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Backbone chemical shift assignments and secondary structure analysis of the U1 protein from the Bas-Congo virus.

ABSTRACT: The Bas-Congo virus (BASV) is the first rhabdovirus associated with a human outbreak of acute hemorrhagic fever. The single-stranded, negative-sense RNA genome of BASV contains the five core genes present in all rhabdoviral genomes plus an additional three genes, annotated U1, U2, and U3, with weak (<21%) sequence similarity only to a handful of genes observed in a few other rhabdoviral genomes. The function of the rhabdoviral U proteins is unknown, but, they are hypothesized to play a role in viral infection or replication. To better understand this unique family of proteins, a construct containing residues 27-203 of the 216-residue U1 protein (BASV-U1*) was prepared. By collecting data in 0.5 M urea it was possible to eliminate transient association enough to enable the assignment of most of the observable ¹H^N, ¹Hα, ¹⁵N, ¹³Cα, ¹³Cβ, and ¹³C´ chemical shifts for BASV-U1* that will provide a foundation to study its solution properties. The analyses of these chemical shifts along with ¹⁵N-edited NOESY data enabled the identification of the elements of secondary structure present in BASV-U1*.

SUBMITTER: Buchko GW

PROVIDER: S-EPMC8457264 | biostudies-literature |

REPOSITORIES: biostudies-literature

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