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Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs.

ABSTRACT: A Streptococcus suis surface protein reacting with convalescent-phase sera from pigs clinically infected by S. suis type 2 was identified. The apparent 110-kDa protein, designated Sao, exhibits typical features of membrane-anchored surface proteins of gram-positive bacteria, such as a signal sequence and an LPVTG membrane anchor motif. In spite of high identity with the partially sequenced genomes of S. suis Canadian strain 89/1591 and European strain P1/7, Sao does not share significant homology with other known sequences. However, a conserved avirulence domain that is often found in plant pathogens has been detected. Electron microscopy using an Sao-specific antiserum has confirmed the surface location of the Sao protein on S. suis. The Sao-specific antibody reacts with cell lysates of 28 of 33 S. suis serotypes and 25 of 26 serotype 2 isolates in immunoblots, suggesting its high conservation in S. suis species. The immunization of piglets with recombinant Sao elicits a significant humoral antibody response. However, the antibody response is not reflected in protection of pigs that are intratracheally challenged with a virulent strain in our conventional vaccination model.

SUBMITTER: Li Y

PROVIDER: S-EPMC1346615 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature

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Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs.

Li Yuanyi Y Martinez Gabriela G Gottschalk Marcelo M Lacouture Sonia S Willson Philip P Dubreuil J Daniel JD Jacques Mario M Harel Josee J

Infection and immunity 20060101 1

A Streptococcus suis surface protein reacting with convalescent-phase sera from pigs clinically infected by S. suis type 2 was identified. The apparent 110-kDa protein, designated Sao, exhibits typical features of membrane-anchored surface proteins of gram-positive bacteria, such as a signal sequence and an LPVTG membrane anchor motif. In spite of high identity with the partially sequenced genomes of S. suis Canadian strain 89/1591 and European strain P1/7, Sao does not share significant homolog ...[more]

PMID: 16368985

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Project description:In our continued effort to search for a Streptococcus suis protein(s) that can serve as a vaccine candidate or a diagnostic reagent, we constructed and screened a gene library with a polyclonal antibody raised against the whole-cell protein of S. suis type 2. A clone that reacted with the antibody was identified and characterized. Analysis revealed that the gene encoding the protein is localized within a 2.0-kbp EcoRI DNA fragment. The nucleotide sequence contained an open reading frame that encoded a polypeptide of 445 amino acid residues with a calculated molecular mass of 46.4 kDa. By in vitro protein synthesis and Western blot experiments, the protein exhibited an electrophoretic mobility of approximately 38 kDa. At the amino acid level the deduced primary sequence shared homology with sequences of unknown function from Streptococcus pneumoniae (89%), Streptococcus mutans (86%), Lactococcus lactis (80%), Listeria monocytogenes (74%), and Clostridium perfringens (64%). Except for strains of serotypes 20, 26, 32, and 33, Southern hybridization analysis revealed the presence of the gene in strains of other S. suis serotypes and demonstrated restriction fragment length differences caused by a point mutation in the EcoRI recognition sequence. We confirmed expression of the 38-kDa protein in the hybridization-positive isolates using specific antiserum against the purified protein. The recombinant protein was reactive with serum from pigs experimentally infected with virulent strains of S. suis type 2, suggesting that the protein is immunogenic and may serve as an antigen of diagnostic importance for the detection of most S. suis infections. Pigs immunized with the recombinant 38-kDa protein mounted antibody responses to the protein and were completely protected against challenge with a strain of a homologous serotype, the wild-type virulent strain of S. suis type 2, suggesting that it may be a good candidate for the development of a vaccine that can be used as protection against S. suis infection. Analysis of the cellular fractions of the bacterium by Western blotting revealed that the protein was present in the surface and cell wall extracts. The functional role of the protein with respect to pathogenesis and whether antibodies against the antigen confer protective immunity against diseases caused by strains of other pathogenic S. suis capsular types remains to be determined.

Project description:BackgroundProphylaxis and treatment of emerging zoonotic Streptococcus suis infection in agricultural and healthcare settings mainly rely on antibiotics. However, continued use of antibiotics contributing to emergence and widespread of antibiotic resistant S. suis becomes a significant challenge in many endemic countries, including Thailand. Meanwhile, the knowledge of antibiotic susceptibility patterns of bacterial pathogens is required for overcoming the antimicrobial resistance problem, the information of antibiotic susceptibility of S. suis strains isolated in Thailand remains limited. This study aims to assess the susceptibility of Thai-isolated S. suis strains to different antibiotic classes in order to gain an insight into the distribution of antibiotic-resistant patterns of S. suis strains in different regions of Thailand.ResultsThis study revealed the antimicrobial resistance and multidrug resistance of 262 S. suis strains isolated in different regions of Thailand. Susceptibility testing indicated widespread resistance to macrolides and tetracyclines of S. suis strains in the country. Beta-lactam antibiotic drugs (including cefotaxime and ceftiofur), vancomycin, chloramphenicol, as well as florfenicol were potentially the most effective therapeutic drugs for the treatment of S. suis infection in both pigs and humans. High prevalence of intermediate susceptibility of S. suis isolated from asymptomatic pigs for penicillin G, gentamicin, enrofloxacin, and norfloxacin could be the premise of the emergence of S. suis antibiotic resistance. Resistance was also found in S. suis strains isolated from asymptomatic pigs indicating that they could act as reservoirs of antibiotic resistance genes.ConclusionsTo the best of our knowledge, this is the first report on antimicrobial resistance of a large collection of S. suis strains isolated from pigs and humans in Thailand. It revealed the multidrug resistance of S. suis strains in pigs and humans. The information gained from this study raises an awareness and encourage best practices of appropriate antibiotic drug prescribing and use among human health and agriculture sectors.

Dataset Information

Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs.

Publications

Identification of a surface protein of Streptococcus suis and evaluation of its immunogenic and protective capacity in pigs.

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