Journal
FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY
Volume 65, Issue 1, Pages 116-120Publisher
WILEY-BLACKWELL
DOI: 10.1111/j.1574-695X.2012.00933.x
Keywords
beta-hexosaminidase; periodontal pathogens; Tannerella forsythia
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Funding
- Royal Society
- Dunhill Medical Trust
- British Oral and Dental Research Trust
- University of Sheffield
- Wellcome Trust
- U.S. Public Health [DE014749]
- The Dunhill Medical Trust [R185/0211] Funding Source: researchfish
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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 beta-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 beta-hexosaminidases. We show here that T.similar to 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 beta-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 beta-hexosaminidase activity has a significant role in biofilm formation in combination with sialidase activity in the biofilm lifestyle of T.similar to forsythia.
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