Characterization of the domain of fibronectin-binding protein I of Streptococcus pyogenes responsible for elicitation of a protective immune response.

Citation data:

Infection and immunity, ISSN: 0019-9567, Vol: 69, Issue: 1, Page: 622-5

Publication Year:
2001
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Citations 32
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Repository URL:
https://ro.uow.edu.au/smhpapers/1962
PMID:
11119566
DOI:
10.1128/iai.69.1.622-625.2001
PMCID:
PMC97932; 97932
Author(s):
Schulze, Kai; Medina, Eva; Talay, Susanne R; Towers, Rebecca J; Chhatwal, Gursharan S; Guzman, Carlos A
Publisher(s):
American Society for Microbiology
Tags:
Immunology and Microbiology; Medicine; immune; fibronectin; domain; protective; elicitation; responsible; pyogenes; streptococcus; i; protein; response; binding; characterization; Medicine and Health Sciences; Social and Behavioral Sciences
article description
Fibronectin-binding protein I (SfbI) represents a major adhesin of Streptococcus pyogenes. Mice were intranasally immunized with recombinant proteins spanning different portions of SfbI to identify the minimal fragment able to elicit a protective response against a lethal challenge with S. pyogenes. The strongest cellular responses and the highest levels of antigen-specific secretory immunoglobulin A (IgA) were detected in mice immunized with the fibronectin-binding region of SfbI. In contrast, animals vaccinated with a polypeptide spanning the aromatic and proline-rich regions showed the highest titers and fastest IgG response in serum. Vaccination with either SfbI without a membrane anchor and signal peptide or a polypeptide encompassing its fibronectin-binding regions resulted in efficient protection against heterologous challenge (60% and 80%, respectively), whereas the use of a polypeptide lacking this region conferred marginal protection (10%) with respect to the control group (0%). These results demonstrate that the fibronectin-binding region of SfbI is a promising candidate antigen for developing anti-S. pyogenes vaccines.