Sequence analysis and characterization of a novel fibronectin-binding repeat domain from the surface of Streptococcus pneumoniae

Daniela Bumbaca, James E Littlejohn, Hannah Nayakanti, Daniel J. Rigden, Michael Y. Galperin, Mark J. Jedrzejas

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Streptococcus pneumoniae open reading frame SP0082 encodes a surface protein that contains four copies of a novel conserved repeat domain that bears no significant sequence similarity to proteins of known function. Homologous sequences from other streptococci contain two to six of these repeats, designated the SSURE (streptococcal surface repeat) domain. To investigate the functional role(s) of this domain, the third SSURE repeat of SP0082 sequence has been expressed in Escherichia coli, purified to homogeneity and characterized by biochemical and immunological methods. The expressed protein fragment was found to bind to fibronectin, but not to collagen or submaxillary mucin. Anti-SSURE antibodies recognized the corresponding protein on the surface of pneumococcal cells. These data identify S. pneumoniae SP0082 protein and its homologs in other streptococci as fibronectin-binding surface adhesins. The SSURE domain is likely to contain a novel protein fold, which was tentatively modeled using ab initio modeling methods.

Original languageEnglish (US)
Pages (from-to)341-356
Number of pages16
JournalOMICS A Journal of Integrative Biology
Volume8
Issue number4
StatePublished - 2004
Externally publishedYes

    Fingerprint

ASJC Scopus subject areas

  • Biotechnology
  • Genetics

Cite this

Bumbaca, D., Littlejohn, J. E., Nayakanti, H., Rigden, D. J., Galperin, M. Y., & Jedrzejas, M. J. (2004). Sequence analysis and characterization of a novel fibronectin-binding repeat domain from the surface of Streptococcus pneumoniae. OMICS A Journal of Integrative Biology, 8(4), 341-356.