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Peptidoglycan recognition protein 2

N-acetylmuramoyl-L-alanine amidase, PGRP-L, TagL, PGLYRP2, peptidoglycan recognition protein 2, mPGRP-L
This gene encodes a peptidoglycan recognition protein, which belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. This protein hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in bacterial cell wall glycopeptides, and thus may play a scavenger role by digesting biologically active peptidoglycan into biologically inactive fragments. [provided by RefSeq, Sep 2011] (from NCBI)
Top mentioned proteins: ACID, fibrillin-1, CAN, HAD, Lysozyme
Papers on N-acetylmuramoyl-L-alanine amidase
Exoproteome analysis reveals higher abundance of proteins linked to alkaline stress in persistent Listeria monocytogenes strains.
Wagner et al., Vienna, Austria. In Int J Food Microbiol, Mar 2016
Furthermore proteins involved in cell wall modification, such as the lipoteichonic acid primase LtaP and the N-acetylmuramoyl-l-alanine amidase (Lmo2591) are more abundant in EGDe than in the persistent strains and could indirectly contribute to virulence.
Purification and Partial Characterization of a Novel Bacteriocin Synthesized by Lactobacillus paracasei HD1-7 Isolated from Chinese Sauerkraut Juice.
Ping et al., Harbin, China. In Sci Rep, Dec 2015
The N-terminal amino acid sequence of Paracin 1.7 was VSNTFFA, and the LC/LTQ results revealed that the N-terminal amino acid sequence was similar to that of ABC-type oligopeptide transport system protein and N-acetylmuramoyl-L-alanine amidase.
Investigation of antibacterial mechanism and identification of bacterial protein targets mediated by antibacterial medicinal plant extracts.
Wong et al., Kampar, Malaysia. In Food Chem, Dec 2015
From our study, seven differentially expressed bacterial proteins (triacylglycerol lipase, N-acetylmuramoyl-L-alanine amidase, flagellin, outer membrane protein A, stringent starvation protein A, 30S ribosomal protein s1 and 60 kDa chaperonin) were identified.
Characterization, Genome Sequence, and Analysis of Escherichia Phage CICC 80001, a Bacteriophage Infecting an Efficient L-Aspartic Acid Producing Escherichia coli.
Cheng et al., Beijing, China. In Food Environ Virol, Nov 2015
One protein belonged to class II holin, and the other two belonged to the endopeptidase family and N-acetylmuramoyl-L-alanine amidase family, respectively.
Expression, purification, and characterization of a bifunctional 99-kDa peptidoglycan hydrolase from Pediococcus acidilactici ATCC 8042.
Farrés et al., Mexico. In Appl Microbiol Biotechnol, Oct 2015
It has a higher N-acetylglucosaminidase activity, but the N-acetylmuramoyl-L-alanine amidase can also be detected spectrophotometrically.
Host Protein Biomarkers Identify Active Tuberculosis in HIV Uninfected and Co-infected Individuals.
Paramithiotis et al., United States. In Ebiomedicine, Sep 2015
Biomarker panels whose composition differed according to HIV status, and consisted of 8 host proteins in HIV(-) individuals (CD14, SEPP1, SELL, TNXB, LUM, PEPD, QSOX1, COMP, APOC1), or 10 host proteins in HIV(+) individuals (CD14, SEPP1, PGLYRP2, PFN1, VASN, CPN2, TAGLN2, IGFBP6), respectively, distinguished TB from ORD with excellent accuracy (AUC = 0.96 for HIV(-) TB, 0.95 for HIV(+) TB).
A Thermophilic Phage Endolysin Fusion to a Clostridium perfringens-Specific Cell Wall Binding Domain Creates an Anti-Clostridium Antimicrobial with Improved Thermostability.
Donovan et al., Beltsville, United States. In Viruses, Jun 2015
To produce a thermostabile endolysin for treating poultry, an E. coli codon-optimized gene was synthesized that fused the N-acetylmuramoyl-L-alanine amidase domain from the endolysin of the thermophilic bacteriophage ɸGVE2 to the cell-wall binding domain (CWB) from the endolysin of the C. perfringens-specific bacteriophage ɸCP26F.
Plasma clusterin as a candidate pre-diagnosis marker of colorectal cancer risk in the Florence cohort of the European Prospective Investigation into Cancer and Nutrition: a pilot study.
