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Assembly of the oligomeric membrane pore formed by Staphylococcal alpha-hemolysin examined by truncation mutagenesis.

Abstract:

The alpha-hemolysin (alpha HL) from Staphylococcus aureus causes the lysis of susceptible cells such as rabbit erythrocytes (rRBCs). Lysis is associated with the formation of a hexameric pore in the plasma membrane. Here we show that truncation mutants of alpha HL missing 2 to 22 N-terminal amino acids form oligomers on the surfaces of rRBCs but fail to lyse the cells. By contrast, mutants missing 3 or 5 amino acids at the C terminus are very inefficient at oligomerization but do lyse rRBCs, ...

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Publication status:
Published

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Authors


Krishnasastry, M More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Chemical Biology
Journal:
The Journal of biological chemistry
Volume:
267
Issue:
30
Pages:
21782-21786
Publication date:
1992-10-05
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:00f4332a-45ae-4244-86bc-00ed51035950
Source identifiers:
52219
Local pid:
pubs:52219

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