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Application of immunoproteomics to analysis of post‐translational processing of the antiphagocytic M protein of Streptococcus
Author(s) -
Romer Terence G.,
Boyle Michael D. P.
Publication year - 2003
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200390005
Subject(s) - streptococcus pyogenes , protease , virulence , pathogen , monoclonal antibody , proteomics , microbiology and biotechnology , streptococcus suis , myeloma protein , streptococcus , antibody , chemistry , biology , bacteria , biochemistry , staphylococcus aureus , immunology , enzyme , gene , genetics
Post‐translational modification of the antiphagocytic M1 protein of Streptococcus pyogenes can influence its binding properties for human immunoglobulin G subclasses and its invasive potential. Current methods of monitoring this modification event involve N ‐terminal sequencing and are cumbersome, slow and not amenable to routine analysis. In this study we demonstrate that surface enhanced laser desorption/ionization‐time of flight mass spectrometry can be used to monitor modification of the M1 protein by the secreted bacterial cysteine protease, SpeB. This method, when combined with a specific antibody capture step provides a specific, rapid and sensitive assay for key virulence factors of the important human pathogen Streptococcus pyogenes .