Journal article

Porphyromonas gingivalis Gingipains Display Transpeptidation Activity

Lianyi Zhang, Paul D Veith, N Laila Huq, Yu-Yen Chen, Christine A Seers, Keith J Cross, Dhana G Gorasia, Eric C Reynolds

JOURNAL OF PROTEOME RESEARCH | AMER CHEMICAL SOC | Published : 2018

Abstract

Porphyromonas gingivalis is a keystone periodontal pathogen that has been associated with autoimmune disorders. The cell surface proteases Lys-gingipain (Kgp) and Arg-gingipains (RgpA and RgpB) are major virulence factors, and their proteolytic activity is enhanced by small peptides such as glycylglycine (GlyGly). The reaction kinetics suggested that GlyGly may function as an acceptor molecule for gingipain-catalyzed transpeptidation. Purified gingipains and P. gingivalis whole cells were used to digest selected substrates including human hemoglobin in the presence or absence of peptide acceptors. Mass spectrometric analysis of the substrates digested with gingipains in the presence of GlyGl..

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Grants

Awarded by Australian Government Department of Industry, Innovation and Science


Funding Acknowledgements

This work was supported by the Australian Government Department of Industry, Innovation and Science Grant ID 20080108. The authors thank Drs. Shuai Nie, Ching-Seng Ang, and Nicholas Williamson for the acquisition of Orbitrap LC-MS/MS data and their technical support through the Mass Spectrometry and Proteomics Facility at Bio21 Institute, The University of Melbourne, Australia.