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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1994-2-24
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pubmed:abstractText |
The application of extracellular arabinases from a Cellulomonas sp. and fast atom bombardment-mass spectrometry (FAB-MS) provided new insight into the structure of lipoarabinomannan (LAM) of Mycobacterium tuberculosis, a key molecule in the pathogenesis and physiology of the tubercle bacillus. Previously, the non-reducing arabinan ends of LAM from the virulent (Erdman) strain of M. tuberculosis were shown to be 'capped' by short (alpha 1-->2)-linked mannopyranose (Manp)-containing oligosaccharides, a product called ManLAM. The structural relationship between these Manp units and the underlying arabinofuranose (Araf)-containing arabinan was examined by digesting ManLAM from M.tuberculosis Erdman with the Cellulomonas enzyme, resolving fragments by various means and subjecting the derivatized oligoglycosylalditols to FAB-MS. The sequences Manp2Araf4, Manp3Araf4 and Manp1-6Araf6 were recognized as the major terminal motifs. Upon complete structural definition, all of the Ara6-containing products were shown to be based on a 3,5-linked branched Araf unit, whereas those containing Ara4 were linear. Minor non-mannosylated terminal arrangements containing Ara4-6, branched, linear and cyclical, were also recognized. In addition, the mannan 'core' of ManLAM was isolated from enzyme digests and shown to contain segments of the phosphatidylinositol anchor and a 'stub' of the arabinan side-chain in the form of a 'linker' alpha-Araf-(1-->5)-Araf unit attached to C-2, apparently of the penultimate 2,6-linked Manp residue. The structural unravelling of this complex molecule further substantiates the case for structural and biological similarities to the enterobacterial lipopolysaccharides/lipoglycans and other important 'capped' lipooligomers such as the lipooligosaccharides of Neisseria species and the lipophosphoglycan of Leishmania promastigotes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0959-6658
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
497-506
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pubmed:dateRevised |
2009-9-29
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pubmed:meshHeading |
pubmed-meshheading:8286863-Carbohydrate Sequence,
pubmed-meshheading:8286863-Glycosylation,
pubmed-meshheading:8286863-Lipopolysaccharides,
pubmed-meshheading:8286863-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8286863-Molecular Sequence Data,
pubmed-meshheading:8286863-Molecular Structure,
pubmed-meshheading:8286863-Mycobacterium tuberculosis,
pubmed-meshheading:8286863-Oxidation-Reduction,
pubmed-meshheading:8286863-Spectrometry, Mass, Fast Atom Bombardment,
pubmed-meshheading:8286863-Virulence
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pubmed:year |
1993
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pubmed:articleTitle |
Structural definition of the non-reducing termini of mannose-capped LAM from Mycobacterium tuberculosis through selective enzymatic degradation and fast atom bombardment-mass spectrometry.
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pubmed:affiliation |
Department of Microbiology, Colorado State University, Fort Collins 80523.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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