Complementarity‐determining region 2 is implicated in the binding of staphylococcal protein A to human immunoglobulin VHIII variable regions Academic Article uri icon

Overview

MeSH Major

  • Immunoglobulin Variable Region
  • Staphylococcal Protein A

abstract

  • Staphylococcal protein A (SPA) has two distinct binding sites on human immunoglobulins. In addition to binding to the Fc region of most IgG molecules, an "alternative" binding site has been localized to the Fab region of human immunoglobulins encoded by heavy chain variable gene segments belonging to the VHIII family. Comparison of amino acid sequences of closely related SPA-binding and -non-binding proteins suggested that VHIII-specific residues in the second complementarity-determining region (CDR2) were likely responsible for SPA binding activity. Site-directed mutagenesis of a single amino acid residue in CDR2 converted an IgM rheumatoid factor which did not bind SPA to an SPA binder. These findings, therefore, locate a critical site involved in SPA binding to the CDR2 of human immunoglobulins encoded by VHIII family gene segments.

publication date

  • January 1993

Research

keywords

  • Academic Article

Identity

Language

  • eng

Digital Object Identifier (DOI)

  • 10.1002/eji.1830231044

PubMed ID

  • 8405066

Additional Document Info

start page

  • 2682

end page

  • 6

volume

  • 23

number

  • 10