Structural and Mechanistic Studies of the Rare Myristoylation Signal of the Feline Immunodeficiency Virus.

ABSTRACT: All retroviruses encode a Gag polyprotein containing an N-terminal matrix domain (MA) that anchors Gag to the plasma membrane and recruits envelope glycoproteins to virus assembly sites. Membrane binding by the Gag protein of HIV-1 and most other lentiviruses is dependent on N-terminal myristoylation of MA by host N-myristoyltransferase enzymes (NMTs), which recognize a six-residue "myristoylation signal" with consensus sequence: M₁GXXX[ST]. For unknown reasons, the feline immunodeficiency virus (FIV), which infects both domestic and wild cats, encodes a non-consensus myristoylation sequence not utilized by its host or by other mammals (most commonly: M₁GNGQG). To explore the evolutionary basis for this sequence, we compared the structure, dynamics, and myristoylation

SUBMITTER: Brown JB 

PROVIDER: S-EPMC7316625 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature