AftD functions as an α1→5 arabinofuranosyltransferase involved in the biosynthesis of the mycobacterial cell wall core

Luke J. Alderwick, Helen L. Birch, Karin Krumbach, Michael Bott, Lothar Eggeling, Gurdyal S. Besra

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)
130 Downloads (Pure)

Abstract

Arabinogalactan (AG) is an essential structural macromolecule present in the cell wall of Mycobacterium tuberculosis, serving to connect peptidoglycan with the outer mycolic acid layer. The D-arabinan segment is a highly branched component of AG and is assembled in a step-wise fashion by a variety of arabinofuranosyltransferases (AraT). We have previously used Corynebacterium glutamicum as a model organism to study these complex processes which are otherwise essential in mycobacteria. In order to further our understanding of the molecular basis of AG assembly, we investigated the role of a fourth AraT, now termed AftD by generating single (ΔaftD) and double deletion (ΔaftB ΔaftD) mutants of C. glutamicum. We demonstrate that AftD functions as an α(1→5) AraT and reveal the point at which it exerts its activity in the AG biosynthetic pathway.
Original languageEnglish
Pages (from-to)2-14
JournalThe Cell Surface
Volume1
Early online date1 Dec 2017
DOIs
Publication statusPublished - Mar 2018

Keywords

  • Corynebacterium glutamicum
  • Mycobacterium tuberculosis
  • cell wall
  • Arabinogalacan
  • Glycosyltransferase

Fingerprint

Dive into the research topics of 'AftD functions as an α1→5 arabinofuranosyltransferase involved in the biosynthesis of the mycobacterial cell wall core'. Together they form a unique fingerprint.

Cite this