Premium
Antigenic Heterogeneity in the 115,000 M r Major Surface Antigen of Trichomonas vaginalis 1
Author(s) -
TORIAN BRUCE E.,
CONNELLY ROBERTA J.,
BARNES ROBERT C.,
KENNY GEORGE E.
Publication year - 1988
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1988.tb04343.x
Subject(s) - epitope , antigen , trichomonas vaginalis , biology , monoclonal antibody , pronase , antibody , virology , microbiology and biotechnology , immunology , biochemistry , enzyme , trypsin
The 115,000‐molecular‐weight antigen of Trichomonas vaginalis was characterized using monoclonal antibodies developed to three different strains of T. vaginalis and one strain of Tritrichomonas foetus . The antigen was found to be present on all strains or isolates of T. vaginalis examined and was demonstrated to be located on the external surface plasma membrane by agglutination assays and complement‐mediated lysis assays. Characteristics of the antigen were assessed with a proteolytic enzyme and periodate oxidation. Periodate treatment of whole T. vaginalis abrogated binding for eight antibodies while use of pronase‐treated antigen resulted in loss of antibody binding for two different antibodies. Screening of 19 axenized clinical isolates of T. vaginalis and one strain each of T. foetus and Giardia lamblia with type‐specific antibodies delineated three major groups of T. vaginalis based on antigenic specificities (epitope distributions) within the 115,000‐molecular‐weight antigen. In addition, one epitope of the 115,000‐molecular‐weight antigen was found only on the immunizing strain. Two epitopes were present on all T. vaginalis isolates as well as T. foetus and G. lamblia . One epitope was common to all T. vaginalis except one. A minimum of six different epitopes of the 115,000‐molecular‐weight antigen were identified. Antigens purified with type‐specific or “common” monoclonal antibodies shared the same partial peptide maps demonstrating relatedness.