NDLI: New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis.

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New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis.

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New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Guerin, Marcelo E. Gest, Petra Somashekar, B. S. Chatterjee, Delphi Brennan, Patrick J. Gibbs, Sara Kaur, Devinder Jackson, Mary
Description	Author Affiliation: Guerin ME ( Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, Colorado 80523-1682, USA. mrcguerin@gmail.com)
Abstract	Phosphatidyl-myo-inositol mannosides (PIMs) are key glycolipids of the mycobacterial cell envelope. They are considered not only essential structural components of the cell but also important molecules implicated in host-pathogen interactions. Although their chemical structures are well established, knowledge of the enzymes and sequential events leading to their biosynthesis is still incomplete. Here we show for the first time that although both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol (PI) as a lipid acceptor, PimA specifically catalyzes the transfer of a Manp residue to the 2-position of the myo-inositol ring of PI, whereas PimB' exclusively transfers to the 6-position. Moreover, whereas PimB' can catalyze the transfer of a Manp residue onto the PI-monomannoside (PIM1) product of PimA, PimA is unable in vitro to transfer Manp onto the PIM1 product of PimB'. Further assays using membranes from Mycobacterium smegmatis and purified PimA and PimB' indicated that the acylation of the Manp residue transferred by PimA preferentially occurs after the second Manp residue has been added by PimB'. Importantly, genetic evidence is provided that pimB' is an essential gene of M. smegmatis. Altogether, our results support a model wherein Ac1PIM2, a major form of PIMs produced by mycobacteria, arises from the consecutive action of PimA, followed by PimB', and finally the acyltransferase MSMEG_2934. The essentiality of these three enzymes emphasizes the interest of novel anti-tuberculosis drugs targeting the initial steps of PIM biosynthesis.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	38
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-09-18
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism Cell Membrane Enzymology Mannosyltransferases Mycobacterium Smegmatis Phosphatidylinositols Biosynthesis Antitubercular Agents Antagonists & Inhibitors Chemistry Isolation & Purification Mannose Pathogenicity Tuberculosis Drug Therapy Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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