Poster abstracts
Poster number 23 submitted by Sarah Cooper
Structural implications of Gag-mediated assembly during bovine leukemia virus replication
Sarah E. Cooper (Berry College Chemistry Department), Dr. Dominic F. Qualley (Berry College Chemistry Department)
Abstract:
Like most retroviruses, including human immunodeficiency virus type 1 (HIV-1), bovine leukemia virus (BLV) utilizes the structural polyprotein Gag in its replication process. Gag is composed of three different domains: the matrix domain, the capsid domain, and the nucleocapsid domain. The function of these three domains is essential in the viral assembly process, but how they work is still poorly understood. Specifically, it is unknown which domains play an active role in facilitating assembly by packaging the genomic RNA of the virus. Through computational structure modeling and gel-shift annealing assays, the interaction of the Gag domains with viral nucleic acids in BLV was studied. Our results indicate that, unlike HIV-1 Gag, BLV Gag adopts a rigid conformation with little flexibility. Similar to HIV-1 Gag, however, the MA domain is important for membrane binding while the NC domain is responsible for RNA binding and packaging. By better understanding this interaction, the domains responsible for genome packaging can potentially be inhibited in order to disrupt viral assembly and prevent BLV from replicating. Because BLV is an agriculturally significant pathogen that infects domestic cattle, a potential treatment would have an important impact on agricultural production. Additionally, BLV has been proposed as an animal model for human T-cell leukemia virus type 1 (HTLV-1), so treatments for BLV could potentially be translated into human medical therapies.
Keywords: Bovine leukemia virus, Gag protein, genome packaging