lcp1 is a phosphotransferase responsible for ligating arabinogalactan to peptidoglycan in mycobacterium tuberculosis

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ID: 239786
2016
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Abstract
Mycobacterium tuberculosis, the etiological agent of tuberculosis (TB), has a unique cell envelope which accounts for its unusual low permeability and contributes to resistance against common antibiotics. The main structural elements of the cell wall consist of a cross-linked network of peptidoglycan (PG) in which some of the muramic acid residues are covalently attached to a complex polysaccharide, arabinogalactan (AG), via a unique α-l-rhamnopyranose–(1→3)-α-d-GlcNAc-(1→P) linker unit. While the molecular genetics associated with PG and AG biosynthetic pathways have been largely delineated, the mechanism by which these two major pathways converge has remained elusive. In Gram-positive organisms, the LytR-CpsA-Psr (LCP) family of proteins are responsible for ligating cell wall teichoic acids to peptidoglycan, through a linker unit that bears a striking resemblance to that found in mycobacterial arabinogalactan. In this study, we have identified Rv3267 as a mycobacterial LCP homolog gene that encodes a phosphotransferase which we have named Lcp1. We demonstrate that lcp1 is an essential gene required for cell viability and show that recombinant Lcp1 is capable of ligating AG to PG in a cell-free radiolabeling assay.
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harrison2016mbiolcp1 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;James Harrison;Georgina Lloyd;Maju Joe;Todd L. Lowary;Edward Reynolds;Hannah Walters-Morgan;Apoorva Bhatt;Andrew Lovering;Gurdyal S. Besra;Luke J. Alderwick
Journal synlett
Year 2016
DOI
10.1128/mBio.00972-16
URL
http://mbio.asm.org/cgi/content/full/7/4/e00972-16
Keywords
Microbiology

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