Literature DB >> 2504012

Structure and function of mycobacterial glycolipids and glycopeptidolipids.

D Chatterjee1, S W Hunter, M McNeil, I Jardine, P J Brennan.   

Abstract

Earlier work from this and other laboratories has revealed the presence within Mycobacterium spp. of three classes of glycolipid antigens which we have called the glycopeptidolipids, the lipooligosaccharides and the phenolic glycolipids. Representative structures of each from different species and sub-species have been proposed. More recently, new variants of these antigens and older structures have been analyzed by Fourier transform infrared, NMR, particularly at high temperatures, and, most notably, by fast atom bombardment and Californium desorption mass spectrometry. Extraordinary novelty and diversity were revealed, particularly at the distal non-reducing end of the oligosaccharide chains, marked by the presence of new branched-chain sugars, amino sugars and sugar acids. These epitopes and monoclonal antibodies to them have been used for the critical identification of mycobacteria. In addition, the pure antigens are the basis of specific serological tests for various mycobacterioses. The resurgence of interest in "atypical" mycobacteria stems from their occurrence as opportunistic pathogens in many patients with acquired immunodeficiency syndrome, although they have long been associated with pulmonary and other organ infections. Foremost among these mycobacteria are serovars of the Mycobacterium avium-Mycobacterium intracellulare complex (the M. avium complex). The surface antigens which differentiate these serovars are glycopeptidolipids, related to "mycoside C" and, accordingly, composed of a glycosylated lipopeptide "core", fatty acyl-D-Phe-D-alloThr-D-Ala-L-acanyl-O- (3,4-di-O-methyl-alpha-L-rhamnopyranoside), to which a haptenic oligosaccharide is linked at the threonine substituent; this oligoglycosyl unit is the source of type specificity.(ABSTRACT TRUNCATED AT 250 WORDS)

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Year:  1989        PMID: 2504012

Source DB:  PubMed          Journal:  Acta Leprol        ISSN: 0001-5938


  2 in total

1.  Human {beta}-defensin 2 is expressed and associated with Mycobacterium tuberculosis during infection of human alveolar epithelial cells.

Authors:  Bruno Rivas-Santiago; Stephan K Schwander; Carmen Sarabia; Gill Diamond; Marcia E Klein-Patel; Rogelio Hernandez-Pando; Jerrold J Ellner; Eduardo Sada
Journal:  Infect Immun       Date:  2005-08       Impact factor: 3.441

2.  Differentiation of mycobacteria on the basis of chemotype profiles by using matrix solid-phase dispersion and thin-layer chromatography.

Authors:  M E Hines; K S Frazier
Journal:  J Clin Microbiol       Date:  1993-03       Impact factor: 5.948

  2 in total

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