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Peptidoglycan recognition protein

Ke-Yi Zhang, Wen-Jie Yuan, Ji-Dong Xu, Jin-Xing Wang
The cation-dependent mannose-6-phosphate receptor (CD-MPR) is a member of the P-type lectin family. As a type I transmembrane glycoprotein, it functions in the delivery of newly synthesized acid hydrolases from the trans-Golgi network to endosomes for their subsequent transfer to the lysosome by binding the mannose-6-phosphate receptor-recognition moieties in the hydrolases. However, the functions of CD-MPR in immune responses are seldom reported. In the present study, we identified a CD-MPR-like molecule in Marsupenaeus japonicus and designed it as MjCD-MPR...
August 14, 2018: Developmental and Comparative Immunology
Mariela García-Ramos, Javier de la Mora, Teresa Ballado, Laura Camarena, Georges Dreyfus
In this work we have characterized the soluble lytic transglycosylase (SltF) from Rhodobacter sphaeroides that interacts with the scaffolding protein FlgJ in the periplasm to open space at the cell wall peptidoglycan heteropolymer for the emerging rod. The characterization of the genetic context of flgJ and s ltF in α-proteobacteria shows that these two separate genes coexist frequently in a flagellar gene cluster. Two domains of unknown function in SltF were studied and results show that deletion of a 17 amino acid segment near the N-terminus does not show a recognizable phenotype whereas the deletion of 47 and 95 amino acid of the C-terminus of SltF disrupts the interaction with FlgJ without affecting the transglycosylase catalytic activity of SltF...
July 30, 2018: Journal of Bacteriology
Hui Yang, Xixi Li, Weijia Song, Jiaojun Ji, Fenggang Li, Yingying Zhang, Xiaojun Zhang, Lixin Wang
PGRPs (Peptidoglycan recognition proteins) could recognize peptidoglycan and play vital roles in innate immunity among different animals. Till present, the functions of PGRP have been studied in various animals, but few reports have studied the amphibian PGRPs. In the current research, a short type PGRP was identified from Chinese giant salamander and its involvement in the innate immunity was studied. The ORF of AdPGRP-SC2 cDNA was 573 bp, which encoded 190 amino acids, and contained a PGRP and an amidase_2 domain...
July 12, 2018: Developmental and Comparative Immunology
Ruo-Nan Zhang, Fei-Fei Ren, Cheng-Bo Zhou, Jun-Feng Xu, Hui-Yu Yi, Ming-Qiang Ye, Xiao-Juan Deng, Yang Cao, Xiao-Qiang Yu, Wan-Ying Yang
Lipopolysaccharide (LPS) is a common component of the outermost cell wall in Gram-negative bacteria. In mammals, LPS serves as an endotoxin that can be recognized by a receptor complex of TLR4 (Toll-like receptor 4) and MD-2 (myeloid differentiation-2) and subsequently induce a strong immune response to signal the release of tumor necrosis factor (TNF). In Drosophila melanogaster, no receptors for LPS have been identified, and LPS cannot activate immune responses. Here, we report a protein, BmEsr16, which contains an ML (MD-2-related lipid-recognition) domain, may function as an LPS receptor in the silkworm Bombyx mori...
July 17, 2018: Developmental and Comparative Immunology
Maarten G K Ghequire, Başak Öztürk
Pyocins are bacteriocins secreted by Pseudomonas aeruginosa , and assist in the colonization of different niches. A major subset of these antibacterial proteins adopt a modular organization characteristic of polymorphic toxins. They comprise a receptor-binding domain, a segment enabling membrane passage, and a toxin module at the carboxy-terminus that eventually kills the target cell. To protect from its own product, bacteriocin producer strains concomitantly express an immunity gene along with the bacteriocin...
July 6, 2018: Applied and Environmental Microbiology
Jun Li, Yang Zhang, Yuehuan Zhang, Fan Mao, Shu Xiao, Zhiming Xiang, Haitao Ma, Ziniu Yu
Lysin motif (LysM)-containing proteins are a family of carbohydrate-binding modules and are generally regarded as chitin- and peptidoglycan-binding proteins. In the present study, a novel LysM-containing protein, designated as ChLysM, was cloned and identified in a marine mollusk, Crassostrea hongkongensis. The full-length cDNA of ChLysM consists of 1129 bp, with an open reading frame of 861 bp encoding a 286 amino acid polypeptide. The deduced protein had a calculated molecular mass of 32.66 kDa and a pI of 8...
June 27, 2018: Gene
Lok To Sham, Sanduo Zheng, Anastasiya A Yakhnina, Andrew C Kruse, Thomas G Bernhardt
Bacteria produce a variety of surface-exposed polysaccharides important for cell integrity, biofilm formation, and evasion of the host immune response. Synthesis of these polymers often involves the assembly of monomer oligosaccharide units on the lipid carrier undecaprenyl-phosphate at the inner face of the cytoplasmic membrane. For many polymers, including cell wall peptidoglycan, the lipid-linked precursors must be transported across the membrane by flippases to facilitate polymerization at the membrane surface...