Palli et al., Milano, Italy. In Bmc Cancer, 2014
Eight proteins including apolipoprotein C-II, complement C4-B, complement component C9, clusterin, alpha-2-HS-glycoprotein, mannan-binding lectin serine-protease, mannose-binding protein C, and N-acetylmuramoyl-L-alanine amidase were selected as promising candidate biomarkers.
The First Paenibacillus larvae Bacteriophage Endolysin (PlyPl23) with High Potential to Control American Foulbrood.
Azeredo et al., Braga, Portugal. In Plos One, 2014
The new endolysin described herein has an N-acetylmuramoyl-L-alanine amidase catalytic domain and exhibits a broad-spectrum activity against common P. larvae genotypes.
Functional and structural analysis of the major amidase (Atl) in Staphylococcus.
Stehle et al., Tübingen, Germany. In Int J Med Microbiol, 2014
In staphylococci, the major autolysin (Atl) and its processed products N-acetylmuramoyl-l-alanine amidase (AM) and endo-β-N-acetylglucosaminidase (GL) have been in the research focus for long time.
Role of mouse peptidoglycan recognition protein PGLYRP2 in the innate immune response to Salmonella enterica serovar Typhimurium infection in vivo.
Girardin et al., Toronto, Canada. In Infect Immun, 2012
Nod2(-/-) Pglyrp2(-/-) mice displayed increased susceptibility to infection at 24 h postinfection compared to Pglyrp2(-/-). Thus, PGLYRP2 plays a protective role in vivo in the control of S. Typhimurium infection through a Nod1/Nod2-independent mechanism.
Recombinant Expression of a Putative Amidase Cloned from the Genome of Listeria monocytogenes that Lyses the Bacterium and its Monolayer in Conjunction with a Protease.
Seal et al., Athens, United States. In Probiotics Antimicrob Proteins, 2012
PCR primers were designed that amplified nucleotide sequences of a putative N-acetylmuramoyl-L-alanine amidase gene from L. monocytogenes strain 4b.
Peptidoglycan recognition protein Pglyrp2 protects mice from psoriasis-like skin inflammation by promoting regulatory T cells and limiting Th17 responses.
Dziarski et al., Gary, United States. In J Immunol, 2012
Pglyrp2 limits overactivation of Th17 cells by promoting accumulation of regulatory T cells at the site of inflammation in an experimentally induced mouse model of psoriasis
Control of intestinal Nod2-mediated peptidoglycan recognition by epithelium-associated lymphocytes.
Hornef et al., Hannover, Germany. In Mucosal Immunol, 2011
role in regulation of the enteric host-microbe homeostasis
Review: Mammalian peptidoglycan recognition proteins (PGRPs) in innate immunity.
Gupta et al., Gary, United States. In Innate Immun, 2010
Three PGRPs, PGLYRP1, PGLYRP3, and PGLYRP4 are directly bactericidal for both Gram-positive and Gram-negative bacteria and have no enzymatic activity, whereas PGLYRP2 is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial cell wall peptidoglycan.
PGLYRP-2 and Nod2 are both required for peptidoglycan-induced arthritis and local inflammation.
Dziarski et al., Gary, United States. In Cell Host Microbe, 2009
The authors demonstrate that PGLYRP-2 and Nod2 are both required for arthritis in the peptidoglycan-induced arthritis model in mice.
Mammalian PGRPs in the spotlight.
Boneca, Paris, France. In Cell Host Microbe, 2009
In this issue of Cell Host & Microbe, Saha et al. (2009) report that the mammalian PGRP, PGLYRP-2, functions as a cytokine-like molecule in a PG-induced arthritis model.
Differential expression of peptidoglycan recognition protein 2 in the skin and liver requires different transcription factors.
Gupta et al., Gary, United States. In J Biol Chem, 2006
pglyrp2 expression in skin and liver is important for systemic and local innate immune responses to bacterial infections
Mammalian PGRPs: novel antibacterial proteins.
Gupta et al., Gary, United States. In Cell Microbiol, 2006
One mammalian PGRP, PGLYRP-2, is an N-acetylmuramoyl-L-alanine amidase that hydrolyses bacterial peptidoglycan and reduces its proinflammatory activity.
The peptidoglycan recognition proteins (PGRPs).
Gupta et al., Gary, United States. In Genome Biol, 2005
One mammalian PGRP, PGLYRP-2, is an N-acetylmuramoyl-L-alanine amidase that hydrolyzes bacterial peptidoglycan and reduces its proinflammatory activity; PGLYRP-2 is secreted from the liver into the blood and is also induced by bacteria in epithelial cells.
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