ArticleThe Journal of biological chemistry2016
Assembling of the Mycobacterium tuberculosis Cell Wall Core.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 69 citations in OpenAlex.
- Over-expression, purification, and kinetic analysis ofJournal of enzyme inhibition and medicinal chemistry · 2026Article
- The SigD regulon of Mycobacterium abscessus determines cell envelope composition and antibiotic susceptibility.PLoS genetics · 2026Article
- Rv3839-Rv3840 links the endogenous heme biosynthesis pathway with Mycobacterium tuberculosis adaptation to nitric oxide and iron limitation stress.PLoS genetics · 2026Article
- Structural basis of lipid-linked galactan export by the mycobacterial ABC transporter Wzm-Wzt.Nature communications · 2026Article
- Rv3839-Rv3840 links the endogenous heme biosynthesis pathway withbioRxiv : the preprint server for biology · 2026Article
- Naturally occurring dinactin targets cpsA protein and kills Mycobacterium tuberculosis by disrupting the proton motive force.Communications biology · 2026Article
- Impairment of two non-essential LytR-cpsA-psr (Lcp) cell wall ligases decelerate cell wall assembly in Mycolicibacterium smegmatis.BMC microbiology · 2026Article
- The AcasR-FadD9 regulatory axis modulates iron homeostasis and susceptibility to the anti-mycobacterial compound ACA.Frontiers in tuberculosis · 2026Article
- Protein Architecture and Composition in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- ACA kills Mycobacterium tuberculosis and M. bovis by targeting cell wall core assembling protein CpsA.Communications biology · 2025Article
- Generation of novel polyclonal antibodies against Mycobacterium tuberculosis lipoarabinomannan, EspB, and Mtb8.Applied microbiology and biotechnology · 2025Article
- The identification Mycobacterium tuberculosis genes that modulate long term survival in the presence of rifampicin and streptomycin.Scientific reports · 2025Article
- Protein kinase G-a key regulator of pathogenesis in Mycobacterium tuberculosis infection.Archives of microbiology · 2025Review
- Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimE.Nature communications · 2025Article
- Structural insights into terminal arabinosylation of mycobacterial cell wall arabinan.Nature communications · 2025Article
- Article
- EmbB and EmbC regulate the sensitivity ofmLife · 2024Article
- Mycobacterial CpsA activates type I IFN signaling in macrophages via cGAS-mediated pathway.iScience · 2024Article
- Review
- Preference of Bacterial Rhamnosyltransferases for 6-Deoxysugars Reveals a Strategy To Deplete O-Antigens.Journal of the American Chemical Society · 2023Article
Corrections and comments
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Authors and funding
18 authors at 6 institutions in 5 countries.
Funding
Abstract
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.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.