HmuY haemophore and gingipain proteases constitute a unique syntrophic system of haem acquisition by Porphyromonas gingivalis.

Smalley, John W, Byrne, Dominic P, Birss, Andrew J, Wojtowicz, Halina, Sroka, Aneta ORCID: 0000-0002-3386-5364, Potempa, Jan ORCID: 0000-0002-3600-7461 and Olczak, Teresa (2011) HmuY haemophore and gingipain proteases constitute a unique syntrophic system of haem acquisition by Porphyromonas gingivalis. PloS one, 6 (2). e17182-.

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Abstract

Haem (iron protoporphyrin IX) is both an essential growth factor and virulence regulator for the periodontal pathogen Porphyromonas gingivalis, which acquires it mainly from haemoglobin via the sequential actions of the R- and K-specific gingipain proteases. The haem-binding lipoprotein haemophore HmuY and its cognate receptor HmuR of P. gingivalis, are responsible for capture and internalisation of haem. This study examined the role of the HmuY in acquisition of haem from haemoglobin and the cooperation between HmuY and gingipain proteases in this process. Using UV-visible spectroscopy and polyacrylamide gel electrophoresis, HmuY was demonstrated to wrest haem from immobilised methaemoglobin and deoxyhaemoglobin. Haem extraction from oxyhaemoglobin was facilitated after oxidation to methaemoglobin by pre-treatment with the P. gingivalis R-gingipain A (HRgpA). HmuY was also capable of scavenging haem from oxyhaemoglobin pre-treated with the K-gingipain (Kgp). This is the first demonstration of a haemophore working in conjunction with proteases to acquire haem from haemoglobin. In addition, HmuY was able to extract haem from methaemalbumin, and could bind haem, either free in solution or from methaemoglobin, even in the presence of serum albumin.

Item Type:	Article
Additional Information:	## TULIP Type: Articles/Papers (Journal) ## official_url: www.liv.ac.uk/infection-and-global-health/publications/Smalley_et_al_Feb_2011.pdf
Uncontrolled Keywords:	Porphyromonas gingivalis, Heme, Protoporphyrins, Multiprotein Complexes, Peptide Hydrolases, Cysteine Endopeptidases, Serum Albumin, Adhesins, Bacterial, Hemoglobins, Oxyhemoglobins, Electrophoresis, Protein Binding, Electrophysiological Phenomena, Gingipain Cysteine Endopeptidases
Subjects:	?? RK ??
Divisions:	Faculty of Health and Life Sciences > Institute of Life Courses and Medical Sciences > School of Dentistry
Depositing User:	Symplectic Admin
Date Deposited:	16 May 2011 15:03
Last Modified:	14 Mar 2024 18:01
DOI:	10.1371/journal.pone.0017182
Publisher's Statement :	© 2011 Smalley et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/1500