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. 1991 Nov;59(11):4266–4270. doi: 10.1128/iai.59.11.4266-4270.1991

Site-specific mutagenesis of the catalytic subunit of cholera toxin: substituting lysine for arginine 7 causes loss of activity.

W N Burnette 1, V L Mar 1, B W Platler 1, J D Schlotterbeck 1, M D McGinley 1, K S Stoney 1, M F Rohde 1, H R Kaslow 1
PMCID: PMC259028  PMID: 1937784

Abstract

Cholera and pertussis toxins each contain a subunit with ADP-ribosyltransferase activity, sharing a region of nearly identical amino acid sequence near the NH2 terminus. Previous investigations have shown that substitution of a lysine residue for Arg-9 in the catalytic A subunit of pertussis toxin substantially eliminates its enzyme activity. We now report that substitution of lysine for the position-equivalent Arg-7 of cholera toxin subunit A leads to a similar loss of catalytic activity. This result suggests a correlation of function with structure between the sequence-related cholera and pertussis toxin A subunits and may contribute to the design of a vaccine containing an enzymatically inert analog of cholera toxin.

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Selected References

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