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Gene Review:

vacB - virulence-associated protein

Haemophilus influenzae Rd KW20

Zolli, M. et al., Pereira, M.P. et al., May, B.J. et al., Griffin, R. et al., Wong, S.M. et al.

Griffin, Cox, Makepeace, Richards, Moxon, Hood,

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Disease relevance of vacB

Two previously undescribed open reading frames, accounting for approximately 1% of the genome, encode large proteins with homology to the virulence-associated filamentous hemagglutinin of Bordetella pertussis [1].
Elucidation of the monoclonal antibody 5G8-reactive, virulence-associated lipopolysaccharide epitope of Haemophilus influenzae and its role in bacterial resistance to complement-mediated killing [2].

High impact information on vacB

We report regulation of the display of the virulence-associated phosphorylcholine (PC) epitope on the LOS in response to environmental conditions [3].
CDP-ribitol is an activated precursor for the synthesis of virulence-associated polysaccharides in the capsule of the Gram-negative pathogen Haemophilus influenzae and in the cell walls of Gram-positive pathogens including Staphylococcus aureus [4].
CDP-ribitol synthase is a bifunctional reductase and cytidylyltransferase that catalyzes the transformation of D-ribulose 5-phosphate, NADPH, and CTP to CDP-ribitol, a repeating unit present in the virulence-associated polysaccharide capsules of Haemophilus influenzae types a and b [Follens, A., et al. (1999) J. Bacteriol. 181, 2001] [5].

References

Complete genomic sequence of Pasteurella multocida, Pm70. May, B.J., Zhang, Q., Li, L.L., Paustian, M.L., Whittam, T.S., Kapur, V. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
Elucidation of the monoclonal antibody 5G8-reactive, virulence-associated lipopolysaccharide epitope of Haemophilus influenzae and its role in bacterial resistance to complement-mediated killing. Griffin, R., Cox, A.D., Makepeace, K., Richards, J.C., Moxon, E.R., Hood, D.W. Infect. Immun. (2005) [Pubmed]
Environmental and genetic regulation of the phosphorylcholine epitope of Haemophilus influenzae lipooligosaccharide. Wong, S.M., Akerley, B.J. Mol. Microbiol. (2005) [Pubmed]
Bifunctional catalysis by CDP-ribitol synthase: convergent recruitment of reductase and cytidylyltransferase activities in Haemophilus influenzae and Staphylococcus aureus. Pereira, M.P., Brown, E.D. Biochemistry (2004) [Pubmed]
Reduction precedes cytidylyl transfer without substrate channeling in distinct active sites of the bifunctional CDP-ribitol synthase from Haemophilus influenzae. Zolli, M., Kobric, D.J., Brown, E.D. Biochemistry (2001) [Pubmed]

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