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J. Biol. Chem., Vol. 276, Issue 41, 37834-37838, October 12, 2001
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,
From the Department of Biology and the McCollum-Pratt Institute,
The Johns Hopkins University, Baltimore, Maryland 21218
ygdP, a gene associated with the
invasion of brain microvascular endothelial cells by Escherichia
coli K1 (Badger, J. L., Wass, C. A., and Kim, K. S. (2000) Mol. Microbiol. 36, 174-182), the primary
Gram-negative bacterium causing meningitis in newborns, has been cloned
and expressed in E. coli. The protein, YgdP, was purified
to near homogeneity and identified as a member of the Nudix hydrolase
subfamily of dinucleoside oligophosphate pyrophosphatases. It catalyzes
the hydrolysis of diadenosine tetra-, penta-,
and hexa-phosphates with a preference for diadenosine
penta-phosphate, from which it forms ATP and ADP. The
enzyme has a requirement for a divalent metal cation that can be met
with Mg2+, Zn2+, or Mn2+ and, like
most of the Nudix hydrolases, has an alkaline pH optimum between 8.5 and 9. This is the second identification of a gene associated with the
invasiveness of a human pathogen as a member of the Nudix hydrolase
subfamily of dinucleoside oligophosphate pyrophosphatases, and an
examination of homologous proteins in other invasive bacteria suggests
that this may be a common feature of cellular invasion.
To whom correspondence should be addressed. Tel.: 410-516-7316;
Fax: 410-516-5213; E-mail: zoot@jhu.edu.
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