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Mitogenic properties of two distinct forms of toxic shock syndrome toxin‐1 separated on hydroxyapatite by high‐performance liquid chromatography
Author(s) -
NAIDU A. S.,
ERIKSSON K.O.,
HALLBERG T.,
LINDEBERG J.,
LIAO J.L.,
YAO K.,
WADSTRÖM T.,
HJERTEN S.
Publication year - 1989
Publication title -
apmis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0903-4641
DOI - 10.1111/j.1699-0463.1989.tb00522.x
Subject(s) - polyclonal antibodies , superantigen , isoelectric point , microbiology and biotechnology , toxic shock syndrome , toxin , chromatography , biology , chemistry , antibody , staphylococcus aureus , biochemistry , immunology , bacteria , enzyme , genetics
The homogeneity of a purified staphylococcal toxic shock syndrome toxin‐1 (TSST‐1) was tested by high‐performance methods. This preparation was homogeneous in ion‐exchange chromatography and isoelectric focusing (pI = 7.4), but was resolved into two distinct peaks by high‐performance hydroxyapatite chromatography. Both components, TSST‐1 hA and TSST‐1 hB had similar molecular weights (22 kD) and amino acid compositions. TSST‐1 did not dimerize or polymerize upon heating at 60 °C for 30 min or in solutions with pH varying from 4.0 to 8.5. TSST‐1 hA and TSST‐1 hB showed similar immunological reactivity to native TSST‐1 goat polyclonal antibodies. TSST‐1 hA and TSST‐1 hB as well as staphylococcal enterotoxin A and staphylococcal exfoliative toxin were potent mitogens in lymphocyte proliferation assays. The lymphocyte proliferative response to 10 pg of TSST‐1 hB was comparable to a response elicited by 10 ng of TSST‐1 hA , suggesting that the former component is a more potent mitogen. Rabbit or goat polyclonal antibodies to native TSST‐1 efficiently neutralized both TSST‐1 components. Heat treatment at 80 °C for 15 min had minimal or no effect on the mitogenic properties of TSST‐1 hA and TSST‐1 hB .