Antigen analysis of several pathogenic strains of Trichomonas vaginalis
- 1 March 1983
- journal article
- research article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 39 (3), 1041-1047
- https://doi.org/10.1128/iai.39.3.1041-1047.1983
Abstract
Analysis of several human strains of T. vaginalis and 1 bovine strain of Tritrichomonas foetus was accomplished with standard sodium dodecyl sulfate-gel electrophoresis and fluorography technology. Highly motile, live trichomonads were radiolabeled, and total trichoroacetic acid-precipitated proteins were electrophoresed. Complex protein profiles of the various human strains of T. vaginalis were obtained with proteins ranging in MW from 20,000 to > 200,000. The parasite biosynthesis of the Coomassie brilliant blue-stained protein bands was demonstrated by efficient radiolabeling of trichomonads with [35S]methionine or a 3H-amino acid digest before electrophoresis and fluorography. Immunogenic trichomonal proteins were then identified by a radioimmunoprecipitation method. A detergent extract of [35S]methionine-labeled T. vaginalis proteins was mixed with serum from an immunized rabbit or pooled sera from subcutaneously infected mice and soluble antibody-antigen complexes isolated by adsorption to protein A-bearing Staphylococcus aureus. The radiolabeled protein antigens were then identified by gel electrophoresis and fluorography. Immunized rabbit serum and pooled sera from challenged mice contained high-titered antibody which reacted with numerous high- and low-MW proteins. Individual s.c. infected mice were found to possess identical antibody responses to these immunogenic trichomonal proteins. A high degree of serological cross-reactivity among the various trichomonads was demonstrated. No differences in the composition of immunogenic proteins were observed among cultures grown in vitro for various lengths of time under the experimental conditions employed. Electrophoretic analysis of cloned colonies of T. vaginalis organisms revealed no differences in their protein composition. The biological relevance of these observations is discussed.This publication has 27 references indexed in Scilit:
- THE ULTRASTRUCTURE OF TRICHOMONAS VAGINALIS DONNÉ BEFORE AND AFTER TRANSFER FROM VAGINAL SECRETION TO DIAMONDS MEDIUMActa Pathologica Microbiologica Scandinavica Section B Microbiology, 2009
- Trichomonas vaginalis Infection of the Median Raphe of the PenisSexually Transmitted Diseases, 1981
- Analysis of serum IgG against Treponema pallidum protein antigens in experimentally infected rabbits.Sexually Transmitted Infections, 1981
- The Clinical and Laboratory Diagnosis of Tric ho mo n as vaginaIis InfectionSexually Transmitted Diseases, 1980
- Molecular characterization of receptor binding proteins and immunogens of virulent Treponema pallidum.The Journal of Experimental Medicine, 1980
- ISOLATION OF TRICHOMONAS VAGINALIS RESISTANT TO METRONIDAZOLEThe Lancet, 1978
- Solubilization of membrane proteins by sulfobetaines, novel zwitterionic surfactantsAnalytical Biochemistry, 1978
- Solubilization of bacterial membrane proteins using alkyl glucosides and dioctanoyl phosphatidylcholineBiochimica et Biophysica Acta (BBA) - Biomembranes, 1975
- Antigenic Analysis of Virulent and Avirulent Strains of Trichomonas gallinae by Gel Diffusion Methods*The Journal of Protozoology, 1972
- Immunologic Analysis by Quantitative Fluorescent Antibody Methods of the Effects of Prolonged Cultivation on Trichomonas gallinae*The Journal of Protozoology, 1968