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Volume 272, Number 46,
Issue of November 14, 1997
pp. 29033-29038
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Identification of the Key Protein for Zinc Uptake in
Hemophilus influenzae
(Received for publication, July 17, 1997, and in revised form, August 20, 1997)
Desheng
Lu
§
,
Beth
Boyd
§
and
Clifford A.
Lingwood
§¶
From the Departments of Medical Genetics and
Microbiology, Biochemistry, and ¶ Laboratory Medicine and
Pathobiology, University of Toronto, and § Division of
Microbiology, Research Institute, Hospital for Sick Children,
Toronto, Ontario M5G 1X8, Canada
Very little is known about specific mechanisms
for zinc accumulation and transport in bacteria. In this study a
putative adhesin B in Hemophilus influenzae, the product of
gene HI0119, has been identified as a periplasmic zinc-binding protein
(PZP1). A pzp1-deficient mutant has been constructed which
is defective for growth under aerobic conditions and grows poorly under
anaerobic conditions. The growth defect is specifically rescued by
supplementing the growth medium with high concentrations of zinc.
Subcellular fractionation was used to localize PZP1 to the periplasmic
region in a nontypeable H. influenzae strain and in a
transfected recombinant Escherichia coli strain (TApzp1).
Recombinant PZP1, purified from a periplasmic extract of E. coli strain TApzp1, contained ~two zinc atoms/protein molecule
as determined by neutron activation analysis and atomic absorption
spectroscopy. The zinc atoms could be removed by incubation with EDTA,
and, by further addition of zinc, a total of five zinc atoms/PZP1 could
be bound. Direct binding of 65Zn to the recombinant protein
by Western blot was demonstrated. Taken together, these results provide
direct evidence that PZP1 plays a key role in zinc uptake by H. influenzae.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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