| Literature DB >> 17535300 |
William P McArthur1, Nikki R Rhodin, Trevor B Seifert, Monika W Oli, Rebekah A Robinette, Donald R Demuth, L Jeannine Brady.
Abstract
Sequences contributing to epitopes recognized by a panel of monoclonal antibodies (mAbs) against the Streptococcus mutans surface protein P1 were delineated by Western blot and enzyme-linked immunosorbent assay using a battery of deletion constructs and recombinant polypeptides. mAbs that recognize complex discontinuous epitopes reconstituted by combining the alanine-rich and proline-rich repeat domains and varying degrees of flanking sequence were identified as well as mAbs that bound epitopes contained within contiguous segments of P1. Cross-reactivity with SspA and SspB from Streptococcus gordonii is also reported. This information enables insight into the structure and function of a streptococcal adhesin and its correlates of protection and furthers our understanding of the immunomodulatory and bacterial-adherence inhibition activities of anti-P1 mAbs.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17535300 DOI: 10.1111/j.1574-695X.2007.00260.x
Source DB: PubMed Journal: FEMS Immunol Med Microbiol ISSN: 0928-8244