The Experts below are selected from a list of 2025 Experts worldwide ranked by ideXlab platform
Jialong Yang - One of the best experts on this subject based on the ideXlab platform.
-
Peptidoglycan Recognition Protein of Solen grandis (SgPGRP-S1) mediates immune Recognition and bacteria clearance.
Fish & shellfish immunology, 2017Co-Authors: Xiumei Wei, Dinglong Yang, Tianyu Zhao, Hailin Jiang, Xiangquan Liu, Jialong YangAbstract:Peptidoglycan Recognition Proteins (PGRPs) are indispensable molecules in innate immunity due to their prominent function in sensing and eliminating invading microorganisms. In the present study, a short type PGRP from razor clam Solen grandis (SgPGRP-S1) was recombinantly expressed and purified to investigate its potential function in innate immunity. As a pattern Recognition receptor, recombinant SgPGRP-S1 (rSgPGRP-S1) specifically bind Lys-type and Dap-type Peptidoglycan in vitro, but not lipopolysaccharide or β-glucan. The Peptidoglycan binding ability of rSgPGRP-S1 resulted in significant agglutination activity against Gram-negative Escherichia coli and Listonella anguillarum, as well as Gram-positive Micrococcus luteus. Furthermore, rSgPGRP-S1 was bactericidal, significantly suppressing the growth of both E. coli and Gram-positive Staphylococcus aureus. The Protein also exhibited strong amidase activity and degraded bacterial Peptidoglycan in the presence of Zn2+, suggesting amidase activity might contribute to SgPGRP-S1 antibacterial activity. These results indicate SgPGRP-S1 is multifunctional in innate immunity, mediating both immune Recognition and bacteria elimination.
-
Peptidoglycan Recognition Protein of chlamys farreri cfpgrp s1 mediates immune defenses against bacterial infection
Developmental and Comparative Immunology, 2010Co-Authors: Jialong Yang, Limei Qiu, Huan Zhang, Wan Wang, Xiumei Wei, Lingling Wang, Linsheng SongAbstract:Peptidoglycan Recognition Protein (PGRP) is an essential molecule in innate immunity for both invertebrates and vertebrates, owing to its prominent ability in detecting and eliminating the invading bacteria. Several PGRPs have been identified from mollusk, but their functions and the underlined mechanism are still unclear. In the present study, the mRNA expression profiles, location, and possible functions of PGRP-S1 from Zhikong scallop Chlamys farreri (CfPG RP-St) were analyzed. The CfPGRP-S1 Protein located in the mantle, gill, kidney and gonad of the scallops. Its mRNA expression in hemocytes was up-regulated extremely after PGN stimulation (P < 0.01), while moderately after the stimulations of LPS (P < 0.01) and beta-glucan (P < 0.05). The recombinant Protein of CfPGRP-S1 (designated as rCfPGRP-S1) exhibited high affinity to PGN and moderate affinity to LPS, but it did not bind beta-glucan. Meanwhile, rCfPGRP-S1 also exhibited strong agglutination activity to Gram-positive bacteria Micrococcus luteus and Bacillus subtilis and weak activity to Gram-negative bacteria Escherichia coli. More importantly, rCfPGRP-S1 functioned as a bactericidal amidase to degrade PGN and strongly inhibit the growth of E. coli and Staphyloccocus aureus in the presence of Zn(2+). These results indicated that CfPGRP-S1 could not only serve as a pattern Recognition receptor recognizing bacterial PGN and LPS, but also function as a scavenger involved in eliminating response against the invaders. (C) 2010 Elsevier Ltd. All rights reserved.
Linsheng Song - One of the best experts on this subject based on the ideXlab platform.
