Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2

Zhang, Anding; Chen, Bo; Mu, Xiaofeng; Li, Ran; Pei, Zhihua; Zhao, Yi; Chen, Huanchun; Jin, Meilin

doi:10.1016/j.vaccine.2008.12.047

Cited by 88 publications

(71 citation statements)

References 27 publications

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“…An important inhibition of C. albicans adhesion was also observed by Segal and Savage after pretreatment of mice duodenal disks with chitin soluble extracts (Segal and Savage, 1986). Our data are in line with a previous study reporting a decrease in adhesion of S. suis , serotype two, to epithelial cells exposed to recombinant enolase (Zhang et al, 2009). Altogether these results suggest that enolase directly interacted to specific epithelial receptors on mice intestinal disks, thus inhibiting C. albicans adhesion.…”

Section: Discussionsupporting

confidence: 94%

Extracellular enolase of Candida albicans is involved in colonization of mammalian intestinal epithelium

Silva

Padovan

Pimenta

et al. 2014

Front. Cell. Infect. Microbiol.

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Enolase is secreted by Candida albicans and is present in its biofilms although its extracellular function is unknown. Here we show that extracellular enolase mediates the colonization of small intestine mucosa by C. albicans. Assays using intestinal mucosa disks show that C. albicans adhesion is inhibited, in a dose dependent mode, either by pretreatment of intestinal epithelium mucosa disks with recombinant C. albicans enolase (70% at 0.5 mg/ml enolase) or by pretreatment of C. albicans yeasts with anti-enolase antibodies (48% with 20 μg antiserum). Also using flow cytometry, immunoblots of conditioned media and confocal microscopy we demonstrate that enolase is present in biofilms and that the extracellular enolase is not an artifact due to cell lysis, but must represent functional secretion of a stable form. This is the first direct evidence that C. albicans' extracellular enolase mediates colonization on its primary translocation site. Also, because enolase is encoded by a single locus in C. albicans, its dual role peptide, as glycolytic enzyme and extracellular peptide, is a remarkable example of gene sharing in fungi.

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Section: Discussionsupporting

confidence: 94%

Extracellular enolase of Candida albicans is involved in colonization of mammalian intestinal epithelium

Silva

Padovan

Pimenta

et al. 2014

Front. Cell. Infect. Microbiol.

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“…Si et al 127 demonstrated that glutamine synthetase, the glnA- encoding product, is associated with S. suis virulence using a mouse model. We and two other research groups 96 , 129 , 143 have reported that S. suis enolase acts as an octamer, 144 and can exported to the bacterial surface with capability of binding to host fibronectin, indicating its possible role in crosstalk between pathogen and host. However, the protective efficiency of recombinant enolase with different bacterial origins does not seem consistent 96 , 129 , 130 .…”

Section: Molecular Mechanism For Streptococcus Suis Infectionmentioning

confidence: 76%

“…Among them, eight enzymes are proposed to be virulence factors by Wilson et al 100 using the system of signature-tagged mutagenesis (Table 2). Four of them are generally regarded as enzymes of central metabolism, which separately correspond to (1) GlnA, glutamine synthetase, 127 (2) Gdh, glutamate dehydrogenase, 128 (3) enolase catalyzing dehydration of 2-phosphoglycerate to phosphor-enolpyruvate, 96 , 129 , 130 and (4) Impdh, inosine 5-monophosphate dehydrogenase 131 . Five of these enzymes are directly or indirectly related to synthesis and/or modification of bacterial surface structure, including DltA, an enzyme catalyzing lipoteichoic d -alanylation, 132 PgdA, peptidoglycan N-acetylglucosamine deacetylase, 133 ApuA, a bifunctional amylopullulanase, 134 DPP IV, di-peptidyl peptidase IV, 135 and sortase A, a transpeptidase 136 , 137 .…”

Section: Molecular Mechanism For Streptococcus Suis Infectionmentioning

confidence: 99%

Streptococcus suisinfection

et al. 2014

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Streptococcus suis (S. suis) is a family of pathogenic gram-positive bacterial strains that represents a primary health problem in the swine industry worldwide. S. suis is also an emerging zoonotic pathogen that causes severe human infections clinically featuring with varied diseases/syndromes (such as meningitis, septicemia, and arthritis). Over the past few decades, continued efforts have made significant progress toward better understanding this zoonotic infectious entity, contributing in part to the elucidation of the molecular mechanism underlying its high pathogenicity. This review is aimed at presenting an updated overview of this pathogen from the perspective of molecular epidemiology, clinical diagnosis and typing, virulence mechanism, and protective antigens contributing to its zoonosis.

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“…Moreover, the antibody against Enolase could decrease the survival of SS2 in human blood. Consisting with that, Enolase was reported as a surface antigen with significant protection against serotype 2 and 7 intra-peritoneal challenges in BALB/c mice (Zhang et al, 2009). …”

Section: Discussionmentioning

confidence: 95%

Proteomics identification of novel fibrinogen-binding proteins of Streptococcus suis contributing to antiphagocytosis

Pian

Wang

Liu

et al. 2015

Front. Cell. Infect. Microbiol.

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Streptococcus suis serotype 2 (SS2) induced sepsis and meningitis are often accompanied by bacteremia. However, the mechanism whereby it helps S. suis to evade PMN-mediated phagocytosis remain unclear. Because of the central roles of bacteria-human fibrinogen (hFg) interaction in innate immunity, here, a proteomics based Far-western blotting (PBFWB) was developed to identify the fibrinogen-binding surface proteins of S. suis (SsFBPs) on a large-scale. And then thirteen potential SsFBPs were identified by PBFWB and we selected seven potential surface proteins to further confirm their binding ability to hFg, of which the gene mutant strains of MRP displayed significantly decrease in binding to immobilized hFg. Additionally, the polyclonal antibodies against Enolase were found to significantly inhibit the binding of SS2 to hFg. Strikingly, MRP and Enolase were found to improve the antiphagocytic ability of SS2 to PMNs by interacting with hFg and enhance the survival of SS2 in human blood. Taken together, the PBFWB method provides useful clues to the bacteria-host interactions. These studies firstly disclose MRP and Enolase were involved in immune evasion of SS2 at least in part by binding to Fg, which make them potential targets for therapies for SS2 infection.

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Identification and characterization of a novel protective antigen, Enolase of Streptococcus suis serotype 2

Cited by 88 publications

References 27 publications

Extracellular enolase of Candida albicans is involved in colonization of mammalian intestinal epithelium

Extracellular enolase of Candida albicans is involved in colonization of mammalian intestinal epithelium

Streptococcus suisinfection

Proteomics identification of novel fibrinogen-binding proteins of Streptococcus suis contributing to antiphagocytosis

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