HOST-CELL-SPECIFIC GLYCOSYLATION OF HIV-2 ENVELOPE GLYCOPROTEIN

Neutral complex-type N-glycans of the envelope glycoprotein 120 of HIV -2, propagated in different host cells, display cell-type specific var iations. In order to identify typical structural elements, glycans wer e analysed by gel filtration, by enzymic sequencing and, in part, by m atrix-assisted laser desorption/ionization time-of-flight mass spectro metry. The characteristic substituents of di-tri-and tetraantennary ca rbohydrate units thus observed include N-acetyllactosamine repeats, bi secting N-acetylglucosamine and fucose linked to the chitobiose core a s well as to N-acetyllactosamine antennae. Each glycoprotein preparati on displayed a characteristic set of glycoforms.