-
Peptidoglycan Recognition Protein of chlamys farreri cfpgrp s1 mediates immune defenses against bacterial infection
Developmental and Comparative Immunology, 2010Co-Authors: Jialong Yang, Limei Qiu, Huan Zhang, Wan Wang, Xiumei Wei, Lingling Wang, Linsheng SongAbstract:Peptidoglycan Recognition Protein (PGRP) is an essential molecule in innate immunity for both invertebrates and vertebrates, owing to its prominent ability in detecting and eliminating the invading bacteria. Several PGRPs have been identified from mollusk, but their functions and the underlined mechanism are still unclear. In the present study, the mRNA expression profiles, location, and possible functions of PGRP-S1 from Zhikong scallop Chlamys farreri (CfPG RP-St) were analyzed. The CfPGRP-S1 Protein located in the mantle, gill, kidney and gonad of the scallops. Its mRNA expression in hemocytes was up-regulated extremely after PGN stimulation (P < 0.01), while moderately after the stimulations of LPS (P < 0.01) and beta-glucan (P < 0.05). The recombinant Protein of CfPGRP-S1 (designated as rCfPGRP-S1) exhibited high affinity to PGN and moderate affinity to LPS, but it did not bind beta-glucan. Meanwhile, rCfPGRP-S1 also exhibited strong agglutination activity to Gram-positive bacteria Micrococcus luteus and Bacillus subtilis and weak activity to Gram-negative bacteria Escherichia coli. More importantly, rCfPGRP-S1 functioned as a bactericidal amidase to degrade PGN and strongly inhibit the growth of E. coli and Staphyloccocus aureus in the presence of Zn(2+). These results indicated that CfPGRP-S1 could not only serve as a pattern Recognition receptor recognizing bacterial PGN and LPS, but also function as a scavenger involved in eliminating response against the invaders. (C) 2010 Elsevier Ltd. All rights reserved.
-
The expression of Peptidoglycan Recognition Protein-S1 gene in the scallop Chlamys farreri was enhanced after a second challenge by Listonella anguillarum.
Journal of invertebrate pathology, 2008Co-Authors: Ming Cong, Linsheng Song, Limei Qiu, Bo Wang, Huan Zhang, Lei ZhangAbstract:A more rapid and powerful response against repeated exposure of same pathogen in vertebrates is usually considered as the reflection of immunological memory, but it is not well understood in invertebrates. In the present Study, the temporal expression profiles of Chlamys farreri Peptidoglycan Recognition Protein-S1 (CfPGRP-S1) gene after two challenges of Listonella anguillarum were examined to evaluate priming response in scallops. The up-regulation of CFPGRP-S1 mRNA occurred 3 h earlier, and the expression level was significant higher (P < 0.05), after the second challenge than that after the first challenge. The preliminary results Provided new insights into invertebrate immunological memory, and they also would be helpful to develop strategies for disease control. (C) 2008 Elsevier Inc. All rights reserved.
-
molecular cloning and characterization of a short type Peptidoglycan Recognition Protein cfpgrp s1 cdna from zhikong scallop chlamys farreri
Fish & Shellfish Immunology, 2007Co-Authors: Linsheng Song, Jianmin Zhao, Limei QiuAbstract:Peptidoglycan Recognition Protein (PGRP) specifically binds to Peptidoglycan and plays a crucial role in the innate immune responses as a pattern Recognition receptor (PRR). The cDNA of a short type PGRP was cloned from scallop Chlamys farreri (named CfPGRP-SI) by homology cloning with degenerate primers, and confirmed by virtual Northern blots. The full length of CfPGRP-SI cDNA was 1073 bp in length, including a 5 ' untranslated region (UTR) of 59 bp, a 3 ' UTR of 255 bp, and an open reading frame (ORF) of 759 bp encoding a polypeptide of 252 amino acids with an estimated molecular mass of 27.88 kDa and a predicted isoelectric point of 8.69. BLAST analysis revealed that CfPGRP-S1 shared high identities with other known PGRPs. A conserved PGRP domain and three zinc-binding sites were present at its C-terminus. The temporal expression of QPGRP-S1 gene in healthy, Vibrio anguillarum-challenged and Micrococcus lysodeikticus-challenged scallops was measured by RT-PCR analysis. The expression of CfPGRP-S1 was upregulated initially in the first 12 h or 24 h either by M. lysodeikticus or V. anguillarum challenge and reached the maximum level at 24 h or 36 h, then dropped progressively, and recovered to the original level as the stimulation decreased at 72 h. There was no significant difference between V. anguillarum and M. lysodeikticus challenge. The results indicated that the CfPGRP-S1 was a constitutive and inducible acute-phase Protein which was involved in the immune response against bacterial infection. (c) 2007 Elsevier Ltd. All rights reserved.
