The role of gp55 N-glycosylation in pathogenesis of Friend spleen focus-forming virus.
The product of the envelope gene (gp55) of Friend spleen focus-forming virus is responsible for the acute form of erythroleukaemia caused by this virus. In order to investigate the role that the four known N-linked carbohydrate side-chains of gp55 play in pathogenesis, we have inactivated the four N-glycosylation signals by mutating the asparagine residues of these four sites into serine. When glycosylation sites 1 and/or 2 were altered, the viruses remained fully pathogenic. However, mutation at either of glycosylation sites 3 or 4 rendered the virus apathogenic, independent of mutations at other sites. Furthermore, when site 3 was changed, a new product appeared which seemed to have acquired a carbohydrate chain at a position normally not glycosylated, presumably at position Asn378.
Rau
S
S
Institute of Medical Virology, Justus Liebig University, Giessen, Germany.
Geyer
R
R
Friedrich
R W
RW
D000818:Animals; D001483:Base Sequence; D015686:Gene Products, env / Q000737:chemistry / Q000378:metabolism*; D006023:Glycoproteins / Q000502:physiology; D006031:Glycosylation; D004915:Leukemia, Erythroblastic, Acute / Q000382:microbiology; D007942:Leukemia, Experimental / Q000382:microbiology; D051379:Mice; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016297:Mutagenesis, Site-Directed; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D013155:Spleen Focus-Forming Viruses / Q000737:chemistry / Q000472:pathogenicity*; D013329:Structure-Activity Relationship
D015686:Gene Products, env; D006023:Glycoproteins; D009838:Oligodeoxyribonucleotides