June 15, 2018: Molecular Microbiology
Ping Zhao, Fei Xia, Liang Jiang, Huizhen Guo, Guowen Xu, Qiang Sun, Bingbing Wang, Yumei Wang, Zhongyan Lu, Qingyou Xia
In insect innate immunity, peptidoglycan recognition proteins act as pattern recognition receptors, helping hosts combat invasive microorganisms. Bombyx mori cytoplasmic polyhedrosis virus (BmCPV) is the main silkworm pathogen that invades the midgut columnar cell layer. We previously reported that B. mori peptidoglycan recognition protein S2 (BmPGRP-S2) was upregulated in silkworm larvae after BmCPV infection. Here, we constructed a transgenic vector overexpressing BmPGRP-S2 under the control of a midgut-specific promoter...
October 2018: Developmental and Comparative Immunology
Lian-Qin Chai, Jing-Hui Meng, Jie Gao, Yi-Hui Xu, Xian-Wei Wang
Prophenoloxidase (proPO) activating system is an important immune response for arthropods. β-1, 3-glucanase related protein (previously named as lipopolysaccharide and β-1, 3-glucan binding protein (LGBP) in crustaceans) is a typical pattern recognition receptor family involved in the proPO activation by recognizing the invading microbes. In this study, we pay special attention to a bacteria-induced β-1,3-glucanase related protein from red swamp crayfish Procambarus clarkii, an important aquaculture specie in China...
September 2018: Fish & Shellfish Immunology
Rolf Grempler, Michael Wolff, Eric Simon, Ramona Schmid, Claudia Eisele, Kathrin Rieber, Elke Fischer, Sonja Mettel, Ogsen Gabrielyan, Denis Delic, Gerd Luippold, Norbert Redeman
BACKGROUND: Activation of the AMP-activated protein kinase (AMPK) is an attractive approach for the treatment of type 2 diabetes. AMPK activation reduces glucose levels in animal models of type 2 diabetes by increasing glucose uptake in skeletal muscles and reducing hepatic glucose production. Furthermore, AMPK activation ameliorates hepatic steatosis in animal models. For the clinical development of AMPK activators it is essential to have a reliable target engagement marker for appropriate dose finding and to support proof of clinical principle...
2018: PloS One
Matthew R Alexander, Allison E Norlander, Fernando Elijovich, Ravi V Atreya, Amadou Gaye, Juan S Gnecco, Cheryl L Laffer, Cristi L Galindo, Meena S Madhur
BACKGROUND AND PURPOSE: Monocytes play a critical role in hypertension. The purpose of our study was to use an unbiased approach to determine whether hypertensive individuals on conventional therapy exhibit an altered monocyte gene expression profile and to perform validation studies of selected genes to identify novel therapeutic targets for hypertension. EXPERIMENTAL APPROACH: Next generation RNA sequencing identified differentially expressed genes in a small discovery cohort of normotensive and hypertensive individuals...
May 18, 2018: British Journal of Pharmacology
Hui Wang, Zhuang Xue, Zhaoqun Liu, Weilin Wang, Feifei Wang, Ying Wang, Lingling Wang, Linsheng Song
C-type lectins (CTLs) are Ca2+ dependent carbohydrate-binding proteins that share structural homology in their carbohydrate-recognition domains (CRDs). In the present study, a novel CTL was identified from sea cucumber Apostichopus japonicus (named as AjCTL-2). The deduced amino acid sequence of AjCTL-2 was homologous to CTLs from other animals with the identities ranging from 33% to 40%. It contained a canonical signal peptide at the N-terminus, a low density lipoprotein receptor class A (LDLa), a C1r/C1s/Uegf/bone morphogenetic protein 1 (CUB), and a CRD with two motifs Glu-Pro-Asn (EPN) and Trp-Asn-Asp (WND) in Ca2+ binding site 2...
August 2018: Fish & Shellfish Immunology
Dongyang Liu, Qilin Yi, Yichen Wu, Guangxia Lu, Changhao Gong, Xiaorui Song, Jiejie Sun, Chen Qu, Conghui Liu, Lingling Wang, Linsheng Song
Immunoglobulin superfamily (IgSF), an extensive collection of proteins possessing at least one immunoglobulin-like (Ig-like) domain, performs a wide range of functions in recognition, binding or adhesion process of cells. In the present study, a cysteine-rich motif associated immunoglobulin domain containing protein (designated CgCAICP-1) was identified in Pacific oyster Crassostrea gigas. The deduced protein sequence of CgCAICP-1 contained 534 amino acidresidues, with three Ig domains which were designated as IG1, IG2 and IG3, and a cysteine-rich motif between the first and second Ig domain...