Limei Qiu - One of the best experts on this subject based on the ideXlab platform.
-
Peptidoglycan Recognition Protein of chlamys farreri cfpgrp s1 mediates immune defenses against bacterial infection
Developmental and Comparative Immunology, 2010Co-Authors: Jialong Yang, Limei Qiu, Huan Zhang, Wan Wang, Xiumei Wei, Lingling Wang, Linsheng SongAbstract:Peptidoglycan Recognition Protein (PGRP) is an essential molecule in innate immunity for both invertebrates and vertebrates, owing to its prominent ability in detecting and eliminating the invading bacteria. Several PGRPs have been identified from mollusk, but their functions and the underlined mechanism are still unclear. In the present study, the mRNA expression profiles, location, and possible functions of PGRP-S1 from Zhikong scallop Chlamys farreri (CfPG RP-St) were analyzed. The CfPGRP-S1 Protein located in the mantle, gill, kidney and gonad of the scallops. Its mRNA expression in hemocytes was up-regulated extremely after PGN stimulation (P < 0.01), while moderately after the stimulations of LPS (P < 0.01) and beta-glucan (P < 0.05). The recombinant Protein of CfPGRP-S1 (designated as rCfPGRP-S1) exhibited high affinity to PGN and moderate affinity to LPS, but it did not bind beta-glucan. Meanwhile, rCfPGRP-S1 also exhibited strong agglutination activity to Gram-positive bacteria Micrococcus luteus and Bacillus subtilis and weak activity to Gram-negative bacteria Escherichia coli. More importantly, rCfPGRP-S1 functioned as a bactericidal amidase to degrade PGN and strongly inhibit the growth of E. coli and Staphyloccocus aureus in the presence of Zn(2+). These results indicated that CfPGRP-S1 could not only serve as a pattern Recognition receptor recognizing bacterial PGN and LPS, but also function as a scavenger involved in eliminating response against the invaders. (C) 2010 Elsevier Ltd. All rights reserved.
-
The expression of Peptidoglycan Recognition Protein-S1 gene in the scallop Chlamys farreri was enhanced after a second challenge by Listonella anguillarum.
Journal of invertebrate pathology, 2008Co-Authors: Ming Cong, Linsheng Song, Limei Qiu, Bo Wang, Huan Zhang, Lei ZhangAbstract:A more rapid and powerful response against repeated exposure of same pathogen in vertebrates is usually considered as the reflection of immunological memory, but it is not well understood in invertebrates. In the present Study, the temporal expression profiles of Chlamys farreri Peptidoglycan Recognition Protein-S1 (CfPGRP-S1) gene after two challenges of Listonella anguillarum were examined to evaluate priming response in scallops. The up-regulation of CFPGRP-S1 mRNA occurred 3 h earlier, and the expression level was significant higher (P < 0.05), after the second challenge than that after the first challenge. The preliminary results Provided new insights into invertebrate immunological memory, and they also would be helpful to develop strategies for disease control. (C) 2008 Elsevier Inc. All rights reserved.
-
molecular cloning and characterization of a short type Peptidoglycan Recognition Protein cfpgrp s1 cdna from zhikong scallop chlamys farreri
Fish & Shellfish Immunology, 2007Co-Authors: Linsheng Song, Jianmin Zhao, Limei QiuAbstract:Peptidoglycan Recognition Protein (PGRP) specifically binds to Peptidoglycan and plays a crucial role in the innate immune responses as a pattern Recognition receptor (PRR). The cDNA of a short type PGRP was cloned from scallop Chlamys farreri (named CfPGRP-SI) by homology cloning with degenerate primers, and confirmed by virtual Northern blots. The full length of CfPGRP-SI cDNA was 1073 bp in length, including a 5 ' untranslated region (UTR) of 59 bp, a 3 ' UTR of 255 bp, and an open reading frame (ORF) of 759 bp encoding a polypeptide of 252 amino acids with an estimated molecular mass of 27.88 kDa and a predicted isoelectric point of 8.69. BLAST analysis revealed that CfPGRP-S1 shared high identities with other known PGRPs. A conserved PGRP domain and three zinc-binding sites were present at its C-terminus. The temporal expression of QPGRP-S1 gene in healthy, Vibrio anguillarum-challenged and Micrococcus lysodeikticus-challenged scallops was measured by RT-PCR analysis. The expression of CfPGRP-S1 was upregulated initially in the first 12 h or 24 h either by M. lysodeikticus or V. anguillarum challenge and reached the maximum level at 24 h or 36 h, then dropped progressively, and recovered to the original level as the stimulation decreased at 72 h. There was no significant difference between V. anguillarum and M. lysodeikticus challenge. The results indicated that the CfPGRP-S1 was a constitutive and inducible acute-phase Protein which was involved in the immune response against bacterial infection. (c) 2007 Elsevier Ltd. All rights reserved.
