CRYSTAL STRUCTURE OF STRUCTURAL AND FUNCTIONAL PROTEINS FROM VESICULAR STOMATITI

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Vesicular stomatitis virus (VSV) is a non-segmented negative-stranded RNA virus belonging to the rhabdovirus family. The 11,161 nucleotide genome of VSV contains five genes and is encapsidated by the viral nucleocapsid protein(N). Our group has developed a co-expression system in E. coli for production of soluble N protein that is functional as determined by its abilty to bind RNA and form complexes with the viral phosphoprotein(P). We have purified and subsequently crystallized an N protein oligomer(a 10-mer) in complex with a 90 nucleotide RNA. In addition, we have crystallized this N protein-RNA oligomer in complex with the N protein binding domain of the P protein(P4). In line with the project, other fragments of the P protein have also been crystallized. Preliminary datasets for these proteins and protein complexes have been collected. Model building for the N protein-RNA complex is underway. Currently, there are no high resolution structures for the N proteins of this viral family.