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PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1.

PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Research Abstract Details 

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  • PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Abstract Text:

    pawan kumarPawan Kumar,michael w schelleMichael W Schelle,madhulika jainMadhulika Jain,fiona l linFiona L Lin,christopher j petzoldChristopher J Petzold,michael d leavellMichael D Leavell,julie a learyJulie A Leary,jeffery s coxJeffery S Cox,carolyn r bertozziCarolyn R Bertozzi,

    Mycobacterium tuberculosis produces numerous exotic lipids that have been implicated as virulence determinants. One such glycolipid, Sulfolipid-1 (SL-1), consists of a trehalose-2-sulfate (T2S) core acylated with four lipid moieties. A diacylated intermediate in SL-1 biosynthesis, SL(1278), has been shown to activate the adaptive immune response in human patients. Although several proteins involved in SL-1 biosynthesis have been identified, the enzymes that acylate the T2S core to form SL(1278) and SL-1, and the biosynthetic order of these acylation reactions, are unknown. Here we demonstrate that PapA2 and PapA1 are responsible for the sequential acylation of T2S to form SL(1278) and are essential for SL-1 biosynthesis. In vitro, recombinant PapA2 converts T2S to 2'-palmitoyl T2S, and PapA1 further elaborates this newly identified SL-1 intermediate to an analog of SL(1278). Disruption of papA2 and papA1 in M. tuberculosis confirmed their essential role in SL-1 biosynthesis and their order of action. Finally, the Delta papA2 and Delta papA1 mutants were screened for virulence defects in a mouse model of infection. The loss of SL-1 (and SL(1278)) did not appear to affect bacterial replication or trafficking, suggesting that the functions of SL-1 are specific to human infection.

    PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Publishing Authors By Initials

    p kumarP Kumar,mw schelleMW Schelle,m jainM Jain,fl linFL Lin,cj petzoldCJ Petzold,md leavellMD Leavell,ja learyJA Leary,js coxJS Cox,cr bertozziCR Bertozzi,

    For similar biological factors: toxins, biological: virulence factors research abstracts see: biological factors: toxins, biological: virulence factors research

    PUBMED ID PMID:

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    PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Proceedings of the National Academy of Sciences of

    VOLUME: 104

    Page Numbers: 11221-6

    Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

    ISSN: 0027-8424

    DAY: 25

    MONTH: 06

    YEAR: 2007

    PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 7505876

    PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Keywords Mesh Terms:

    KEYWORDS: Virulence Factors

    MESH TERMS: biosynthesis

    Chemical & Substance for Abstract: PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1. Information

    Substance Name: Acyltransferases

    Registry Number: EC 2.3.-

    Grant and Affiliation Information for PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1.

    AFFILIATION: Department of Chemistry and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIAID

    GRANT: AI51667

    ACRONYM: AI

    MEDLINETA: Proc Natl Acad Sci U S A

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    PapA1 and PapA2 are acyltransferases essential for the biosynthesis of the Mycobacterium tuberculosis virulence factor sulfolipid-1 Related Publications

     

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