHC) group, which were fed a diet containing 8% protein. After weaning (21 days), C and LPHC

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Pankov, Genady, Alice Dawson, and William N. Hunter. "The structure of lipopolysaccharide transport protein B (LptB) from Burkholderia pseudomallei." Acta Crystallographica Section F Structural Biology Communications 75, no. 4 (2019): 227–32. http://dx.doi.org/10.1107/s2053230x19001778.

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The thick outer membrane (OM) of Gram-negative bacteria performs an important protective role against hostile environments, supports cell integrity, and contributes to surface adhesion and in some cases also to virulence. A major component of the OM is lipopolysaccharide (LPS), a complex glycolipid attached to a core containing fatty-acyl chains. The assembly and transport of lipid A, the membrane anchor for LPS, to the OM begins when a heteromeric LptB2FG protein complex extracts lipid A from the outer leaflet of the inner membrane. This process requires energy, and upon hydrolysis of ATP one

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Malke, Horst. "Cytoplasmic Membrane Lipoprotein LppC ofStreptococcus equisimilis Functions as an Acid Phosphatase." Applied and Environmental Microbiology 64, no. 7 (1998): 2439–42. http://dx.doi.org/10.1128/aem.64.7.2439-2442.1998.

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ABSTRACT The function of the streptococcal cytoplasmic membrane lipoprotein, LppC, was identified with isogenic Streptococcus equisimilis H46A and Escherichia coli JM109 strain pairs differing in whether they contained [H46A and JM109(pLPP2)] or lacked (H46A lppC::pLPP10 and JM109) the functional lppC gene for comparative phosphatase determinations under acidic conditions. lppC-directed acid phosphatase activity was demonstrated zymographically and by specific enzymatic activity assays, with whole cells or cell membrane preparations as enzyme sources. LppC acid phosphatase showed optimum activ

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Navarro-Meza, Mónica, Mauricio Díaz-Muñoz, Perla Belén García-Solano, et al. "Effects of Low Protein-High Carbohydrate Diet during Early and Late Pregnancy on Respiratory Quotient and Visceral Adiposity." Oxidative Medicine and Cellular Longevity 2022 (April 7, 2022): 1–11. http://dx.doi.org/10.1155/2022/3878581.

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Background. Low Protein-High Carbohydrate (LPHC) diet during pregnancy is considered a nutritional and health problem related to the development of maternal metabolic alterations, such as fatty liver and obesity in the perinatal and postnatal period. It is known that increase in visceral adiposity tissue (VAT) modulates maternal metabolic rate, with the respiratory quotient (RQ) being a parameter related to that variable; however, it is unknown whether LPHC intake during pregnancy affects the VAT and the RQ. In this study, we examine if consumption of LPHC during pregnancy modifies the VAT and

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Daimon, Yasushi, Shin-ichiro Narita, Ryoji Miyazaki та ін. "Reversible autoinhibitory regulation ofEscherichia colimetallopeptidase BepA for selective β-barrel protein degradation". Proceedings of the National Academy of Sciences 117, № 45 (2020): 27989–96. http://dx.doi.org/10.1073/pnas.2010301117.

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Escherichia coliperiplasmic zinc-metallopeptidase BepA normally functions by promoting maturation of LptD, a β-barrel outer-membrane protein involved in biogenesis of lipopolysaccharides, but degrades it when its membrane assembly is hampered. These processes should be properly regulated to ensure normal biogenesis of LptD. The underlying mechanism of regulation, however, remains to be elucidated. A recently solved BepA structure has revealed unique features: In particular, the active site is buried in the protease domain and conceivably inaccessible for substrate degradation. Additionally, th

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Buzelle, Samyra L., Maísa P. Santos, Amanda M. Baviera, et al. "A low-protein, high-carbohydrate diet increases the adipose lipid content without increasing the glycerol-3-phosphate or fatty acid content in growing rats." Canadian Journal of Physiology and Pharmacology 88, no. 12 (2010): 1157–65. http://dx.doi.org/10.1139/y10-096.

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The amount of triacylglycerol (TAG) that accumulates in adipose tissue depends on 2 opposing processes: lipogenesis and lipolysis. We have previously shown that the weight and lipid content of epididymal (EPI) adipose tissue increases in growing rats fed a low-protein, high-carbohydrate (LPHC) diet for 15 days. The aim of this work was to study the pathways involved in lipogenesis and lipolysis, which ultimately regulate lipid accumulation in the tissue. De novo fatty acid synthesis was evaluated in vivo and was similar for rats fed an LPHC diet or a control diet; however, the LPHC-fed rats ha

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Pereira, Mayara P., Samyra L. Buzelle, Emanuele Batistela, et al. "High glucose uptake in growing rats adapted to a low-protein, high-carbohydrate diet determines low fasting glycemia even with high hepatic gluconeogenesis." Canadian Journal of Physiology and Pharmacology 92, no. 6 (2014): 460–66. http://dx.doi.org/10.1139/cjpp-2013-0346.

