Assembling of the Mycobacterium tuberculosis Cell Wall Core

Grzegorzewicz, Anna E. and de Sousa-d'Auria, Célia and McNeil, Michael R. and Huc-Claustre, Emilie and Jones, Victoria and Petit, Cécile and Angala, Shiva Kumar and Zemanová, Júlia and Wang, Qinglan and Belardinelli, Juan Manuel and Gao, Qian and Ishizaki, Yoshimasa and Miku�ová, Katarína and Brennan, Patrick J. and Ronning, Donald R. and Chami, Mohamed and Houssin, Christine and Jackson, Mary. (2016) Assembling of the Mycobacterium tuberculosis Cell Wall Core. Journal of Biological Chemistry, 291 (36). pp. 18867-18879.

Full text not available from this repository.

Official URL: https://edoc.unibas.ch/78624/

Downloads: Statistics Overview


The unique cell wall of mycobacteria is essential to their viability and the target of many clinically used anti-tuberculosis drugs and inhibitors under development. Despite intensive efforts to identify the ligase(s) responsible for the covalent attachment of the two major heteropolysaccharides of the mycobacterial cell wall, arabinogalactan (AG) and peptidoglycan (PG), the enzyme or enzymes responsible have remained elusive. We here report on the identification of the two enzymes of Mycobacterium tuberculosis, CpsA1 (Rv3267) and CpsA2 (Rv3484), responsible for this function. CpsA1 and CpsA2 belong to the widespread LytR-Cps2A-Psr (LCP) family of enzymes that has been shown to catalyze a variety of glycopolymer transfer reactions in Gram-positive bacteria, including the attachment of wall teichoic acids to PG. Although individual cpsA1 and cpsA2 knock-outs of M. tuberculosis were readily obtained, the combined inactivation of both genes appears to be lethal. In the closely related microorganism Corynebacterium glutamicum, the ortholog of cpsA1 is the only gene involved in this function, and its conditional knockdown leads to dramatic changes in the cell wall composition and morphology of the bacteria due to extensive shedding of cell wall material in the culture medium as a result of defective attachment of AG to PG. This work marks an important step in our understanding of the biogenesis of the unique cell envelope of mycobacteria and opens new opportunities for drug development.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
05 Faculty of Science > Departement Biozentrum > Services Biozentrum > BioEM Lab (Chami)
UniBasel Contributors:Chami, Mohamed
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society for Biochemistry and Molecular Biology
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:05 Oct 2020 06:39
Deposited On:05 Oct 2020 06:39

Repository Staff Only: item control page