The gram-negative bacterium V. vulnificus is a deadly seafood-borne pathogen, and has been implicated in recent outbreaks of necrotizing faciitis. The expression of the capsule, a mucoid extracellular polysaccharide, has been associated with high virulence. The capsule of clinical strain MO6-24 is a tetrasaccharide comprised of three L-α-N-acetylquinovosamine (L-QuiNAc) residues and one α-N-acetylgalactosamineuronic acid (GalNAcA) residue. Several genes in the capsule polysaccharide operon code for enzymes responsible for modifying these residues before polymerization. Our work focuses on the characterization of the function of these enzymes to determine their role in capsule biosynthesis. The dehydratase WbjB and the reductase RmlD have been shown to convert uridyl diphosphate-N-acetylglucosamine (UDP-GlcNAc) to an L-QuiNAc precursor. Function of the epimerase WbpP and the dehydratase WecC has been investigated, as well as the membrane-bound enzyme WbfY; also proposed to convert UDP-GlcNAc to UDP-GalNAcA.

Study and characterization of the sugar-modifying enzymes of the capsule biosynthesis pathway of Vibrio vulnificus

249th National Meeting (2015)

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