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THE INTERACTION BETWEEN PERTUSSIS TOXIN AND 10 MONOCLONAL ANTIBODIES
Author(s) -
Schou Carsten,
AuJensen Monika,
Heron Iver
Publication year - 1987
Publication title -
acta pathologica microbiologica scandinavica series c: immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.909
H-Index - 88
eISSN - 1600-0463
pISSN - 0108-0202
DOI - 10.1111/j.1699-0463.1987.tb00028.x
Subject(s) - epitope , monoclonal antibody , pertussis toxin , chinese hamster ovary cell , diphtheria toxin , toxin , microbiology and biotechnology , antibody , bordetella pertussis , chemistry , biology , virology , biochemistry , g protein , immunology , receptor , genetics , bacteria
Data on the epitope specificity of 10 monoclonal hybridoma antibodies (Mabs) that showed positive reaction in enzyme‐linked immunosorbent assay (ELISA) towards pertussins toxin (Ptx) are presented. The relative functional affinity of the Mabs was determined in a catching ELISA system. The Mabs were tested for their ability to inhibit the biological activities of this toxin in two in vitro systems, viz. haemagglutination (HA) and Chinese Hamster Ovary cell (CHO) test, and in three in vivo assays: histamine sensitization (HS), leucocytosis‐promoting activity (LP) and protection against intra‐cerebral challenge (i.c.) with virulent B. pertussis organisms. Four Mabs were found inhibiting HA and three inhibited the effect on CHO cells. Two Mabs showed demonstrable protective effect on mice in i.c. test. The same two Mabs were also able to inhibit HS and LP activity of Ptx. Five of the ten Mabs reacted with Ptx subjected to blotting after separation of the toxin subunits in sodium‐dodecyl sulphate polyacrylamide gel electrophoresis. The five Mabs all bound to more than one subunit. The epitopes defined by several of the Mabs might be useful in the context of a third‐generation whooping cough vaccine.