<i>Streptococcus suis</i>Enolase Functions as a Protective Antigen Displayed on the Bacterial Cell Surface

Feng, Youjun; Pan, Xiuzhen; Sun, Wen; Wang, Changjun; Zhang, Huimin; Li, Xianfu; Ma, Ying; Shao, Zhu‐Qing; Ge, Junchao; Feng, Zijian; Gao, George F.; Tang, Jiaqi

doi:10.1086/644602

Cited by 129 publications

(110 citation statements)

References 41 publications

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“…We used B. subtilis enolase (EnoBs) as the model system. Enolase is a key glycolytic enzyme and has been reported as a plasminogen-binding protein that is displayed on the bacterial cell surface (1,16). Using the crystal structure of Enterococcus hirae enolase as a template, a predicted threedimensional (3D) molecular structure was generated by SwissModel (Swiss-Prot database entry no.…”

Section: Signal-less Protein Secretion Is Not Mediated Significantly mentioning

confidence: 99%

Nonclassical Protein Secretion by Bacillus subtilis in the Stationary Phase Is Not Due to Cell Lysis

Yang¹,

Ewis²,

Zhang³

et al. 2011

Journal of Bacteriology

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The carboxylesterase Est55 has been cloned and expressed in Bacillus subtilis strains. Est55, which lacks a classical, cleavable N-terminal signal sequence, was found to be secreted during the stationary phase of growth such that there is more Est55 in the medium than inside the cells. Several cytoplasmic proteins were also secreted in large amounts during late stationary phase, indicating that secretion in B. subtilis is not unique to Est55. These proteins, which all have defined cytoplasmic functions, include GroEL, DnaK, enolase, pyruvate dehydrogenase subunits PdhB and PdhD, and SodA. The release of Est55 and those proteins into the growth medium is not due to gross cell lysis, a conclusion that is supported by several lines of evidence: constant cell density and secretion in the presence of chloramphenicol, constant viability count, the absence of EF-Tu and SecA in the culture medium, and the lack of effect of autolysin-deficient mutants. The shedding of these proteins by membrane vesicles into the medium is minimal. More importantly, we have identified a hydrophobic ␣-helical domain within enolase that contributes to its secretion. Thus, upon the genetic deletion or replacement of a potential membrane-embedding domain, the secretion of plasmid gene-encoded mutant enolase is totally blocked, while the wild-type chromosomal enolase is secreted normally in the same cultures during the stationary phase, indicating differential specificity. We conclude that the secretion of Est55 and several cytoplasmic proteins without signal peptides in B. subtilis is a general phenomenon and is not a consequence of cell lysis or membrane shedding; instead, their secretion is through a process(es) in which protein domain structure plays a contributing factor.Bacillus subtilis secretes large amounts of proteins into the growth medium (43). Of the known secretory pathways in B. subtilis, the majority of proteins are exported from the cytoplasm by the Sec-dependent pathway, through which secretory proteins are synthesized as precursors with typical cleavable N-terminal signal peptides (3, 36). Fewer proteins are released into the medium via the cleavable twin-arginine translocation (TAT) system (39). Still other proteins are exported into the medium via ATP-binding cassette transporters, a dedicated pseudopilin export pathway, a competence development system or an ESAT-6 (Mycobacterium tuberculosis early secreted antigenic target of 6 kDa)-like system (31).The genome of B. subtilis 168 is 4,215 kbp in length and contains about 4,100 genes that are predicted to include over 250 extracellular proteins; the majority of these proteins are secreted through the aforementioned pathways (3, 18). However, proteomic studies have revealed that genome-based predictions reflect only 50% of the actual composition of the extracellular proteome. This significant discrepancy is mainly due to the difficulties in the prediction of extracellular proteins lacking signal peptides (including cytoplasmic proteins) and lipoproteins (3, 18). These findin...

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Section: Signal-less Protein Secretion Is Not Mediated Significantly mentioning

confidence: 99%

Nonclassical Protein Secretion by Bacillus subtilis in the Stationary Phase Is Not Due to Cell Lysis

Yang¹,

Ewis²,

Zhang³

et al. 2011

Journal of Bacteriology

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“…Thus, parasite enolase could play an essential role in energy metabolism of parasites, growth and development of the parasite stages and virulence of the parasite. Enolase was found to be immunogenic in Streptococcus suis (Feng et al, 2009), Candida albicans (Eroles et al, 1997), Brugia malayi (Wongkamchai et al, 2011), Trichomonas vaginalis (Mundodi et al, 2008) and Plasmodium falciparum (Pal-Bhowmick et al, 2007). pVAXEnol, a DNA vaccine, triggered Th1/Th2 mixed response in mice against A. suum larvae (Chen et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Comparative immunoprophylactic efficacy of Haemonchus contortus recombinant enolase (rHcENO) and Con A purified native glycoproteins in sheep

Kalyanasundaram

Jawahar

Ilangopathy

et al. 2015

Experimental Parasitology

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“…Similarly, phosphopyruvate hydratase (enolase) is a surface protein demonstrated previously to directly participate in microbial virulence by facilitating pathogen dissemination via interaction with host factors. It has been shown to be a strong plasmin(ogen) binding protein on the surface of pathogenic Streptococci, B. anthracis and Borrelia burgdorferi [42e44] and functions as a protective antigen displayed on the bacterial cell surface in Streptococcus suis [45]. Our study highlights major proteins that possibly contribute to C. perfringens colonisation and pathogenesis and warrants further investigation with respect to their expression and role in actual disease settings.…”

Section: Differential Protein Expression Under Host-simulated Conditionsmentioning

confidence: 75%

Comparative analysis of extractable proteins from Clostridium perfringens type A and type C strains showing varying degree of virulence

et al. 2015

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Streptococcus suisEnolase Functions as a Protective Antigen Displayed on the Bacterial Cell Surface

Abstract: We conclude that S. suis enolase functions as a protective antigen displayed on the bacterial cell surface and that it can be used to develop new strategies to combat SS2 infections.

Cited by 129 publications

References 41 publications

Nonclassical Protein Secretion by Bacillus subtilis in the Stationary Phase Is Not Due to Cell Lysis

Nonclassical Protein Secretion by Bacillus subtilis in the Stationary Phase Is Not Due to Cell Lysis

Comparative immunoprophylactic efficacy of Haemonchus contortus recombinant enolase (rHcENO) and Con A purified native glycoproteins in sheep

Comparative analysis of extractable proteins from Clostridium perfringens type A and type C strains showing varying degree of virulence

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