Work

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

Year: 2002

Type: article

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 chemical modification during single-channel recording. Four LukF and four LukS subunits coassemble to form an octamer. This result in part explains properties of the leukocidin pore, such as its high conductance compared to the alpha HL pore. It is also pertinent to the mechanism of assembly of beta-PFT pores and suggests new possibilities for engineering these proteins.

Source: Protein Science

DOI: 10.1110/ps.4360102

Authors: George Miles, Liviu Movileanu, Hagan Bayley

Institutions: Texas A&M Health Science Center, Texas A&M University System, Texas A&M University

Language: English

Topic: Ion channel regulation and function

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: U.S. Department of Energy, Texas A and M University, Texas A and M University Health Science Center

OpenAlex ID: W2161696543

FWCI: 2.503

Cites: 62

Cited by: 123

Related to: 10