Pin Nie - One of the best experts on this subject based on the ideXlab platform.
-
functional characterization of a short Peptidoglycan Recognition Protein from chinese giant salamander andrias davidianus
Oncotarget, 2017Co-Authors: Shisi Ren, Pin Nie, Jun Zou, Qihuan Zhang, Zisheng Wang, Guo Qiao, Ming Xian ChangAbstract:Peptidoglycan (PGN) Recognition Proteins (PGRPs) are important pattern Recognition receptors (PRRs) involved in immune defense against bacterial infections. In this study, a short PGRP (termed AdPGRP-S1) was cloned and functionally characterized from Chinese giant salamander (Andrias davidianus), the largest extant urodela amphibian species. AdPGRP-S1 was 184 aa in length and shared 38.7%-54.9% sequence identities with other vertebrates' short PGRPs. It contained one typical PGRP domain at the C-terminal region and several conserved amino acid (aa) residues involved in amidase and PGN binding. AdPGRP-S1 was constitutively expressed in all tissues examined, with the highest expression level seen in spleen and intestine. It has been shown that AdPGRP-S1 could bind and degrade Lys-PGN and Dap-PGN. Further, AdPGRP-S1 had antibacterial activity against the Gram-negative bacteria, Edwardsiella tarda, and was able to trigger the activation of NF-κB signaling. These results demonstrated that AdPGRP-S1 possesses multiple functions in pathogen Recognition, mediating ceullular signaling, and initiating antibacterial response. This is the first functional study of a salamander PGRP, providing insight to further understand the functional evolution of verterbates' PGRPs.
-
functional characterization of a short Peptidoglycan Recognition Protein pgrp5 in grass carp ctenopharyngodon idella
Fish & Shellfish Immunology, 2013Co-Authors: Ming Xian Chang, Na Na Xue, Pin NieAbstract:Peptidoglycan Recognition Proteins (PGRPs), which are evolutionarily conserved from insects to mammals, recognize bacterial Peptidoglycan (PGN) and function in antibacterial innate immunity. In this study, a short-form PGRP, designated as gcPGRP5 was identified from grass carp Ctenopharyngodon idella. The deduced amino acid sequence of gcPGRP5 is composed of 180 residues with a conserved PGRP domain at the C-terminus. The gcPGRP5 gene consists of four exons and three introns, spacing approximately 2.3 kb in genomic sequence. Phylogenetic analysis demonstrated that the gcPGRP5 is clustered with other PGRP-S identified in teleost fish. The gcPGRP5 is constitutively expressed in all organs/tissues examined, and its expression was significantly induced in CIK cells treated with lipoteichoic acid (LTA), polyinosinic polycytidylic acid (Poly I:C) and PGN. Fluorescence analysis showed that gcPGRP5 is distributed in cytoplasm of CIK cells, and cell lysates from CIK cells transfected with pTurbo-gcPGRP5-GFP and ptGFP1-gcPGRP5 plasmids display the binding activity and Peptidoglycan-lytic amidase activity toward Lys-PGN from Staphylococcus aureus and Dap-PGN from Bacillus subtilis. Furthermore, heat-shock Protein70 (Hsp70), and MyD88, an adaptor molecule in Toll-like receptor pathway, had an increased expression in CIK cells overexpressed with gcPGRP5. It is thus indicated that gcPGRP5 exhibits amidase activity, and also possesses roles in anti-stress, and in Toll-like receptor signaling pathway. (C) 2013 Elsevier Ltd. All rights reserved.
