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Journal of Bacteriology, November 2000, p. 6456-6462, Vol. 182, No. 22
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Characterization of a Novel Outer Membrane
Hemin-Binding Protein of Porphyromonas gingivalis
S. G.
Dashper,1
A.
Hendtlass,1
N.
Slakeski,1
C.
Jackson,1
K. J.
Cross,1
L.
Brownfield,1
R.
Hamilton,2
I.
Barr,2 and
E. C.
Reynolds1,*
School of Dental Science, The University of
Melbourne, Melbourne,1 and CSL Ltd.,
Parkville,2 Victoria, Australia
Received 15 May 2000/Accepted 30 August 2000
Porphyromonas gingivalis is a gram-negative, anaerobic
coccobacillus that has been implicated as a major etiological agent in
the development of chronic periodontitis. In this paper, we report the
characterization of a protein, IhtB (iron heme transport; formerly
designated Pga30), that is an outer membrane hemin-binding protein
potentially involved in iron assimilation by P. gingivalis. IhtB was localized to the cell surface of P. gingivalis by
Western blot analysis of a Sarkosyl-insoluble outer membrane
preparation and by immunocytochemical staining of whole cells using
IhtB peptide-specific antisera. The protein, released from the cell
surface, was shown to bind to hemin using hemin-agarose. The growth of
heme-limited, but not heme-replete, P. gingivalis cells was
inhibited by preincubation with IhtB peptide-specific antisera. The
ihtB gene was located between an open reading frame
encoding a putative TonB-linked outer membrane receptor and three open
reading frames that have sequence similarity to ATP binding cassette
transport system operons in other bacteria. Analysis of the deduced
amino acid sequence of IhtB showed significant similarity to the
Salmonella typhimurium protein CbiK, a cobalt chelatase
that is structurally related to the ATP-independent family of
ferrochelatases. Molecular modeling indicated that the IhtB amino acid
sequence could be threaded onto the CbiK fold with the IhtB structural
model containing the active-site residues critical for chelatase
activity. These results suggest that IhtB is a peripheral outer
membrane chelatase that may remove iron from heme prior to uptake by
P. gingivalis.
*
Corresponding author. Mailing address: School of Dental
Science, The University of Melbourne, 711 Elizabeth St., Melbourne 3000, Victoria, Australia. Phone: 61 3 9341 0270. Fax: 61 3 9341 0236. E-mail: e.reynolds{at}dent.unimelb.edu.au.
Journal of Bacteriology, November 2000, p. 6456-6462, Vol. 182, No. 22
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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