Immunoglobulin-binding FcrA and Enn Proteins and M Proteins of Group A Streptococci Evolved Independently from a Common Ancestral Protein

Overview

Journal Med Microbiol Immunol

Specialty Allergy & Immunology

Date 1994 Feb 1

PMID 8202029

Citations 7

Authors

A Podbielski

P P Cleary

Affiliations

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Abstract

Significant sequence homology between M proteins and immunoglobulin (Ig)-binding proteins of group A streptococci suggests that these proteins arose by gene duplication followed by the development of functional diversity due to mutations and intragenic recombinations. The deduced sequence of multiple Ig-binding proteins and M proteins were compared to distinguish between two evolutionary models. Did these functionally distinct genes originate in the distant past from duplication of a common ancestral gene and then functionally evolve independently or did they evolve more recently, one from the other by duplication of a fixed gene? Multiple alignments of conserved sequences of these proteins are consistent with the former hypothesis. Comparison of N termini of Ig-binding proteins revealed less diversity than that of the M proteins' N termini, suggesting that these proteins are under less selective pressure to change.

Citing Articles

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Protective immunogenicity of group A streptococcal M-related proteins.

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M-protein and other intrinsic virulence factors of Streptococcus pyogenes are encoded on an ancient pathogenicity island.

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