September 2018: Developmental and Comparative Immunology
Siqi Zhao, Xialu Wang, Siyu Cai, Siqiang Zhang, Hao Luo, Chunfu Wu, Rong Zhang, Jinghai Zhang
Pattern recognition receptors (PRRs) are employed in insects to defend against infectious pathogens by triggering various immune responses. Peptidoglycan recognition proteins (PGRPs), a vital family of PRRs, are widely distributed and highly conserved from vertebrates to invertebrates. To date, five PGRP genes have been identified in Antheraea pernyi, but their biochemical roles still remain unknown. In this study, we focused on the immune functions of PGRP-SA in A. pernyi (ApPGRP-SA), which was confirmed to be immune-related according to its significantly up-regulated expression level post microbial injection...
September 2018: Developmental and Comparative Immunology
Bishnu Dawadi, Xinghong Wang, Rong Xiao, Abrar Muhammad, Youming Hou, Zhanghong Shi
Many notorious insect pests live in the symbiotic associations with gut microbiota. However, the mechanisms underlying how they host their gut microbiota are unknown. Most gut bacteria can release peptidoglycan (PGN) which is an important antigen to activate the immune response. Therefore, how to keep the appropriate gut immune intensity to host commensals while to efficiently remove enteropathogens is vital for insect health. This study is aimed at elucidating the roles of an amidase PGRP, Rf PGRP-LB, in maintaining the gut-microbe symbiosis of Red palm weevil (RPW), Rhynchophorus ferrugineus Olivier...
September 2018: Developmental and Comparative Immunology
Gurmeet Kaur, Lakshminarayan M Iyer, Srikrishna Subramanian, L Aravind
SH3-fold-β-barrel domains of the chromo-like superfamily recognize epigenetic marks in eukaryotic proteins. Their provenance has been placed either in archaea, based on apparent structural similarity to chromatin-compacting Sul7d and Cren7 proteins, or in bacteria based on the presence of sequence homologs. Using sequence and structural evidence we establish that the archaeal Cren7/Sul7 proteins emerged from a zinc ribbon (ZnR) ancestor. Further, we show that the ancestral eukaryotic chromo-like domains evolved from bacterial versions, likely acquired from early endosymbioses, which already possessed an aromatic cage for recognition of modified amino-groups...
April 18, 2018: Scientific Reports
Ying Wang, Zhuang Xue, Qilin Yi, Hui Wang, Lingling Wang, Guangxia Lu, Yu Liu, Chen Qu, Yannan Li, Linsheng Song
F-type lectin (also known as fucolectin) is a newly identified family of fucose binding lectins with the sequence characters of a fucose binding motif and a unique lectin fold (the "F-type" fold). In the present study, a fucolectin was identified from sea cucumber Apostichopus japonicus (designated AjFL-1). The open reading frame (ORF) of AjFL-1 was of 546 bp, encoding a polypeptide of 181 amino acids with a predicted molecular mass of about 20 kDa. The deduced amino acid sequence of AjFL-1 shared 30%-40% similarity with the fucolectins from other animals...
June 2018: Fish & Shellfish Immunology
Kwang-Min Choi, Min-Soo Joo, Dong-Hee Cho, Jin-Sol Bae, Ji-Min Jeong, Won-Sik Woo, Hyun-Ja Han, Deok Chan Lee, Mi Young Cho, Sung Hee Jung, Do-Hyung Kim, Chan-Il Park
Peptidoglycan recognition proteins are members of the family of pattern recognition receptors (PRRs), that play important roles in the recognition of peptidoglycan and various biological processes. In this study, we have characterized peptidoglycan recognition protein-SC2 (PGRP-SC2) in rock bream (Oplegnathus fasciatus) (RbPGRP-SC2) and analysed its expression in various tissues after pathogen challenge. A sequence alignment revealed that the residues essential to zinc binding of the deduced protein were highly conserved among all the organisms...
June 2018: Fish & Shellfish Immunology
Xin Huang, Keke Han, Tingting Li, Wen Wang, Qian Ren
L-type lectins (LTLs) play important roles in the secretory pathway of animals, including selective protein trafficking, sorting, and targeting. They have a leguminous lectin domain and can bind to high-mannose-type oligosaccharides. In this study, a novel LTL, designated as MrVIP36, was identified from Macrobrachium rosenbergii. The full-length cDNA of MrVIP36 was 1687 bp with a 972 bp open reading frame encoding a putative protein of 323 deduced amino acids. The deduced MrVIP36 protein contained an LTL-like domain (LTLD) and a transmembrane domain...
June 2018: Fish & Shellfish Immunology
Jie Yan, Lei Chen, Zhuang Liu, Yonglin Chen, Ying Sun, Jia Han, Lijun Feng
Intelectin is a recently characterized soluble galactofuranose-binding lectin that exists in species ranging from amphioxus to human. Interestingly, intelectin does not contain a canonical carbohydrate-recognition domain (CRD). Therefore, we designed serial deletions of intelectin in the Chinese amphioxus (Branchiostoma belcheri tsingtauense, AmphiITLN71469) in order to identify functional regions required for carbohydrate binding. Our results revealed that Domain 5 (aa 203-302) was able to bind lipopolysaccarides (LPS) or peptidoglycan (PGN) and agglutinate bacteria as efficiently as the full-length protein...
August 2018: Developmental and Comparative Immunology
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