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

Kay S. Faaberg, Gene A. Palmer, Chen Even, Grant W. Anderson, Peter G.W. Plagemann

Research output: Contribution to journalArticle

14 Scopus citations

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 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.

Original languageEnglish (US)
Pages (from-to)331-340
Number of pages10
JournalVirus research
Volume39
Issue number2-3
DOIs
StatePublished - Dec 1995

Keywords

  • Envelope glycoprotein
  • Glycosylation
  • Lactate dehydrogenase-elevating virus
  • Neuropathogenicity

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