USE OF SYNTHETIC PEPTIDES AND SITE-SPECIFIC ANTIBODIES TO LOCALIZE A DIPHTHERIA-TOXIN SEQUENCE ASSOCIATED WITH ADP-RIBOSYLTRANSFERASE ACTIVITY

被引:8
作者
OLSON, JC
机构
关键词
D O I
10.1128/JB.175.3.898-901.1993
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Diphtheria toxin (DT) and Pseudomonas aeruginosa exotoxin A have the same molecular mechanism of toxicity; both toxins ADP-ribosylate a modified histidine residue in elongation factor 2. To help identify amino acids involved in this reaction, sequences in DT that share homology with P. aeruginosa exotoxin A were synthesized and examined for a role in the ADP-ribosyltransferase reaction. By using this approach, residues 32 to 54 of DT were found to define an epitope associated with antibody-mediated inhibition of DT enzyme activity. This lends further support to the notion that residues in this region of DT are involved in the enzymatic reaction.
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页码:898 / 901
页数:4
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