ArticleCurrent microbiology2011
Comparative proteomic analyses of Streptococcus suis serotype 2 cell wall-associated proteins.
Article in Current microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Unlocking the Secrets of Streptococcus suis: A peptidomics comparison of virulent and non-virulent serotypes 2, 14, 18, and 19.PloS one · 2023Article
- The identification of two M20B family peptidases required for full virulence inFrontiers in cellular and infection microbiology · 2023Article
- Investigation into the role of catabolite control protein A in the metabolic regulation ofExperimental and therapeutic medicine · 2015Article
- Candidate proteomic biomarkers for three genogroups of the swine pathogen Streptococcus suis serotype 2.BMC microbiology · 2015Article
- Mass Spectrometric Analysis of Whole Secretome and Amylase-precipitated Secretome Proteins fromJournal of proteomics & bioinformatics · 2014Article
- Catabolite control protein A is an important regulator of metabolism inBiomedical reports · 2014Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Streptococcus suis serotype 2 (SS2) is a zoonotic pathogen that is distributed throughout the world. Virulence factors and/or markers of the virulent serotype 2 strains have not been fully identified. In this study a simple, rapid, and non-destructive method was used to extract cell wall-associated proteins from SS2 strains. Two virulent strains were compared with one avirulent strain by 2-dimensional electrophoresis (2DE). When the results of the 2DE analyses were combined with the results of mass spectrometry analyses, a total of 40 unique proteins were identified, including 26 antigens (2DE immunoblotting was used as a preliminary study). In addition to a known virulence factor, muramidase-released protein, two new proteins, catabolite control protein A and leucyl aminopeptidase, and nine potential virulence factors were also identified. The formers may be a potential virulence regulator or drug target, and the latter contains plasminogen-binding proteins and molecular chaperones. Our results complemented previous immunoproteomics studies of SS2 strains.
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