Skip navigation

An orthologue of Bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia

An orthologue of Bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia

Thompson, Hayley ORCID: 0000-0003-3822-2234, Homer, Karen A, Rao, Susmitha, Booth, Veronica and Hosie, Arthur H F (2009) An orthologue of Bacteroides fragilis NanH is the principal sialidase in Tannerella forsythia. Journal of Bacteriology, 191 (11). pp. 3623-3628. ISSN 0021-9193 (Print), 1098-5530 (Online) (doi:https://doi.org/10.1128/JB.01618-08)

[img]
Preview
PDF (Publisher VoR)
38629_THOMPSON_An_orthologue_of_Bacteroides_fragilis_NanH.pdf - Published Version

Download (534kB) | Preview

Abstract

Sialidase activity is a putative virulence factor of the anaerobic periodontal pathogen Tannerella forsythia, but it is uncertain which genes encode this activity. Characterization of a putative sialidase, SiaHI, by others, indicated that this protein alone may not be responsible for all of the sialidase activity. We describe a second sialidase in T. forsythia (TF0035), an orthologue of Bacteroides fragilis NanH, and its expression in Escherichia coli. Sialidase activity of the expressed NanH was confirmed by using 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid as a substrate. Biochemical characterization of the recombinant T. forsythia NanH indicated that it was active over a broad pH range, with optimum activity at pH 5.5. This enzyme has high affinity for 2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid (K(m) of 32.9 +/- 10.3 microM) and rapidly releases 4-methylumbelliferone (V(max) of 170.8 +/- 11.8 nmol of 4-methylumbelliferone min(-1) mg of protein(-1)). E. coli lysates containing recombinant T. forsythia NanH cleave sialic acid from a range of substrates, with a preference for alpha2-3 glycosidic linkages. The genes adjacent to nanH encode proteins apparently involved in the metabolism of sialic acid, indicating that the NanH sialidase is likely to be involved in nutrient acquisition.

Item Type: Article
Uncontrolled Keywords: oral bacteria; periodontitis; sialidase; virulence
Subjects: Q Science > QR Microbiology
R Medicine > RK Dentistry
Faculty / School / Research Centre / Research Group: Faculty of Engineering & Science
Faculty of Engineering & Science > Natural Resources Institute
Faculty of Engineering & Science > Natural Resources Institute > Agriculture, Health & Environment Department
Faculty of Engineering & Science > Natural Resources Institute > Pest Behaviour Research Group
Last Modified: 24 Feb 2023 11:06
URI: http://gala.gre.ac.uk/id/eprint/38629

Actions (login required)

View Item View Item

Downloads

Downloads per month over past year

View more statistics