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Protein F2, a novel fibronectin‐binding protein from Streptococcus pyogenes , possesses two binding domains
Author(s) -
Jaffe Joseph,
NatansonYaron Shira,
Caparon Michael G.,
Hanski Emanuel
Publication year - 1996
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1996.6331356.x
Subject(s) - biology , binding protein , streptococcus pyogenes , bacterial adhesin , protein g , dna binding protein , gene , plasma protein binding , retinoblastoma like protein 1 , binding domain , biochemistry , microbiology and biotechnology , amino acid , protein a/g , hspa2 , binding site , peptide sequence , genetics , bacteria , escherichia coli , recombinant dna , transcription factor , antibody , staphylococcus aureus , fusion protein
Binding of the group A streptococcus (GAS) to respiratory epithelium is mediated by the fibronectin (Fn)‐binding adhesin, protein F1. Previous studies have suggested that certain GAS strains express Fn‐binding proteins that are different from protein F1. In this study, we have cloned, sequenced, and characterized a gene ( prtF2 ) from GAS strain 100076 encoding a novel Fn‐binding protein, termed protein F2. Insertional inactivation of prtF2 in strain 100076 abolishes its high‐affinity Fn binding. prtF2 ‐related genes exist in most GAS strains that lack prtF1 (encoding protein F1) but bind Fn with high affinity. These observations suggest that protein F2 is a major Fn‐binding protein in GAS. Protein F2 is highly homologous to Fn‐binding proteins from Streptococcus dysgalactiae and Strep‐tococcus equisimilis , particularly in its carboxy‐terminal portion. Two domains are responsible for Fn binding by protein F2. One domain (FBRD) consists of three consecutive repeats, whereas the other domain (UFBD) resides on a non‐repeated stretch of approximately 100 amino acids and is located 100 amino acids amino‐terminal of FBRD. Each of these domains is capable of binding Fn when expressed as a separate protein. In strain 100076, protein F2 activity is regulated in response to alterations in the concentration of atmospheric oxygen.