M protein (Streptococcus)
Viruses, parasites and bacteria are covered in protein and sugar molecules that help them gain entry into a host by counteracting the host's defences. One such molecule is the M protein produced by certain streptococcal bacteria. M proteins embody a motif that is now known to be shared by many Gram-positive bacterial surface proteins. The motif includes a conserved pentapeptide LPXTG, which precedes a hydrophobic C-terminal membrane anchor, which itself precedes a cluster of basic residues.
M protein is strongly anti-phagocytic and is a major virulence factor. It binds to serum factor H, destroying C3-convertase and preventing opsonization by C3b. However plasma B cells can generate antibodies against M protein which will help in opsonization and further the destruction of the microorganism by the macrophages and neutrophilis. Cross-reactivity of anti-M protein antibodies with heart muscle is the basis for rheumatic fever.
It was originally identified by Rebecca Lancefield, who also formulated the Lancefield classification system for streptococcal bacteria. Bacteria like S. pyogenes, which possess M protein are classified in group A of the Lancefield system.
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- Fischetti VA, Pancholi V, Schneewind O (September 1990). "Conservation of a pentapeptide sequence in the anchor region of surface proteins from gram-positive cocci". Mol. Microbiol. 4 (9): 1603–5. doi:10.1111/j.1365-2958.1990.tb02072.x. PMID 2287281.
- "Streptococcal M protein: molecular design and biological behavior.". Retrieved 2009-06-21.
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