title: Differential glycosylation of the ectodomain of the primary envelope glycoprotein of two strains of lactate dehydrogenase-elevating virus that differ in neuropathogenicity.
abstract: ORF 5 encoding the primary envelope glycoprotein, VP-3P, of a highly neuropathogenic isolate of lactate dehydrogenase-elevating virus (LDV-v) has been sequenced. It exhibits 92% nucleotide identity with the ORF 5 of an LDV isolate that lacks neuropathogenicity, LDV-P, and the amino acid identities of the predicted VP-3Ps of the two strains is 90%. Most striking, however, is the absence in the ectodomain of LDV-v VP-3P of two out of three potential N-glycosylation sites present in the ectodomain of VP-3P of LDV-P. The ectodomain of VP-3P has been implicated to play an important role in host receptor interaction. VP-3P of another neuropathogenic LDV strain, LDV-C, lacks the same two N-glycosylation sites (Godeny et al., 1993). In vitro transcription/translation of the ORFs 5 of LDV-P and LDV-v indicated that all three N-glycosylation sites in the ectodomain of LDV-P VP-3P became glycosylated when synthesized in the presence of microsomal membranes, whereas the glycosylation of the ORF 5 proteins of LDV-v and LDV-C was consistent with glycosylation at a single site. No other biological differences between the neuropathogenic and non-neuropathogenic strains have been detected. They replicate with equal efficiency in mice and in primary macrophage cultures.
authors.affiliation: Department of Microbiology, University of Minnesota, Minneapolis 55455, USA.
authors.forename: K S
authors.initials: KS
authors.lastname: Faaberg
authors.forename: G A
authors.initials: GA
authors.lastname: Palmer
authors.forename: C
authors.initials: C
authors.lastname: Even
authors.forename: G W
authors.initials: GW
authors.lastname: Anderson
authors.forename: P G
authors.initials: PG
authors.lastname: Plagemann
mesh_terms: D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D004279:DNA, Viral; D004285:Dogs; D006031:Glycosylation; D007772:Lactate dehydrogenase-elevating virus / Q000737:chemistry* / Q000302:isolation & purification / Q000472:pathogenicity; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D021382:Protein Sorting Signals / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D004279:DNA, Viral; C096094:M-VP-2 protein, lactate dehydrogenase-elevating virus; D008562:Membrane Glycoproteins; D021382:Protein Sorting Signals; C096091:VP-3 protein, lactate dehydrogenase-elevating virus; D014759:Viral Envelope Proteins; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase