Disease relevance of G

• Characterization of Borna disease virus p56 protein, a surface glycoprotein involved in virus entry [1].
• Our findings suggest that BVp56 exhibits a novel form of processing for an animal NNS RNA virus surface glycoprotein, which might influence the assembly and budding of BDV [1].
• The major structural glycoprotein E2 of classical swine fever virus (CSFV) is responsible for eliciting neutralizing antibodies and conferring protective immunity [2].
• Subdivision of the pestivirus genus based on envelope glycoprotein E2 [3].
• The maturation of Borna disease virus (BDV) glycoprotein GP was studied in regard to intracellular compartmentalization, compartmentalization signal-domains, proteolytic processing, and packaging into virus particles [4].

High impact information on G

• Borna disease virus glycoprotein is required for viral dissemination in neurons [5].
• We assessed whether the viral envelope glycoprotein (GP) is required for neuronal dissemination of BDV by using primary cultures of rat hippocampal neurons [5].
• Enhanced neurovirulence of borna disease virus variants associated with nucleotide changes in the glycoprotein and L polymerase genes [6].
• In concert these findings indicate that ORF IV encodes a 94-kDa N-linked glycoprotein with extensive high mannose- and/or hybrid-type oligosaccharide modifications [7].
• Whereas the N and P ORFs are translated from monocistronic transcripts, the M, G, and pol ORFs are translated from polycistronic transcripts [8].

Chemical compound and disease context of G

• The only surface membrane glycoprotein of Borna disease virus (BDV) is synthesized as a polypeptide with a molecular mass of 57 kDa and N-glycosylated to a precursor glycoprotein (GP) of about 94 kDa [9].

Biological context of G

• Differential splicing of the two introns and cytoplasmic accumulation of the unspliced and partially spliced RNA are critical for the balanced expression of the putative matrix protein, glycoprotein, and polymerase [10].
• Nested amplification of the second region was designed to differentiate HCV from BVDV and BDV by exploiting relatively conserved differences in the nucleotide sequences that encode the major envelope glycoprotein [11].
• Identification of a novel virulence determinant within the E2 structural glycoprotein of classical swine fever virus [12].
• The envelope glycoprotein E2 is a determinant of cell culture tropism in ruminant pestiviruses [13].
• Inhibition of Borna disease virus-mediated cell fusion by monoclonal antibodies directed against the viral glycoprotein [14].

Anatomical context of G

• At birth, the clinically affected lambs had diffuse spinal cord hypomyelination, confirmed by immunocytochemical staining for myelin-associated glycoprotein and myelin basic protein [15].
• Scattered myelin-associated glycoprotein-positive oligodendrocytes were positive for BDV antigen, but only in the infected cultures from the older fetuses [16].
• Borna disease virus-infected Vero cells express on their surface the major viral glycoprotein which mediates cell fusion after low pH treatment [14].

Other interactions of G

• Lectin binding and endoglycosidase sensitivity assays indicate that gp18 is an unusual N-linked glycoprotein [17].

Analytical, diagnostic and therapeutic context of G

• The complex-trapping-blocking (CTB) ELISA for detection of antibodies against classical swine fever virus (CSFV) using two monoclonal antibodies (mAbs) directed against envelope glycoprotein E2, has been improved using recombinant CSFV E2-antigen [18].

References