Differential glycosylation of the ectodomain of the primary envelope glycoprotein of two strains of lactate dehydrogenase-elevating virus that differ in neuropathogenicity

• Published in: Virus research 1995-12, Vol.39 (2-3), p.331-340
• Main Authors: Faaberg, Kay S., Palmer, Gene A., Even, Chen, Anderson, Grant W., Plagemann, Peter G.W.
• Format: Article
• Language: English
• Subjects: Amidohydrolases - metabolism; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; DNA, Viral; Dogs; Envelope glycoprotein; Glycosylation; Lactate dehydrogenase-elevating virus; Lactate dehydrogenase-elevating virus - chemistry; Lactate dehydrogenase-elevating virus - isolation & purification; Lactate dehydrogenase-elevating virus - pathogenicity; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - genetics; Membrane Glycoproteins - metabolism; Mice; Molecular Sequence Data; Neuropathogenicity; Open Reading Frames; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; Protein Sorting Signals - chemistry; Protein Sorting Signals - metabolism; Sequence Homology, Amino Acid; Structure-Activity Relationship; Viral Envelope Proteins - chemistry; Viral Envelope Proteins - genetics; Viral Envelope Proteins - metabolism
• ISSN: 0168-1702; 1872-7492
• DOI: 10.1016/0168-1702(95)00088-7

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 identify with the ORF 5 of an LDV isolate that lacks neuropathogenicity, LDV-P, and the amino acid identifies of the predicted VP-3Ps of the two strains is 90%. Most striking, however, is the absence 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.