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The our objective was to investigate the adaptations induced by a low-protein, high-carbohydrate (LPHC) diet in growing rats, which by comparison with the rats fed a control (C) diet at displayed lower fasting glycemia and similar fasting insulinemia, despite impairment in insulin signaling in adipose tissues. In the insulin tolerance test the LPHC rats showed higher rates of glucose disappearance (30%) and higher tolerance to overload of glucose than C rats. The glucose uptake by the soleus muscle, evaluated in vivo by administration of 2-deoxy-[14C]glucose, increased by 81%. The phosphoenolp

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Saidi, Oussama, Emmanuelle Rochette, Giovanna Del Sordo, et al. "Isocaloric Diets with Different Protein-Carbohydrate Ratios: The Effect on Sleep, Melatonin Secretion and Subsequent Nutritional Response in Healthy Young Men." Nutrients 14, no. 24 (2022): 5299. http://dx.doi.org/10.3390/nu14245299.

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This study aimed to determine the short-term effect of two isocaloric diets differing in the ratio of protein–carbohydrate on melatonin levels, sleep, and subsequent dietary intake and physical activity in healthy young men. Twenty-four healthy men took part in a crossover design including two sessions of three days on isocaloric diets whether high-protein, low-carbohydrate (HPLC) or low-protein, high-carbohydrate (LPHC) followed by 24-h free living assessments. Sleep was measured by ambulatory polysomnography pre-post-intervention. Melatonin levels were assessed on the third night of each ses

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Chege, Boniface M., Peter W. Mwangi, Charles G. Githinji, and Frederick Bukachi. "Dietary regimens appear to possess significant effects on the development of combined antiretroviral therapy (cART)-associated metabolic syndrome." PLOS ONE 19, no. 2 (2024): e0298752. http://dx.doi.org/10.1371/journal.pone.0298752.

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Introduction This study investigated the interactions between a low protein high calorie (LPHC) diet and an integrase inhibitor-containing antiretroviral drug regimen (INI-CR)in light of evidence suggesting that the initiation of cART in patients with poor nutritional status is a predictor of mortality independent of immune status. Methods Freshly weaned Sprague Dawley rats (120) were randomized into the standard, LPHC and normal protein high calorie (NPHC) diet groups (n = 40/group) initially for 15 weeks. Thereafter, experimental animals in each diet group were further randomized into four t

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Schultz, Kathryn M., Tanner J. Lundquist, and Candice S. Klug. "Lipopolysaccharide binding to the periplasmic protein LptA." Protein Science 26, no. 8 (2017): 1517–23. http://dx.doi.org/10.1002/pro.3177.

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Chang, Kai-Fu, Xiao-Fan Huang, Yu-Ling Lin, et al. "Positively Charged Nanoparticle Delivery of n-Butylidenephthalide Enhances Antitumor Effect in Hepatocellular Carcinoma." BioMed Research International 2021 (March 19, 2021): 1–14. http://dx.doi.org/10.1155/2021/8817875.

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Hepatocellular carcinoma (HCC) is the second and sixth leading cause of cancer death in men and woman in 185 countries statistics, respectively. n-Butylidenephthalide (BP) has shown anti-HCC activity, but it also has an unstable structure that decreases its potential antitumor activity. The aim of this study was to investigate the cell uptake, activity protection, and antitumor mechanism of BP encapsulated in the novel liposome LPPC in HCC cells. BP/LPPC exhibited higher cell uptake and cytotoxicity than BP alone, and combined with clinical drug etoposide (VP-16), BP/LPPC showed a synergistic

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CHEN, Sharon C. A., Lesley C. WRIGHT, John C. GOLDING, and Tania C. SORRELL. "Purification and characterization of secretory phospholipase B, lysophospholipase and lysophospholipase/transacylase from a virulent strain of the pathogenic fungus Cryptococcus neoformans." Biochemical Journal 347, no. 2 (2000): 431–39. http://dx.doi.org/10.1042/bj3470431.