-
zebrafish Peptidoglycan Recognition Protein sc zfpgrp sc mediates multiple intracellular signaling pathways
Fish & Shellfish Immunology, 2009Co-Authors: Ming Xian Chang, Yuqiong Wang, Pin NieAbstract:Insect PGRPs can function as bacterial Recognition molecules triggering proteolytic and/or signal transduction pathways, with the resultant production of antimicrobial peptides. To explore if zebrafish Peptidoglycan Recognition Protein SC (zfPGRP-SC) has such effects, RNA interference (siRNA) and high-density oligonucleotide microarray analysis were used to identify differentially expressed genes regulated by zfPGRP-SC. The mRNA levels for a set of genes involved in Toll-like receptor signaling pathway, such as TLRs, SARM, MyD88, TRAF6 and nuclear factor (NF)-kappa B2 (p100/p52), were examined by quantitative RT-PCR (QT-PCR). The results from the arrays and QT-PCR showed that the expression of 133 genes was involved in signal transduction pathways, which included Toll-like receptor signaling, Wnt signaling, BMP signaling, insulin receptor signaling, TGF-beta signaling, GPCR signaling, small GTPase signaling, second-messenger-mediated signaling, MAPK signaling, JAK/STAT signaling, apoptosis and anti-apoptosis signaling and other signaling cascades. These signaling pathways may connect with each other to form a complex network to regulate not just immune responses but also other processes such as development and apoptosis. When transiently over-expressed in HEK293T cells, zfPGRP-SC inhibited NF-kappa B activity with and without lipopolysacharide (LPS) stimulation. (C) 2008 Elsevier Ltd. All rights reserved.
-
rnai suppression of zebrafish Peptidoglycan Recognition Protein 6 zfpgrp6 mediated differentially expressed genes involved in toll like receptor signaling pathway and caused increased susceptibility to flavobacterium columnare
Veterinary Immunology and Immunopathology, 2008Co-Authors: Ming Xian Chang, Pin NieAbstract:In Drosophila, Toll signaling cascade, which resembles the mammalian Toll-like receptor (TLR)/IL-1R signaling pathways and regulates the expression of anti-microbial peptide genes, mainly relies on Peptidoglycan Recognition Proteins (PGRPs) for the detection of bacterial pathogens. To explore the effect of zebrafish Peptidoglycan Recognition Protein 6 (zfPGRP6) on Toll-like receptor signaling pathway, RNA interference (siRNA) and real time quantitative PCR (RQ-PCR) methods were used to identify differentially expressed genes regulated by zfPGRP6. The target genes included TLR2, TLR3, TLR5, TLR7, TLR8, IL1R, Sterile-alpha and Armadillo motif containing Protein (SARM), myeloid differentiation factor 88 (MyD88) and nuclear factor (NF)-kappa B2 (p100/p52). The results of RQ-PCR showed that RNAi-mediated Suppression of zfPGRP6 significantly down-regulated the expression of TLR2, TLR5, IL1R, SARM, MyD88 and p100/p52. The expression of beta-defensin-1 was also down-regulated in those embryos silenced by zfPGRP6. In challenge experiments to determine the anti-bacterial response to Gram-negative bacteria, RNAi knock-down of zfPGRP6 markedly increased susceptibility to Flavobacterium columnare. (C) 2008 Elsevier B.V. All rights reserved.
-
RNAi suppression of zebrafish Peptidoglycan Recognition Protein 6 (zfPGRP6) mediated differentially expressed genes involved in Toll-like receptor signaling pathway and caused increased susceptibility to Flavobacterium columnare.
