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Article

Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.

The Journal of biological chemistry - 4 Nov 2005

Valeva Angela, Walev Ivan, Kemmer Helene, Weis Silvia, Siegel Isabel, Boukhallouk Fatima, Wassenaar Trudy M, Chavakis Triantafyllos, Bhakdi Sucharit

Abstract excerpt

Production of a single cysteine substitution mutant, S177C, allowed Escherichia coli hemolysin (HlyA) to be radioactively labeled with tritiated N-ethylmaleimide without affecting biological activity. It thus became possible to study the binding characteristics of HlyA as well as of toxin mutants in which one or both acylation sites were deleted. All toxins bound to erythrocytes and granulocytes in a nonsaturable...

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Identifiers

PMID: 16131494
DOI: 10.1074/jbc.M507690200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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