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Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.

Abstract:

Staphylococcal leukocidin pores are formed by the obligatory interaction of two distinct polypeptides, one of class F and one of class S, making them unique in the family of beta-barrel pore-forming toxins (beta-PFTs). By contrast, other beta-PFTs form homo-oligomeric pores; for example, the staphylococcal alpha-hemolysin (alpha HL) pore is a homoheptamer. Here, we deduce the subunit composition of a leukocidin pore by two independent methods: gel shift electrophoresis and site-specific chemi...

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Publication status:
Published

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Publisher copy:
10.1110/ps.4360102

Authors


Movileanu, L More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Chemical Biology
Journal:
Protein science : a publication of the Protein Society
Volume:
11
Issue:
4
Pages:
894-902
Publication date:
2002-04-05
DOI:
EISSN:
1469-896X
ISSN:
0961-8368
URN:
uuid:53f32b05-a4f2-4adc-8721-309f5c890b6b
Source identifiers:
52204
Local pid:
pubs:52204

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