Abstract
In mature HIV-1 particles, viral capsid (CA) proteins form the conical core structure that encapsidates two copies of the viral RNA genome. After fusion of the viral envelope and cellular membranes, the CA core enters into the cytoplasm of the target cells. CA proteins then interact with a variety of viral other protein as well as host factors, which may either support or inhibit replication of the virus. Recent studies have revealed that CA proteins are important not only for the uncoating step but also for the later nuclear import step. Identification of proteins that interact with CA to fulfill these functions is, therefore, important for understanding the unknown HIV-1 replication machinery. CA proteins can also be targets of the host immune response. Notably, some HLA-restricted cytotoxic T-lymphocyte (CTL) responses that recognize CA functional regions can greatly contribute to delay in AIDS progression. The multi-functionality of the CA protein may limit the flexible virus evolution and reduce the possibility of an escape mutant arising. The presence of many functional regions in CA protein may make it a potential target for effective therapies.
Highlights
The HIV-1 gag gene encodes the Gag protein, major structural component of virus particles (Vogt, 1997; Scarlata and Carter, 2003; Engelman and Cherepanov, 2012)
In this mini-review, we are summarizing the interaction of the CA and host cellular proteins such as cyclophilin A (CypA), Nuclear pore proteins (Nups), TRIM5alpha, and/or host immune response
CypA incorporates into HIV-1 particles via interaction with pr55Gag protein (Luban et al, 1993; Franke et al, 1994; Luban, 1996), binding at a site in the CA protein NTD, termed the CypA-binding loop (Figures 1B and 2)
Summary
The HIV-1 gag gene encodes the Gag protein, major structural component of virus particles (Vogt, 1997; Scarlata and Carter, 2003; Engelman and Cherepanov, 2012). Capsid (CA) is the largest component of Gag protein, and forms core structure of the mature HIV-1 particle. HIV-1 CAPSID PROTEINS CONSTITUTE THE VIRAL CORE STRUCTURE The HIV-1 Gag proteins are synthesized as Pr55Gag polyprotein in cytoplasm of the virus-producing cell, and are translocated to the plasma membrane. They are coassembled into virus particles, which bud and are released from the plasma membrane. In the mature virus particles, CA proteins form a conical core structure encapsidating two copies of the viral RNA genome associated by NC proteins. The identification of such host proteins is, likely to be essential for understanding the HIV-1 replication cycle
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