NDLI: Identification of amino acid residues essential for the enzymatic activities of pertussis toxin.

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Identification of amino acid residues essential for the enzymatic activities of pertussis toxin.

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Identification of amino acid residues essential for the enzymatic activities of pertussis toxin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Locht, C. Capiau, C. Feron, C.
Description	Author Affiliation: Locht C ( Department of Molecular and Cellular Biology, Smith Kline-Biologicals, Rixensart, Belgium.);
Abstract	The enzymatic ADP-ribosyltransferase activity associated with the S1 subunit of pertussis toxin is considered to be responsible for its biological effects. Although pertussis toxin has no significant homology to other ADP-ribosylating toxins such as diphtheria toxin and Pseudomonas aeruginosa exotoxin A, the results presented in this paper show that, as for diphtheria toxin and exotoxin A, tryptophan and glutamic acid residues are essential for the enzymatic activities of pertussis toxin. Moreover, a structural motif can be identified around the critical glutamic acid residue. Chemical modification or site-directed deletion or replacement of Trp-26 abolishes ADP-ribosyltransferase and the associated NAD glycohydrolase activities. Both enzymatic activities are also abolished when Glu-129 is deleted or replaced by aspartic acid. Mutations at the Glu-106 position do not significantly reduce the enzymatic activities of the S1 subunit. The mutations do not affect the ability of the different S1 forms to be recognized by a variety of monoclonal antibodies, including neutralizing antibodies. Pertussis toxin containing a deletion or replacement of Trp-26, Glu-129, or both in the S1 subunit should thus be devoid of toxic activities without losing its reactivity with protective antibodies and, therefore, could be safely included in new generation vaccines against whooping cough.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amino Acids Pertussis Toxin Virulence Factors, Bordetella Metabolism 2-Hydroxy-5-nitrobenzyl Bromide Pharmacology Adenosine Diphosphate Ribose Amino Acid Sequence Bacteriophages Genetics Chemical Phenomena Chemistry DNA, Recombinant Epitopes Immunology Escherichia Coli GTP-Binding Proteins Gene Expression Regulation Glutamates Glutamic Acid Molecular Sequence Data Mutation NAD+ Nucleosidase Poly(ADP-ribose) Polymerases Structure-Activity Relationship Transfection Tryptophan Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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