Veterinary immunology and immunopathology, 2008Co-Authors: Ming Xian Chang, Pin NieAbstract:In Drosophila, Toll signaling cascade, which resembles the mammalian Toll-like receptor (TLR)/IL-1R signaling pathways and regulates the expression of anti-microbial peptide genes, mainly relies on Peptidoglycan Recognition Proteins (PGRPs) for the detection of bacterial pathogens. To explore the effect of zebrafish Peptidoglycan Recognition Protein 6 (zfPGRP6) on Toll-like receptor signaling pathway, RNA interference (siRNA) and real time quantitative PCR (RQ-PCR) methods were used to identify differentially expressed genes regulated by zfPGRP6. The target genes included TLR2, TLR3, TLR5, TLR7, TLR8, IL1R, Sterile-alpha and Armadillo motif containing Protein (SARM), myeloid differentiation factor 88 (MyD88) and nuclear factor (NF)-kappa B2 (p100/p52). The results of RQ-PCR showed that RNAi-mediated suppression of zfPGRP6 significantly down-regulated the expression of TLR2, TLR5, IL1R, SARM, MyD88 and p100/p52. The expression of beta-defensin-1 was also down-regulated in those embryos silenced by zfPGRP6. In challenge experiments to determine the anti-bacterial response to Gram-negative bacteria, RNAi knock-down of zfPGRP6 markedly increased susceptibility to Flavobacterium columnare.
Xiumei Wei - One of the best experts on this subject based on the ideXlab platform.
-
Peptidoglycan Recognition Protein of Solen grandis (SgPGRP-S1) mediates immune Recognition and bacteria clearance.
Fish & shellfish immunology, 2017Co-Authors: Xiumei Wei, Dinglong Yang, Tianyu Zhao, Hailin Jiang, Xiangquan Liu, Jialong YangAbstract:Peptidoglycan Recognition Proteins (PGRPs) are indispensable molecules in innate immunity due to their prominent function in sensing and eliminating invading microorganisms. In the present study, a short type PGRP from razor clam Solen grandis (SgPGRP-S1) was recombinantly expressed and purified to investigate its potential function in innate immunity. As a pattern Recognition receptor, recombinant SgPGRP-S1 (rSgPGRP-S1) specifically bind Lys-type and Dap-type Peptidoglycan in vitro, but not lipopolysaccharide or β-glucan. The Peptidoglycan binding ability of rSgPGRP-S1 resulted in significant agglutination activity against Gram-negative Escherichia coli and Listonella anguillarum, as well as Gram-positive Micrococcus luteus. Furthermore, rSgPGRP-S1 was bactericidal, significantly suppressing the growth of both E. coli and Gram-positive Staphylococcus aureus. The Protein also exhibited strong amidase activity and degraded bacterial Peptidoglycan in the presence of Zn2+, suggesting amidase activity might contribute to SgPGRP-S1 antibacterial activity. These results indicate SgPGRP-S1 is multifunctional in innate immunity, mediating both immune Recognition and bacteria elimination.
-
Peptidoglycan Recognition Protein of chlamys farreri cfpgrp s1 mediates immune defenses against bacterial infection
Developmental and Comparative Immunology, 2010Co-Authors: Jialong Yang, Limei Qiu, Huan Zhang, Wan Wang, Xiumei Wei, Lingling Wang, Linsheng SongAbstract:Peptidoglycan Recognition Protein (PGRP) is an essential molecule in innate immunity for both invertebrates and vertebrates, owing to its prominent ability in detecting and eliminating the invading bacteria. Several PGRPs have been identified from mollusk, but their functions and the underlined mechanism are still unclear. In the present study, the mRNA expression profiles, location, and possible functions of PGRP-S1 from Zhikong scallop Chlamys farreri (CfPG RP-St) were analyzed. The CfPGRP-S1 Protein located in the mantle, gill, kidney and gonad of the scallops. Its mRNA expression in hemocytes was up-regulated extremely after PGN stimulation (P < 0.01), while moderately after the stimulations of LPS (P < 0.01) and beta-glucan (P < 0.05). The recombinant Protein of CfPGRP-S1 (designated as rCfPGRP-S1) exhibited high affinity to PGN and moderate affinity to LPS, but it did not bind beta-glucan. Meanwhile, rCfPGRP-S1 also exhibited strong agglutination activity to Gram-positive bacteria Micrococcus luteus and Bacillus subtilis and weak activity to Gram-negative bacteria Escherichia coli. More importantly, rCfPGRP-S1 functioned as a bactericidal amidase to degrade PGN and strongly inhibit the growth of E. coli and Staphyloccocus aureus in the presence of Zn(2+). These results indicated that CfPGRP-S1 could not only serve as a pattern Recognition receptor recognizing bacterial PGN and LPS, but also function as a scavenger involved in eliminating response against the invaders. (C) 2010 Elsevier Ltd. All rights reserved.