Mapping the Ligand-Binding Region of Borrelia burgdorferi Fibronectin-Binding Protein BBK32
AUTOR(ES)
Probert, William S.
FONTE
American Society for Microbiology
RESUMO
The cellular attachment and entry of pathogenic microorganisms can be facilitated by the expression of microbial adhesins that bind fibronectin. We have previously described a Borrelia burgdorferi gene, bbk32, that encodes a 47-kDa fibronectin-binding protein. In this study, the ligand-binding region of BBK32 from B. burgdorferi isolate B31 was localized to 32 amino acids. The bbk32 gene was cloned and sequenced from three additional B. burgdorferi isolates representing different genospecies of B. burgdorferi sensu lato. All four bbk32 genes encoded proteins having fibronectin-binding activity when expressed in Escherichia coli, and the deduced proteins shared 81 to 91% amino acid sequence identity within the ligand-binding domain. In addition, the ligand-binding region of BBK32 was found to share sequence homology with a fibronectin-binding peptide defined for protein F1 of Streptococcus pyogenes. The structural and functional similarity between the ligand-binding region of BBK32 and the UR region of protein F1 suggests a common mechanism of cellular adhesion and entry for B. burgdorferi and S. pyogenes.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=98480Documentos Relacionados
- Ligand-binding and heterodimerization activities of a conserved region in the ligand-binding domain of the thyroid hormone receptor.
- Fibronectin-binding protein of Streptococcus equi subsp. zooepidemicus.
- Isolation and characterization of fibronectin-binding sites of Borrelia garinii N34.
- Treponema pallidum Fibronectin-Binding Proteins
- Identification of a Fibronectin-Binding Protein from Staphylococcus epidermidis
