The NTD-CTD intersubunit interface plays a critical role in assembly and stabilization of the HIV-1 capsid.

ABSTRACT:

Background

Lentiviruses exhibit a cone-shaped capsid composed of subunits of the viral CA protein. The intrinsic stability of the capsid is critical for HIV-1 infection, since both stabilizing and destabilizing mutations compromise viral infectivity. Structural studies have identified three intersubunit interfaces in the HIV-1 capsid, two of which have been previously studied by mutational analysis. In this present study we analyzed the role of a third interface, that which is formed between the amino terminal domain (NTD) and carboxyl terminal domain (CTD) of adjacent subunits.

Results

We provided evidence for the presence of the NTD-CTD interface in HIV-1 particles by engineering intersubunit NTD-CTD disulfide crosslinks, resulting in accumulation of disulfide-linked oligo

SUBMITTER: Yufenyuy EL 

PROVIDER: S-EPMC3623829 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature