The pmm gene from @entity50079 , which encodes phosphomannomutase (PMM), was cloned and sequenced. The open reading frame consisted of 1,434 bp, encoding a polypeptide of 477 @entity1522 with a molecular mass of 53,325 Da. The predicted amino acid sequence of @entity50079 PMM showed high similarity with PMMs from other enteric bacteria, such as @entity1838 , Salmonella sp. and @entity526 . The PMM protein was overexpressed in @entity526 as a His(6)-tagged recombinant protein. The estimated apparent K(m )and k(cat) values of the purified recombinant protein for @entity42278 were about 60 microM and 800 min(-1), respectively. To investigate the biochemical functions and the role of pmm in the virulence of @entity50079 , a pmm knock-out mutant was constructed by homologous recombination mutation. Under the various physical conditions, cell numbers of the wild-type and the mutant did not differ. Oral introduction of bacterial suspensions to a @entity19 model showed that the pmm-deficient mutant decreased in viability at the intestine. Microscopy of the isolated intestines from @entity19 revealed significant damage after 3 days in intestinal mucosa infected with the wild-type as compared with the mutant. The pmm-deficient mutant caused a reduction of virulence in @entity19 and the loss of O-antigen polysaccharide, and showed low resistance relative to the wild-type when incubated with normal human serum.

Genetic analysis of phosphomannomutase/phosphoglucomutase from XXXX and characterization of its role in virulence.

@entity1522 :: ('CHEBI:33709', 'Chemical') :: ['amino acids'] @entity1838 :: ('666', 'Species') :: ['V. cholerae'] @entity50079 :: ('29494', 'Species') :: ['Vibrio furnissii', 'V. furnissii'] @entity19 :: ('10090', 'Species') :: ['mice', 'mouse'] @entity42278 :: ('MESH:C047217', 'Chemical') :: ['mannose 1-phosphate'] @entity526 :: ('562', 'Species') :: ['Escherichia coli', 'E. coli']
@entity50079 :: (29494,Species) :: ['Vibrio furnissii']