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Infection caused by the fungus Cryptococcus neoformans is potentially fatal. A highly active extracellular phospholipase, demonstrating phospholipase B (PLB), lysophospholipase (LPL) and lysophospholipase/transacylase (LPTA) activities, was purified to homogeneity from C. neoformans using (NH4)2SO4 fractionation, and hydrophobic-interaction, anion-exchange and gel-filtration chromatography. All three enzyme activities co-purified as a single protein with an apparent molecular mass of 70-90 kDa by SDS/PAGE and 160-180 kDa by gel filtration. The ratio of the three activities remained constant af

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Simamora, Cico Jhon Karunia, and Sukmawati Sukmawati. "Identifikasi dan Karakterisasi Aktivitas Ekstrak Kasar Enzim Lipase Isolat Bakteri Lipolitik Lptk 19 Asal Tempe Biji Karet." Median : Jurnal Ilmu Ilmu Eksakta 12, no. 1 (2020): 28. http://dx.doi.org/10.33506/md.v12i1.834.

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Lipase adalah enzim yang larut dalam air yang memiliki kemampuan untuk menghidrolisis triasilgliserol untuk melepaskan asam lemak bebas dan gliserol. Penelitian ini bertujuan untuk mengidentifikasi dan mengkarakterisasi aktivitas ekstrak kasar enzim lipase. Pelaksanaan penelitian meliputi peremajaan isolat, pengujian kualitatif produksi lipase yang ditunjukkan dengan adanya zona bening di sekitar koloni pada medium LAOR, dan dilanjutkan dengan pengujian kuantitatif aktivitas enzim lipase, uji aktivitas spesifik enzim, dan identifikasi biokimia isolat bakteri LpTk 19. Penelitian ini menunjukkan

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Zhang, Qi, Cuiping Zhang, Xiaoyu Li, et al. "WISP1 Is Increased in Intestinal Mucosa and Contributes to Inflammatory Cascades in Inflammatory Bowel Disease." Disease Markers 2016 (2016): 1–11. http://dx.doi.org/10.1155/2016/3547096.

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Inflammatory bowel disease (IBD) is mainly characterized by intestinal tissue damage, which is caused by excessive autoimmune responses poorly controlled by corresponding regulatory mechanisms. WISP1, which belongs to the CCN protein family, is a secreted matricellular protein regulating several inflammatory pathways, such as Wnt/β-catenin pathway, and has been reported in several diseases including cancer. Here we examined the expression, regulatory mechanisms, and functions of WISP1 in IBD. WISP1 mRNA and protein expression was upregulated in colonic biopsies and lamina propria mononuclear c

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Juibari, Aref Doozandeh, Sina Ramezani, and Mohammad Hosein Rezadoust. "Bioinformatics analysis of various signal peptides for periplasmic expression of parathyroid hormone in E.coli." Journal of Medicine and Life 12, no. 2 (2019): 184–91. http://dx.doi.org/10.25122/jml-2018-0049.

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Hypoparathyroidism is a rare endocrine disease which is characterized by the deficiency of serum calcium levels. RhPTH is prescribed as a therapy for the management of refractory hypoparathyroidism. The aim of this study is to investigate 32 signal peptides of gram-negative bacterial origin and evaluate their potential for efficient secretion of recombinant human PTH (1–84)In E.coli to obtain higher expression of recombinant PTH in bacterial systems by using this fusion partner. SignalP and ProtParam servers were employed to predict the presence and location of signal peptide cleavage sites in

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Consoli, Elisa, Jean-François Collet та Tanneke den Blaauwen. "The Escherichia coli Outer Membrane β-Barrel Assembly Machinery (BAM) Anchors the Peptidoglycan Layer by Spanning It with All Subunits". International Journal of Molecular Sciences 22, № 4 (2021): 1853. http://dx.doi.org/10.3390/ijms22041853.

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Gram-negative bacteria possess a three-layered envelope composed of an inner membrane, surrounded by a peptidoglycan (PG) layer, enclosed by an outer membrane. The envelope ensures protection against diverse hostile milieus and offers an effective barrier against antibiotics. The layers are connected to each other through many protein interactions. Bacteria evolved sophisticated machineries that maintain the integrity and the functionality of each layer. The β-barrel assembly machinery (BAM), for example, is responsible for the insertion of the outer membrane integral proteins including the li

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Schmidt, Robert, Russ B. Altman, and Mark Gerstein. "LPFC: An internet library of protein family core structures." Protein Science 6, no. 1 (1997): 246–48. http://dx.doi.org/10.1002/pro.5560060127.

