Domains of group A streptococcal M protein that confer resistance to phagocytosis, opsonization and protection: implications for vaccine development.

Authors

Jason D. McArthur, University of WollongongFollow
Mark J. Walker, University of WollongongFollow

RIS ID

17280

Publication Details

This article was originally published as McArthur, JD and Walker, MJ, Domains of group A streptococcal M protein that confer resistance to phagocytosis, opsonization and protection: implications for vaccine development, Molecular Microbiology, 59(1), 2006, 1-4.

Abstract

Streptococcus pyogenes (group A streptococcus) colonises skin and throat tissues resulting in a range of benign and serious human diseases. Opsonisation and phagocytosis are important defence mechanisms employed by the host to destroy group A streptococci. Antisera against the cell-surface M protein, of which over 150 different types have been identified, are opsonic and contribute to disease protection . In this issue of Molecular Microbiology, Sandin and colleagues have comprehensively analysed the regions of M5 protein that contribute to phagocytosis resistance and opsonisation. Human plasma proteins bound to M5 protein B- and C-repeats were shown to block opsonisation, an observation that needs to be carefully considered for the development of M protein-derived vaccines. Whilst safe and efficacious human group A streptococcal vaccines are not commercially available, candidate M protein-derived vaccines have shown promise in murine vaccine models and a recent phase 1 human clinical trial.