Disease relevance of BUNVsSgp1

• Thus, phylogenetic analysis of the AKA virus N protein gene gives a greater insight into bunyavirus evolution [1].
• Earlier we have shown that Tula hantavirus N protein oligomerization is dependent on the C-terminal domains [2].
• The SSH/LAC/SSH recombinant appears, from polypeptide analysis, to have the SSH type of nucleocapsid protein (N), whereas the SSH/LAC/LAC recombinant has the LAC nucleocapsid protein, suggesting that the viral S RNA codes for the N protein [3].
• The recombinants had the G protein of the Maguari virus parent and the N protein of the Bunyamwera virus parent [4].
• Instead the parental origin of the S RNA subunit was inferred from the electrophoretic mobility of the virion N protein [5].

High impact information on BUNVsSgp1

• Group I appeared to correspond to the genome subunit coding for the N protein, and group II corresponded to the G1/G2 determinant [6].
• All N protein ORFs were 708 nucleotides in length and encoded a 235 amino-acid gene product [7].
• An additional ORF of 150 nucleotides coding for a possible 5.9-kDa protein is present in the +1 reading frame, 3' to the N protein ORF on vcRNA [8].
• In cells infected with ts12 , accumulation of G1 and G2, but not N protein, was observed in the Golgi complex at 39 degrees C. The N protein was found evenly scattered in the cytoplasm, suggesting lack of interaction between the G1/G2 and N proteins [9].
• With ts6 and 11, G1 and G2 appeared to accumulate and aggregate in the endoplasmic reticulum (ER) at 39 degrees C. The location of the N protein coincided with that of the aggregated glycoproteins, suggesting that the N protein interacted with G1/G2 already in the ER [9].

Chemical compound and disease context of BUNVsSgp1

• Analysis of the major Tacaribe virus-specified product by two-dimensional polyacrylamide gel electrophoresis indicated that it had an isoelectric point similar to that of the Tacaribe nucleocapsid polypeptide N; however, the in vitro product had an approximate mol. wt. of 73 000, compared to a mol. wt. of 68 000 for the N protein [10].

Biological context of BUNVsSgp1

• All N protein ORFs were 708 nucleotides in length and encoded a putative 235 amino acid gene product [11].

Analytical, diagnostic and therapeutic context of BUNVsSgp1

• Here we report functional mapping of interacting domains of the Bunyamwera orthobunyavirus N protein by yeast and mammalian two-hybrid systems, immunoprecipitation experiments, and chemical cross-linking studies [12].
• N protein trimerization was supported by three-dimensional reconstruction of the N protein by electron microscopy after negative staining [2].
• The 49.4-kDa product was expressed as a fusion protein with beta-galactosidase in Escherichia coli cells and confirmed as DUG N protein by Western blotting with DUG N-specific monoclonal antibody [8].

References