Subunit composition of a bicomponent toxin: staphylococcal leukocidin forms an octameric transmembrane pore.
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.
Miles
George
G
Department of Medical Biochemistry and Genetics, The Texas A&M University System Health Science Center, College Station, Texas 77843-1114, USA.
Movileanu
Liviu
L
Bayley
Hagan
H
D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins; D006460:Hemolysin Proteins / Q000737:chemistry; D006801:Humans; D007473:Ion Channels / Q000737:chemistry; D007956:Leukocidins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D021122:Protein Subunits; D021381:Protein Transport / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013211:Staphylococcus aureus / Q000737:chemistry*
D001426:Bacterial Proteins; D006460:Hemolysin Proteins; D007473:Ion Channels; D007956:Leukocidins; D021122:Protein Subunits; C074300:LukF protein, Staphylococcus aureus