Abstract:
:ADP-ribosylating protein exotoxins from Vibrio cholerae (CT) and Escherichia coli (LT-I) share two short regions of sequence similarity with Bordetella pertussis toxin (PT). Previous studies have indicated that substitution of arginine for lysine 7 within the first region of CT drastically decreases ADP ribosyltransferase activity. We have more closely defined the role of other amino acids in this region by generating modified proteins in which arginine 7 was replaced with lysine (R7K), aspartate 9 was replaced with arginine (D9R), glycine was substituted for proline 12 (P12G), amino acids 6 to 13 were deleted (delta 613) or the C-terminal KDEL sequence was changed to NEDL. The modified proteins R7K, D9R and delta 613 exhibited undetectable ADP ribosyltransferase activity. Comparison of the tryptic digest of R7K with native CT suggested that changes in protein conformation may be responsible for the loss of ADP-ribosylation activity.
journal_name
Microb Pathogjournal_title
Microbial pathogenesisauthors
Vadheim KL,Singh Y,Keith JMdoi
10.1006/mpat.1994.1079subject
Has Abstractpub_date
1994-11-01 00:00:00pages
339-46issue
5eissn
0882-4010issn
1096-1208pii
S0882-4010(84)71079-5journal_volume
17pub_type
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