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1 direct interaction of the M. leprae-specific phenolic glycolipid 1 (PGL-1) with myelinating glia and
2 nt of the specific trisaccharide unit of the phenolic glycolipid-1 (PGL-1) of Mycobacterium leprae in
5 ic glycopeptidolipids, lipooligosaccharides, phenolic glycolipids, and the genus-specific phosphatidy
7 yielded distinct groups that correlated with phenolic glycolipid I reactivity and clinical diagnosis,
8 nd peripheral blood samples, along with anti-phenolic glycolipid I serology and skin tests from the s
12 y has demonstrated that the species-specific phenolic glycolipid of Mycobacterium leprae triggers upt
14 d a critical role for mycobacterial membrane phenolic glycolipid (PGL) in engineering this transition
15 lipid species-a polyketide synthase-derived phenolic glycolipid (PGL) produced by a subset of M. tub
16 on by HN878 of a polyketide synthase-derived phenolic glycolipid (PGL), as demonstrated by reduced vi
18 tudies reveal in vivo functions for specific phenolic glycolipids (PGLs) in the mycobacteria that cau
22 ly from hydrophilic lipooligosaccharides and phenolic glycolipids to hydrophobic phthiocerol dimycoce
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