ArticleProtein expression and purification2014
Purification and characterization of the acyltransferase involved in biosynthesis of the major mycobacterial cell envelope glycolipid--monoacylated phosphatidylinositol dimannoside.
Article in Protein expression and purification, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Essential role of MptB in the biosynthesis of phosphatidylinositol mannosides, lipomannan and lipoarabinomannan in mycobacteria.The Journal of biological chemistry · 2026Article
- Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA.Science advances · 2021Article
- The Phosphatidyl-Journal of bacteriology · 2021Article
- Article
- Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA.Nature communications · 2016Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Phosphatidylinositol mannosides are essential structural components of the mycobacterial cell envelope. They are implicated in host-pathogen interactions during infection and serve as a basis for biosynthesis of other unique molecules with immunomodulatory properties - mycobacterial lipopolysaccharides lipoarabinomannan and lipomannan. Acyltransferase Rv2611 is involved in one of the initial steps in the assembly of these molecules in Mycobacterium tuberculosis - the attachment of an acyl group to position-6 of the 2-linked mannosyl residue of the phosphatidylinositol mannoside anchor. Although the function of this enzyme was annotated 10 years ago, it has never been completely biochemically characterized due to lack of the pure protein. We have successfully overexpressed and purified MSMEG_2934, the ortholog of Rv2611c from the non-pathogenic model organism Mycobacteriumsmegmatis mc(2)155 using mycobacterial pJAM2 expression system, which allowed confirmation of its in vitro acyltransferase activity, and establishment of its substrate specificity.
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