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Pertussis toxin and target eukaryotic cells: binding, entry, and activation
Author(s) -
Kaslow Harvey R.,
Burns usilla L.
Publication year - 1992
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.6.9.1612292
Subject(s) - pertussis toxin , bordetella pertussis , protein subunit , biochemistry , toxin , chemistry , oligomer , transmembrane protein , adp ribosylation , g protein , microbiology and biotechnology , receptor , biology , enzyme , bacteria , gene , organic chemistry , genetics , nad+ kinase
Pertussis toxin, a protein virulence factor produced by Bordetella pertussis , is composed of an A protomer and a B oligomer. The A protomer consists of a single polypeptide, termed the S1 subunit, which disrupts transmembrane signaling by ADP‐ribosylating eukaryotic G‐proteins. The B oligomer, containing five polypeptides, binds to cell receptors (most likely containing carbohydrate) and delivers the S1 subunit. Current knowledge suggests that expression of ADP‐ribosyltransferase activity in target eukaryotic cells arises after 1 ) nucleotides and membrane lipids allosterically promote the release of the S1 subunit; and 2 ) the single disulfide bond in the S1 subunit is reduced by reductants such as glutathione. This model suggests conditions for the proper use of the toxin as an experimental reagent.— Kaslow, H. R.; Burns, D. L. Pertussis toxin and target eukaryotic cells: binding, entry and activation. FASEB J. 6: 2684‐2690; 1992.