Journal article

Characterization of hemin-binding protein 35 (HBP35) in Porphyromonas gingivalis: its cellular distribution, thioredoxin activity and role in heme utilization

Mikio Shoji, Yasuko Shibata, Teruaki Shiroza, Hideharu Yukitake, Benjamin Peng, Yu-Yen Chen, Keiko Sato, Mariko Naito, Yoshimitsu Abiko, Eric C Reynolds, Koji Nakayama

BMC MICROBIOLOGY | BIOMED CENTRAL LTD | Published : 2010

Abstract

BACKGROUND: The periodontal pathogen Porphyromonas gingivalis is an obligate anaerobe that requires heme for growth. To understand its heme acquisition mechanism, we focused on a hemin-binding protein (HBP35 protein), possessing one thioredoxin-like motif and a conserved C-terminal domain, which are proposed to be involved in redox regulation and cell surface attachment, respectively. RESULTS: We observed that the hbp35 gene was transcribed as a 1.1-kb mRNA with subsequent translation resulting in three proteins with molecular masses of 40, 29 and 27 kDa in the cytoplasm, and one modified form of the 40-kDa protein on the cell surface. A recombinant 40-kDa HBP35 exhibited thioredoxin activit..

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Grants

Awarded by Ministry of Education, Science, Sports, Culture, and Technology, Japan


Awarded by Grants-in-Aid for Scientific Research


Funding Acknowledgements

We thank Kaiting Ng for advice on some aspects of molecular work. We also thank members of the Division of Microbiology and Oral Infection, Nagasaki University Graduate School of Biomedical Sciences, and Cooperative Research Centre for Oral Health Science, Melbourne Dental School, University of Melbourne for helpful discussion. This work was supported by Grants-in-Aid (20249073 and 20791341) for scientific research from the Ministry of Education, Science, Sports, Culture, and Technology, Japan to KN and MS, respectively, by the Global COE Program at Nagasaki University to KN and in part by the president's discretionary fund of Nagasaki University, Japan to MS.