01989nas a2200337   4500000000100000008004100001260001600042653002300058653001800081653004200099653002500141653001100166653002400177653001500201653002500216653002300241653001800264653003100282653002600313653002500339100001300364700002000377700001300397700001500410700001400425245010400439300001300543490000800556520107300564022001401637       2010                            d  c2010 Oct 2910aBacterial Proteins10aCell Membrane10aGene Expression Regulation, Bacterial10aGlycerophospholipids10aLipids10aLipopolysaccharides10aMannosides10aMannosyltransferases10aModels, Biological10aMycobacterium10aMycobacterium tuberculosis10aPhosphatidylinositols10aProtein Conformation1 aGuerin M1 aKorduláková J1 aAlzari P1 aBrennan PJ1 aJackson M00aMolecular basis of phosphatidyl-myo-inositol mannoside biosynthesis and regulation in mycobacteria.  a33577-830 v2853 a<p>Phosphatidyl-myo-inositol mannosides (PIMs) are unique glycolipids found in abundant quantities in the inner and outer membranes of the cell envelope of all Mycobacterium species. They are based on a phosphatidyl-myo-inositol lipid anchor carrying one to six mannose residues and up to four acyl chains. PIMs are considered not only essential structural components of the cell envelope but also the structural basis of the lipoglycans (lipomannan and lipoarabinomannan), all important molecules implicated in host-pathogen interactions in the course of tuberculosis and leprosy. Although the chemical structure of PIMs is now well established, knowledge of the enzymes and sequential events leading to their biosynthesis and regulation is still incomplete. Recent advances in the identification of key proteins involved in PIM biogenesis and the determination of the three-dimensional structures of the essential phosphatidyl-myo-inositol mannosyltransferase PimA and the lipoprotein LpqW have led to important insights into the molecular basis of this pathway.</p>  a1083-351X