PMID: 9425248Mar 14, 1998Paper

Hemin regulation of hemoglobin binding by Porphyromonas gingivalis

Current Microbiology
J W SmalleyP D Marsh

Abstract

Hemoglobin binding to chemostat-grown hemin-excess and hemin-limited cells of Porphyromonas gingivalis W50, and to cells of the avirulent, beige-pigmenting variant W50/BE1, was quantified. Hemin-excess W50 bound more hemoglobin than hemin-limited W50, mirroring the hemin-binding ability of these cells [Microb Ecol Health Dis 7:9-15, 1994]. In contrast to hemin, hemoglobin binding was not enhanced by sodium dithionite. The hemoglobin-binding capacity of hemin-excess W50/BE1 was below that of hemin-limited W50 and only observed under oxidizing conditions. Scatchard analysis revealed similar affinity constants for hemin-excess and hemin-limited W50, and confirmed a lower binding maximum for the latter. Hemin-excess W50/BE1 displayed cooperative binding of hemoglobin. These differences in binding were reflected in the binding of a horse radish peroxidase-conjugated hemoglobin (HHRPO) in a dot-blot assay. However, neither the 32-kDa hemin-binding protein, nor its 19-kDa heat-modified form, from either hemin-limited W50 or hemin-excess W50/BE1, bound this conjugate. These data indicate that hemoglobin binding by P. gingivalis is hemin-regulated and occurs via a mechanism different from hemin binding.

Citations

Feb 7, 2002·The Biochemical Journal·John W SmalleyJack Silver
Nov 26, 2010·Antimicrobial Agents and Chemotherapy·Ji-Hoi MoonJin-Yong Lee
May 5, 2006·Applied and Environmental Microbiology·Takashi MasudaFuminobu Yoshimura
Nov 18, 2000·Infection and Immunity·J A CarrollM F Minnick
Jan 18, 2005·FEMS Microbiology Reviews·Teresa OlczakCaroline Attardo Genco
Sep 5, 2008·Current Protocols in Microbiology·Myriam BélangerAnn Progulske-Fox
Nov 19, 2011·FEMS Microbiology Letters·Ji-Hoi MoonJin-Yong Lee

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