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Vibrio alginolyticus YHL32 is an outstanding model organism in which hemolysin of the integral outer-membrane proteins (OMPs) has been one of the best characterized virulence factors. The physical properties of the purified hemolysin revealed it to be a 26,200 dalton (Mr26k) monomer with Mr26kalpha and Mr26kbeta components. The amino acid sequence of the beta subunit is the same as that of the homologous subunit in Yersinia pseudotuberculosis. Both the alpha and the beta subunits of Mr26k have N-terminal transmembrane segments (5 to 11 amino acids) and a cytoplasmic domain. Deletion of the alpha subunit genes abolished production of the hemolysin. A histidine residue at position 12 of the alpha subunit and a threonine residue at position 16 of the beta subunit were involved in production of the hemolysin. On the other hand, the beta subunit was shown to be a membrane-anchored protein. The alpha subunit was also fused to the OMP in Escherichia coli, and soluble hemolysin was obtained. When assayed as a pore-forming toxin, the hemolysin formed a pore with a 15 pS single-channel conductance, in accord with the known pore-forming characteristics of the homologous OMP in Y. pseudotuberculosis. The alpha subunit appeared to assemble homotetrameric hemolysin at the cell surface. Accordingly, the beta subunit of Mr26k and hemolysin of Y. pseudotuberculosis assembled as heterodimeric holotoxin in E. coli.Q:

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