02473nas a2200397   4500000000100000008004100001260001300042653003800055653002400093653001200117653002400129653001500153653002300168653001400191653003700205653001800242653001600260653002400276653001100300653002800311653002000339653002500359653003300384653002200417653003400439653002600473100001600499700001400515700001600529700001800545245010100563300001200664490000700676520137800683022001402061       1998                            d  c1998 Jun10aATP-Binding Cassette Transporters10aAmino Acid Sequence10aAnimals10aAntigens, Bacterial10aArmadillos10aBacterial Proteins10aCell Wall10aCentrifugation, Density Gradient10aChaperonin 6010aChaperonins10aDiaminopimelic Acid10aLipids10aMolecular Sequence Data10aMonosaccharides10aMycobacterium leprae10aPeptide Elongation Factor Tu10aSequence Analysis10aSequence Homology, Amino Acid10aSubcellular Fractions1 aMarques M A1 aChitale S1 aBrennan P J1 aPessolani M C00aMapping and identification of the major cell wall-associated components of Mycobacterium leprae.  a2625-310 v663 a<p>Mycobacterium leprae, an obligate intracellular pathogen, can be derived only from host tissue and thus affords the opportunity to study in vivo-expressed products responsible for the particular pathogenesis of leprosy. Despite considerable progress in the characterization of the proteins and secondary gene products of M. leprae, there is little information on the nature of the proteins associated with the cell envelope. M. leprae has been fractionated into its major subcellular components, cell wall, cytoplasmic membrane, and soluble cytosol. A number of biochemical markers, including diaminopimelic acid content, monosaccharide composition, mycolic acid, and glycolipid distribution, were applied to their characterization, and two-dimensional gel electrophoresis was used to map the component proteins. A total of 391 major proteins spots were resolved, and 8 proteins were identified based on their reactivity to a panel of monoclonal antibodies and/or relative pI size. Microsequencing of six protein spots present in the cell wall fraction allowed identification of new proteins, including the protein elongation factor EF-Tu and a homolog for the Mycobacterium tuberculosis MtrA response regulator. These results, together with previous studies, contribute to the progressive knowledge of the composition of the in vivo-expressed proteins of M. leprae.</p>  a0019-9567