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Goode, Triona, Joe O'Connell, Wen-Zhe Ho, et al. "Differential Expression of Neurokinin-1 Receptor by Human Mucosal and Peripheral Lymphoid Cells." Clinical Diagnostic Laboratory Immunology 7, no. 3 (2000): 371–76. http://dx.doi.org/10.1128/cdli.7.3.371-376.2000.

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ABSTRACT Substance P (SP) has been implicated in peripheral and mucosal neuroimmunoregulation. However, confusion remains regarding immunocyte expression of the receptor for SP, neurokinin-1 receptor (NK-1R), and whether there is differential NK-1R expression in the mucosal versus the peripheral immune system. In the same assay systems, we examined the expression of NK-1R in human lamina propria mononuclear cells (LPMC), peripheral blood mononuclear cells (PBMC), peripheral blood lymphocytes (PBL), monocytes, and monocyte-derived macrophages (MDM). Using standard reverse transcription (RT)-PCR

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Vrielink, Alice, Anandhi Anandan, Susannah Piek, Isabel Moares, and Charlene Kahler. "Structure of an endotoxin modifying enzyme and virulence factor in Neisseria." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C1047. http://dx.doi.org/10.1107/s2053273314089529.

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Multiple drug resistance (MDR) in Gram-negative bacteria represents one of the most intractable problems facing modern medicine. Not only is antibiotic resistance incrementally increasing during clinical treatment of infections, but also the evolution and acquisition of new mechanisms of antibiotic resistance lead to the sudden loss of the capacity to treat infections. The most recent superbug, MDR-Neisseria gonorrhoeae, causes the untreatable sexually transmitted infection gonorrhoeae. Chronic gonococcal infections have a high morbidity rate and, due to the explosion in cases worldwide, the c

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Wieczorek, Alicja, Anna Sendobra, Akshey Maniyeri, Magdalena Sugalska, Gracjana Klein, and Satish Raina. "A New Factor LapD Is Required for the Regulation of LpxC Amounts and Lipopolysaccharide Trafficking." International Journal of Molecular Sciences 23, no. 17 (2022): 9706. http://dx.doi.org/10.3390/ijms23179706.

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Lipopolysaccharide (LPS) constitutes the major component of the outer membrane and is essential for bacteria, such as Escherichia coli. Recent work has revealed the essential roles of LapB and LapC proteins in regulating LPS amounts; although, if any additional partners are involved is unknown. Examination of proteins co-purifying with LapB identified LapD as a new partner. The purification of LapD reveals that it forms a complex with several proteins involved in LPS and phospholipid biosynthesis, including FtsH-LapA/B and Fab enzymes. Loss of LapD causes a reduction in LpxC amounts and vancom

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Soltan, Mohamed A., Nada Elbassiouny, Helmy Gamal, et al. "In Silico Prediction of a Multitope Vaccine against Moraxella catarrhalis: Reverse Vaccinology and Immunoinformatics." Vaccines 9, no. 6 (2021): 669. http://dx.doi.org/10.3390/vaccines9060669.

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Moraxella catarrhalis (M. catarrhalis) is a Gram-negative bacterium that can cause serious respiratory tract infections and middle ear infections in children and adults. M. catarrhalis has demonstrated an increasing rate of antibiotic resistance in the last few years, thus development of an effective vaccine is a major health priority. We report here a novel designed multitope vaccine based on the mapped epitopes of the vaccine candidates filtered out of the whole proteome of M. catarrhalis. After analysis of 1615 proteins using a reverse vaccinology approach, only two proteins (outer membrane

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WRIGHT, Lesley C., Jackie PAYNE, Rosemary T. SANTANGELO, et al. "Cryptococcal phospholipases: a novel lysophospholipase discovered in the pathogenic fungus Cryptococcus gattii." Biochemical Journal 384, no. 2 (2004): 377–84. http://dx.doi.org/10.1042/bj20041079.

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The pathogenic fungus Cryptococcus neoformans produces an extracellular PLB1 (phospholipase B1), shown previously to be a virulence factor. A novel phospholipase (LPL1) with only LPL (lysophospholipase) and LPTA (transacylase) activities has now been characterized in C. gattii, and found to be a 66-kDa glycoprotein (by SDS/PAGE), with a native molecular mass of 670 kDa. The pI was 6.3, and it was active at high temperatures (to 70 °C), as well as at both acidic and neutral pH values. It was stimulated by calcium and palmitoyl carnitine at pH 7.0, but not at pH 5.0, and palmitoyl lysophosphatid

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