Domain structure of the Staphylococcus aureus collagen adhesin

Biochemistry. 1998 Nov 3;37(44):15423-33. doi: 10.1021/bi981773r.


Sequence analysis of surface proteins from Gram-positive bacteria indicates a composite organization consisting of unique and repeated segments. Thus, these proteins may contain discrete domains that could fold independently. In this paper, we have used a panel of biophysical methods, including gel permeation chromatography, analytical ultracentrifugation, circular dichroism, and fluorescence spectroscopy, to analyze the structural organization of the Staphylococcus aureus collagen adhesin, CNA. Our results indicate that the structure, function, and folding of the ligand-binding domain (A) are not affected by the presence or absence of the other major domain (B). In addition, little or no interaction is observed between the nearly identical repeat units within the B domain. We propose that CNA is indeed a mosaic protein in which the different domains previously indicated by sequence analysis operate independently.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adhesins, Bacterial / chemistry*
  • Adhesins, Bacterial / genetics
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Circular Dichroism
  • Collagen / chemistry*
  • Collagen / genetics
  • Dimerization
  • Models, Molecular
  • Molecular Mimicry
  • Protein Structure, Tertiary*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Repetitive Sequences, Amino Acid
  • Staphylococcus aureus / chemistry*


  • Adhesins, Bacterial
  • Bacterial Proteins
  • Recombinant Proteins
  • adhesin, Staphylococcus aureus
  • Collagen