Beta-hexosaminidase activity of the oral pathogen Tannerella forsythia influences biofilm formation on glycoprotein substrates.

ROY, Sumita, PHANSOPA, Chatchawal, STAFFORD, Prachi, HONMA, Kiyonobu, DOUGLAS, C W Ian, SHARMA, Ashu and STAFFORD, Graham P (2012). Beta-hexosaminidase activity of the oral pathogen Tannerella forsythia influences biofilm formation on glycoprotein substrates. FEMS Immunology and Medical Microbiology, 65 (1), 116-120.

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Link to published version:: 10.1111/j.1574-695X.2012.00933.x

Abstract

Tannerella forsythia is an important pathogen in periodontal disease. Previously, we showed that its sialidase activity is key to utilization of sialic acid from a range of human glycoproteins for biofilm growth and initial adhesion. Removal of terminal sialic acid residues often exposes β-linked glucosamine or galactosamine, which may also be important adhesive molecules. In turn, these residues are often removed by a group of enzymes known as β-hexosaminidases. We show here that T. forsythia has the ability to cleave glucosamine and galactosamine from model substrates and that this activity can be inhibited by the hexosaminidase inhibitor PugNAc (O-(2-acetamido-2-deoxy-d-glucopyranosylidene)amino N-phenyl carbamate). We now demonstrate for the first time that β-hexosaminidase activity plays a role in biofilm growth on glycoprotein-coated surfaces because biofilm growth and initial cell adhesion are inhibited by PugNAc. In contrast, adhesion to siallo-glycoprotein-coated surfaces is unaltered by PugNAc in the absence of sialidase activity (using a sialidase-deficient mutant) or surprisingly on the clinically relevant substrates saliva or serum. These data indicate that β-hexosaminidase activity has a significant role in biofilm formation in combination with sialidase activity in the biofilm lifestyle of T. forsythia.

Item Type: Article
Additional Information: Article first published online: 14 FEB 2012
Research Institute, Centre or Group: Biomolecular Sciences Research Centre
Identification Number: 10.1111/j.1574-695X.2012.00933.x
Depositing User: Jamie Young
Date Deposited: 03 Jun 2015 13:20
Last Modified: 03 Jun 2015 13:20
URI: http://shura.shu.ac.uk/id/eprint/10001

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