01963nas a2200253   4500000000100000008004100001260004900042653001200091653002600103653002400129653001600153653001100169653001200180653002500192653002000217100001500237700001500252245012000267856005100387300001100438490000700449520123900456022001401695       2011                            d  c2011 DecbLEPRA Health in ActionaColchester10aAnimals10aAntibodies, Bacterial10aAntigens, Bacterial10aGlycolipids10aHumans10aleprosy10aMycobacterium leprae10aSerologic Tests1 aSpencer JS1 aBrennan PJ00aThe role of Mycobacterium leprae phenolic glycolipid I (PGL-I) in serodiagnosis and in the pathogenesis of leprosy.  uhttps://leprosyreview.org/article/82/4/34-4357  a344-570 v823 a<p>PGL-I (phenolic glycolipid I) emerged in the early 1980s on the one hand as part of intensive efforts to define the typing antigens of a host of Mycobacterium spp. and also from characterisation of the lipids of skin biopsies from highly bacillary positive lepromatous leprosy patients. PGL-I, despite its extreme lipophilicity due to its inherent phthiocerol dimycocerosyl component, is highly antigenic evoking high titre IgM antibodies in lepromatous leprosy patients, attributable largely to the unique 3,6-di-O-methyl-beta-D-glucosyl entity at the non-reducing terminus of its trisaccharide. PGL-I itself or in the form of semisynthetic neoglycoproteins containing the synthetic terminal disaccharide or the whole trisaccharide chemically conjugated to such as bovine or human serum albumin, has found its greatest utility in the serological diagnosis, confirmation and management of lepromatous leprosy. PGL-I has also been implicated in the tropism of M. leprae for Schwann cells, through specific binding to laminin, and to play an important role in downregulation of the inflammatory immune response and inhibition of dendritic cell maturation and activation, thereby facilitating the persistence of M. leprae/leprosy.</p>  a0305-7518