Glycosylate and move! The glycosyltransferase Maf is involved in bacterial flagella formation

Environmental Microbiology
Gerlind SulzenbacherFrançois Alberto

Abstract

The flagella of various Gram-negative bacteria are decorated with diverse glycan structures, amongst them nonulosonic acids related to the sialic acid family. Although nonulosonic sugar biosynthesis pathways have been dissected in various pathogens, the enzymes transferring the sugars onto flagellin are still poorly characterized. The deletion of genes coding for motility associated factors (Mafs) found in many pathogenic strains systematically gives rise to nonflagellated bacteria lacking specific nonulosonic sugars on the flagellins, therefore, relating Maf function to flagellin glycosylation and bacterial motility. We investigated the role of Maf from our model organism, Magnetospirillum magneticum AMB-1, in the glycosylation and formation of the flagellum. Deletion of the gene amb0685 coding for Maf produced a nonflagellated bacterium where the flagellin was still produced but no longer glycosylated. Our X-ray structure analysis revealed that the central domain of Maf exhibits similarity to sialyltransferases from Campylobacter jejuni. Glycan analysis suggested that the nonulosonic carbohydrate structure transferred is pseudaminic acid or a very close derivative. This work describes the importance of glycosylation in the fo...Continue Reading

References

Oct 5, 1990·Journal of Molecular Biology·S F AltschulD J Lipman
Sep 5, 1993·Journal of Molecular Biology·L Holm, C Sander
Dec 11, 1999·Nucleic Acids Research·H M BermanP E Bourne
Jul 20, 2001·The Journal of Biological Chemistry·P ThibaultP Guerry
Jan 20, 2004·Nature Structural & Molecular Biology·Cecilia P C ChiuNatalie C J Strynadka
Mar 9, 2004·Proceedings of the National Academy of Sciences of the United States of America·Arash KomeiliDianne K Newman
Jul 21, 2004·Journal of Computational Chemistry·Eric F PettersenThomas E Ferrin
May 1, 1997·Acta Crystallographica. Section D, Biological Crystallography·G N MurshudovE J Dodson
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·E Krissinel, K Henrick
May 26, 2005·Protein Expression and Purification·F William Studier
Dec 31, 2005·Journal of Bacteriology·Rocío CanalsSusana Merino
Sep 20, 2006·Journal of Molecular Microbiology and Biotechnology·Sandy Y M NgKen F Jarrell
Aug 8, 2007·Journal of Molecular Biology·Evgeny Krissinel, Kim Henrick
Aug 12, 2009·Proceedings of the National Academy of Sciences of the United States of America·Amanda L LewisAjit Varki
Sep 15, 2009·Journal of Bacteriology·Susan M TwineSusan M Logan
Jan 9, 2010·Acta Crystallographica. Section D, Biological Crystallography·Vincent B ChenDavid C Richardson
Feb 4, 2010·Acta Crystallographica. Section D, Biological Crystallography·Wolfgang Kabsch
Mar 10, 2010·Proceedings of the National Academy of Sciences of the United States of America·Dorothée MuratArash Komeili
Apr 13, 2010·Acta Crystallographica. Section D, Biological Crystallography·P EmsleyK Cowtan
Oct 16, 2010·Nature Reviews. Microbiology·Harald Nothaft, Christine M Szymanski
Apr 5, 2011·Acta Crystallographica. Section D, Biological Crystallography·Navraj S PannuRudolf A G de Graaff
Jun 1, 2011·Nucleic Acids Research·Aurélien GrosdidierOlivier Michielin
Oct 11, 2011·PloS One·Patrick S HopfCarole Creuzenet
Apr 20, 2012·Journal of Synchrotron Radiation·Daniele de SanctisChristoph Mueller-Dieckmann
Aug 3, 2012·BMC Microbiology·Jessica N RicaldiAmanda L Lewis
May 18, 2013·Molecular Microbiology·Jeremy A IwashkiwMario F Feldman
Jun 26, 2013·Acta Crystallographica. Section D, Biological Crystallography·Philip R Evans, Garib N Murshudov
Sep 17, 2013·PloS One·Sebastian BubendorferKai M Thormann
Nov 26, 2013·Nucleic Acids Research·Vincent LombardBernard Henrissat

❮ Previous
Next ❯

Citations

Jan 17, 2020·Chembiochem : a European Journal of Chemical Biology·Emily K P FlackMartin A Fascione
Mar 7, 2020·Microorganisms·Juan Luis Araujo-GarridoFrancisco Ramos-Morales
Jul 30, 2020·Scientific Reports·Hugo F AzurmendiWillie F Vann

❮ Previous
Next ❯

Related Concepts

Related Feeds

Bacterial Protein Structures

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.

Campylobacteriosis (ASM)

Campylobacteriosis is caused by the bacteria Campylobacter jejuni and is a common cause of gastroenteritis in humans. Discover the latest research on Campylobacteriosis here.

Bacterial Protein Structures (ASM)

Bacterial protein structures can expedite the development of novel antibiotics. Here is the latest research on bacterial proteins and the resolution of their structures.