Open AccessMonoclonal antibodies against Streptococcus mutans 74 kDa cell wall saliva receptor (74 kDa SR): correlation between antigenic structure and saliva binding sites
Author(s) -
Bruyere Thierry,
Ackermans Fabienne,
Klein JeanPaul,
Pillat Michael,
Frank Robert M.
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02940.x
Subject(s) - streptococcus mutans , monoclonal antibody , saliva , epitope , microbiology and biotechnology , glycoprotein , antibody , antigen , biology , splenocyte , chemistry , biochemistry , bacteria , immunology , genetics
Five hybrid cell lines secreting monoclonal antibodies (MAbs; LOSM5, 7, 8, 10 and 11) against Streptococcus mutans serotype f 74‐kDa saliva receptor (SR) were generated by fusing rats IR983F myeloma cells with splenocytes from rats immunized with affinity purified 74‐kDa SR. All the five MAbs recognized both native and denatured forms of the SR. Three partially different epitopes could be delineated on protein 74‐kDa by using unlabeled and alkaline phosphatase‐labeled MAbs in competitive enzyme‐linked immunosorbent assay (ELISA). Two of them are involved in the binding of salivary glycoproteins to S. mutans cells; as demonstrated by the inhibition of saliva binding to S. mutans cells by the MAbs LOSM7, 8 and 11. The five MAbs also reacted with 150‐kDa protein, a higher M r protein and peptide mapping of 150‐kDa and 74‐kDa SR showed identical patterns for both polypeptides.