Glycoproteins as components of cell surfaces are not restricted to eukaryotes. The prokaryotic glycoprotein studied in greatest detail so far is the cell surface glycoprotein of the archaebacterium Halobacterium halobium. This bacterial glycoprotein contains 3 different types of glycoconjugates, and each type of glycoconjugate involves a different carbohydrate-protein linkage unit: 1) One glycosaminoglycan chain, constructed from a repeating sulfated pentasaccharide block, is linked to one protein molecule via the novel N-glycosyl linkage unit asparaginyl-N-acetylgalactosamine. 2) Ten sulfated oligosaccharides that contain glucose, glucuronic acid and iduronic acid are bound to the protein via the hitherto unknown N-glycosyl linkage unit asparaginylglucose. 3) About 15 disaccharides, glucosylgalactose, are O-glycosyl-linked to a cluster of threonine residues close to the C-terminus of the core protein. The overall structure of the cell surface glycoprotein of halobacteria is thus reminiscent of animal proteoglycans and a functional role of the glycosaminoglycan chain in maintaining the rod shape of halobacteria is discussed. Biosynthesis of the two N-glycosyl linkage units involves dolichol monophosphate and dolicholdiphosphate-linked saccharide precursors. Sulfation and epimerization of the glycoconjugates occur at the lipid-linked level and the mature saccharides are transferred to the protein core on the cell surface. The sulfated oligosaccharides that finally become bound to asparagine via glucose are transiently methylated at their lipid-linked stage and this transient chemical modification seems to be required for the biosynthesis of the corresponding N-glycosyl bond.