Staphylococcus aureus detoxified alpha-hemolysin (Hla (for alpha-hemolysin); HlaPSGS, HlaH35L)

Staphylococcus aureus detoxified alpha-hemolysin (commonly referred to as mutant, detoxified alpha-toxin or Hla) is an engineered, non-cytolytic variant of the major pore-forming toxin alpha-hemolysin (Hla) produced by Staphylococcus aureus. Wild-type Hla binds target cell membranes and oligomerizes to form heptameric beta-barrel pores, causing lysis of a broad array of host cells and serving as a key virulence factor. Mutant or detoxified forms (e.g., HlaH35L, HlaPSGS) are engineered to eliminate pore-forming and cytolytic activity, while retaining structural epitopes to induce robust immune responses. These detoxified proteins are under development as vaccine antigens and as research tools for studying toxin neutralization, as they can stimulate antibody production that neutralizes the native cytolytic toxin. Their immunogenicity and epitope structure are of interest for vaccines aimed at preventing S. aureus infections. Detoxified alpha-hemolysin does not itself cause toxicity and does not bind (or forms nonfunctional complexes with) cellular receptors such as ADAM10.

Other names

Alpha-hemolysinAlpha-toxinHlaStaphylococcal alpha-hemolysinStaphylococcal alpha-toxinMutant Hla

Neutralization of toxin activity by antibodies (block pore formation); Induction of protective immunity via immunization with the detoxified form