Effects of eliminating a disulfide bridge within domain II of Pseudomonas aeruginosa exotoxin A

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Effects of eliminating a disulfide bridge within domain II of Pseudomonas aeruginosa exotoxin A.

Cysteines 265 and 287 of Pseudomonas aeruginosa exotoxin A (ETA) were substituted by serine, thereby eliminating a disulfide bridge within domain II, the putative membrane insertion-translocation domain. Purified mutant toxin was 80-fold less toxic for mouse L cells than was wild-type ETA while retaining the same specific activity in the ADP-ribosyltransferase reaction as did wild-type toxin. B...

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Influence of deletions within domain II of exotoxin A on its extracellular secretion from Pseudomonas aeruginosa.

Pseudomonas aeruginosa is a gram-negative bacterium that secretes many proteins into the extracellular medium via the Xcp machinery. This pathway, conserved in gram-negative bacteria, is called the type II pathway. The exoproteins contain information in their amino acid sequence to allow targeting to their secretion machinery. This information may be present within a conformational motif. The n...

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protective properties of nontoxic recombinant exotoxin a (domain i-ii) against pseudomonas aeruginosa infection

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ژورنال

عنوان ژورنال: Infection and Immunity

سال: 1989

ISSN: 0019-9567,1098-5522

DOI: 10.1128/iai.57.7.1873-1878.1989