Open AccessAntigenic epitopes on Mycobacterium tuberculosis recognized by antibodies in tuberculosis and mouse antisera
Author(s) -
Kumar Uday,
Saxena Rajiv K.
Publication year - 1991
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.1574-6968.1991.tb04156.x
Subject(s) - epitope , mycobacterium tuberculosis , antibody , antiserum , antigen , trypsin , chymotrypsin , sodium periodate , proteolytic enzymes , tuberculosis , chemistry , biology , virology , microbiology and biotechnology , enzyme , biochemistry , immunology , medicine , organic chemistry , pathology
Summary The effect of sodium periodate and proteolytic enzyme treatments on the antibody binding capacity of Mycobacterium tuberculosis antigen (Ag) was studied by ELISA. Treatment with sodium periodate resulted in a marked decrease in the capacity of M. tuberculosis Ag to bind antibodies in human TB sera, but had no effect on the reactivity with antibodies in mouse. In contrast, treatment with proteolytic enzymes (trypsin and chymotrypsin) had no effect on the reactivity of M. tuberculosis Ag with human TB sera but reduced substantially the reactivity to antibodies in mouse antisera. These results indicate that anti‐ M. tuberculosis antibodies in human TB sera react predominantly with carbohydrate determinants and not with protein epitopes sensitive to trypsin and chymotrypsin. The bulk of murine antibodies on the other hand were directed against protein determinants and not the carbohydrate epitopes.