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Article

Essential Binding of LukF of Staphylococcal<i>γ</i>-Hemolysin Followed by the Binding of H<i>γ</i>II for the Hemolysis of Human Erythrocytes

1 Jan 1995

Abstract excerpt

Staphylococcal gamma-hemolysin consists of two protein components, LukF and H gamma II. This report clarifies the order of binding of the two components to human erythrocytes for the hemolytic activity of the toxin. The initial binding of LukF to the human erythrocytes is essential for the subsequent binding of H gamma II to the same cells, with the formation of a heat-undissociable protein of about 100 kDa...

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Identifiers

PMID: 7613012
DOI: 10.1271/bbb.59.1181

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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.

Related research

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Research trail→

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Essential Binding of LukF of Staphylococcal<i>γ</i>-Hemolysin Followed by the Binding of H<i>γ</i>II for the Hemolysis of Human ErythrocytesPMID 7613012Read ↗

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Tyrosine72 residue at the bottom of rim domain in LukF crucial for the sequential binding of the staphylococcal gamma-hemolysin to human erythrocytes.Semantic proximity Read ↗

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α-hemolysin of <i>Staphylococcus aureus</i> impairs thrombus formationSemantic proximity Read ↗

Essential residues, W177 and R198, of LukF for phosphatidylcholine-binding and pore-formation by staphylococcal gamma-hemolysin on human erythrocyte membranes.Semantic proximity Read ↗

Rim domain loops of staphylococcal β-pore forming bi-component toxin S-components recognize target human erythrocytes in a coordinated manner.Semantic proximity Read ↗

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