NamZ1 and NamZ2 from the Oral Pathogen Tannerella forsythia Are Peptidoglycan Processing Exo-β- N -Acetylmuramidases with Distinct Substrate Specificities

Author:

Borisova Marina1ORCID,Balbuchta Katja1,Lovering Andrew2,Titz Alexander345ORCID,Mayer Christoph1ORCID

Affiliation:

1. Interfaculty Institute of Microbiology and Infection Medicine, Organismic Interactions/Glycobiology, Eberhard Karls Universität Tübingen, Tübingen, Germany

2. Institute of Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, United Kingdom

3. Chemical Biology of Carbohydrates, Helmholtz Institute for Pharmaceutical Research Saarland, Helmholtz Centre for Infection Research, Saarbrücken, Germany

4. Deutsches Zentrum für Infektionsforschung (DZIF), Standort Hannover-Braunschweig, Germany

5. Department of Chemistry, Saarland University, Saarbrücken, Germany

Abstract

Two exo- N -acetylmuramidases from T. forsythia belonging to glycosidase family GH171 ( www.cazy.org ) were shown to differ in their activities, thus revealing a functional diversity within this family: NamZ1 releases disaccharides (GlcNAc-MurNAc/GlcN-MurNAc) from the nonreducing ends of PGN glycans, whereas NamZ2 releases terminal MurNAc monosaccharides. This work provides a better understanding of how T. forsythia may acquire the essential growth factor MurNAc by the salvage of PGN from cohabiting bacteria in the oral microbiome, which may pave avenues for the development of anti-periodontal drugs.

Funder

Deutsche Forschungsgemeinschaft

Wellcome Trust

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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