Contribution of the Alanine-Rich Region of Streptococcus mutans P1 to Antigenicity, Surface Expression, and Interaction with the Proline-Rich Repeat Domain

AUTOR(ES)

Seifert, Trevor B.

FONTE

American Society for Microbiology

RESUMO

Streptococcus mutans is considered to be the major etiologic agent of human dental caries. Attachment of S. mutans to the tooth surface is required for the development of caries and is mediated, in part, by the 185-kDa surface protein variously known as antigen I/II, PAc, and P1. Such proteins are expressed by nearly all species of oral streptococci. Characteristics of P1 include an alanine-rich repeat region and a centrally located proline-rich repeat region. The proline-rich region of P1 has been shown to be important for the translational stability and translocation of P1 through the bacterial membrane. We show here that (i) several anti-P1 monoclonal antibodies require the simultaneous presence of the alanine-rich and proline-rich regions for binding, (ii) the proline-rich region of P1 interacts with the alanine-rich region, (iii) like the proline-rich region, the alanine-rich region is required for the stability and translocation of P1, (iv) both the proline-rich and alanine-rich regions are required for secretion of P1 in Escherichia coli, and (v) in E. coli, P1 is secreted in the absence of SecB.

Documentos Relacionados

• Deletion of the Central Proline-Rich Repeat Domain Results in Altered Antigenicity and Lack of Surface Expression of the Streptococcus mutans P1 Adhesin Molecule
• Identification of antigenic epitopes in an alanine-rich repeating region of a surface protein antigen of Streptococcus mutants.
• Antigenicity, Expression, and Molecular Characterization of Surface-Located Pullulanase of Streptococcus pneumoniae
• Pollen profilin function depends on interaction with proline-rich motifs.
• Structural and Functional Variation within the Alanine-Rich Repetitive Domain of Streptococcal Antigen I/II