Disease relevance of BUNVsLgp1

• The suitability of this system to delineate functional domains within the Bunyamwera virus L protein is discussed [1].
• Expression of functional Bunyamwera virus L protein by recombinant vaccinia viruses [1].
• The recombinant L protein was able to replicate negative-sense RNA supplied by transfected virion-derived nucleocapsids, and both positive- and negative-sense RNAs were synthesized [2].
• Hence the initiation of mRNA transcription by the recombinant L protein resembles that seen during authentic bunyavirus infection and suggests that the L protein has the endonuclease activity which generates the primers [2].
• Detection of the L protein of tomato spotted wilt virus [3].

High impact information on BUNVsLgp1

• Characterization of Bunyamwera virus S RNA that is transcribed and replicated by the L protein expressed from recombinant vaccinia virus [2].
• Previously we reported expression of the Bunyamwera virus L (polymerase) protein by recombinant vaccinia virus and demonstrated that the recombinant L protein was functional in terms of RNA synthesis activity in a nucleocapsid transfection assay (H. Jin and R. M. Elliott, J. Virol. 65: 4182-4189, 1991) [2].
• Comparison with the L protein sequences of other members of the Bunyaviridae showed homology with the Rift Valley fever phlebovirus L protein (38% amino acid identity), but no detectable similarity with bunyavirus, hantavirus or tospovirus L proteins [4].
• The viral-complementary RNA contains a single large open reading frame of 2104 codons which corresponds to the L protein (M(r) 241039) [4].
• Mutagenesis of the L protein encoded by Bunyamwera virus and production of monospecific antibodies [5].

Biological context of BUNVsLgp1

• The amino-terminal 46 amino acids of the L protein show strong homology (63% identity) with the amino-termini of ORFs predicted from limited sequence analysis of the L segments of La Crosse and snowshoe hare bunyaviruses [6].
• Site-specific mutations were made in the L cDNA-containing plasmid to change certain amino acids in the putative polymerase domain of the L protein [5].

Analytical, diagnostic and therapeutic context of BUNVsLgp1

• Of five fusion proteins injected into rabbits, three yielded sera that reacted with the Bunyamwera virus L protein, detected by Western blotting or immunoprecipitation [5].

References