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Activity Augmentation of Amphioxus Peptidoglycan Recognition Protein BbtPGRP3 via Fusion with a Chitin Binding Domain

Peptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isof... Full description

Journal Title: PloS one 2015, Vol.10(10), pp.e0140953
Main Author: Wang, Wen-Jie
Other Authors: Cheng, Wang , Luo, Ming , Yan, Qingyu , Yu, Hong-Mei , Li, Qiong , Cao, Dong-Dong , Huang, Shengfeng , Xu, Anlong , Mariuzza, Roy A , Chen, Yuxing , Zhou, Cong-Zhao
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1932-6203 ; PMID: 26479246 Version:1 ; DOI: 10.1371/journal.pone.0140953
Link: http://pubmed.gov/26479246
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recordid: medline26479246
title: Activity Augmentation of Amphioxus Peptidoglycan Recognition Protein BbtPGRP3 via Fusion with a Chitin Binding Domain
format: Article
creator:
  • Wang, Wen-Jie
  • Cheng, Wang
  • Luo, Ming
  • Yan, Qingyu
  • Yu, Hong-Mei
  • Li, Qiong
  • Cao, Dong-Dong
  • Huang, Shengfeng
  • Xu, Anlong
  • Mariuzza, Roy A
  • Chen, Yuxing
  • Zhou, Cong-Zhao
subjects:
  • Carrier Proteins -- Chemistry
  • Chitin -- Metabolism
  • Recombinant Fusion Proteins -- Chemistry
ispartof: PloS one, 2015, Vol.10(10), pp.e0140953
description: Peptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isoforms of PGRP encoded by Branchiostoma belcheri tsingtauense, termed BbtPGRP1~3, are fused with a chitin binding domain (CBD) at the N-terminus. Here we report the 2.7 Å crystal structure of BbtPGRP3, revealing an overall structure of an N-terminal hevein-like CBD followed by a catalytic PGRP domain. Activity assays combined with site-directed mutagenesis indicated that the individual PGRP domain exhibits amidase activity towards both DAP-type and Lys-type peptidoglycans (PGNs), the former of which is favored. The N-terminal CBD not only has the chitin-binding activity, but also enables BbtPGRP3 to gain a five-fold increase of amidase activity towards the Lys-type PGNs, leading to a significantly...
language: eng
source:
identifier: E-ISSN: 1932-6203 ; PMID: 26479246 Version:1 ; DOI: 10.1371/journal.pone.0140953
fulltext: fulltext
issn:
  • 19326203
  • 1932-6203
url: Link


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titleActivity Augmentation of Amphioxus Peptidoglycan Recognition Protein BbtPGRP3 via Fusion with a Chitin Binding Domain
creatorWang, Wen-Jie ; Cheng, Wang ; Luo, Ming ; Yan, Qingyu ; Yu, Hong-Mei ; Li, Qiong ; Cao, Dong-Dong ; Huang, Shengfeng ; Xu, Anlong ; Mariuzza, Roy A ; Chen, Yuxing ; Zhou, Cong-Zhao
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subjectCarrier Proteins -- Chemistry ; Chitin -- Metabolism ; Recombinant Fusion Proteins -- Chemistry
descriptionPeptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isoforms of PGRP encoded by Branchiostoma belcheri tsingtauense, termed BbtPGRP1~3, are fused with a chitin binding domain (CBD) at the N-terminus. Here we report the 2.7 Å crystal structure of BbtPGRP3, revealing an overall structure of an N-terminal hevein-like CBD followed by a catalytic PGRP domain. Activity assays combined with site-directed mutagenesis indicated that the individual PGRP domain exhibits amidase activity towards both DAP-type and Lys-type peptidoglycans (PGNs), the former of which is favored. The N-terminal CBD not only has the chitin-binding activity, but also enables BbtPGRP3 to gain a five-fold increase of amidase activity towards the Lys-type PGNs, leading to a significantly...
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descriptionPeptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isoforms of PGRP encoded by Branchiostoma belcheri tsingtauense, termed BbtPGRP1~3, are fused with a chitin binding domain (CBD) at the N-terminus. Here we report the 2.7 Å crystal structure of BbtPGRP3, revealing an overall structure of an N-terminal hevein-like CBD followed by a catalytic PGRP domain. Activity assays combined with site-directed mutagenesis indicated that the individual PGRP domain exhibits amidase activity towards both DAP-type and Lys-type peptidoglycans (PGNs), the former of which is favored. The N-terminal CBD not only has the chitin-binding activity, but also enables BbtPGRP3 to gain a five-fold increase of amidase activity towards the Lys-type PGNs, leading to a significantly...
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abstractPeptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isoforms of PGRP encoded by Branchiostoma belcheri tsingtauense, termed BbtPGRP1~3, are fused with a chitin binding domain (CBD) at the N-terminus. Here we report the 2.7 Å crystal structure of BbtPGRP3, revealing an overall structure of an N-terminal hevein-like CBD followed by a catalytic PGRP domain. Activity assays combined with site-directed mutagenesis indicated that the individual PGRP domain exhibits amidase activity towards both DAP-type and Lys-type peptidoglycans (PGNs), the former of which is favored. The N-terminal CBD not only has the chitin-binding activity, but also enables BbtPGRP3 to gain a five-fold increase of amidase activity towards the Lys-type PGNs, leading to a significantly...
doi10.1371/journal.pone.0140953
pmid26479246