Biophysical characterization and crystal structure of the Feline Immunodeficiency Virus p15 matrix protein.

ABSTRACT:

Background

Feline Immunodeficiency Virus (FIV) is a viral pathogen that infects domestic cats and wild felids. During the viral replication cycle, the FIV p15 matrix protein oligomerizes to form a closed matrix that underlies the lipidic envelope of the virion. Because of its crucial role in the early and late stages of viral morphogenesis, especially in viral assembly, FIV p15 is an interesting target in the development of potential new therapeutic strategies.

Results

Our biochemical study of FIV p15 revealed that it forms a stable dimer in solution under acidic conditions and at high concentration, unlike other retroviral matrix proteins. We determined the crystal structure of full-length FIV p15 to 2 Å resolution and observed a helical organization of the protein, typical

SUBMITTER: Serriere J 

PROVIDER: S-EPMC3706335 | biostudies-literature | 2013 Jun

REPOSITORIES: biostudies-literature