Human immunodeficiency virus type 1 is a complex retrovirus encoding 15 distinct proteins.
Substantial progress has been made toward understanding the function of each protein, and …

The Gag proteins of HIV-1, like those of other retroviruses, are necessary and sufficient for
the assembly of virus-like particles. The roles played by HIV-1 Gag proteins during the life …

Like all retroviruses, the human immunodeficiency virus selectively packages two copies of
its unspliced RNA genome, both of which are utilized for strand-transfer-mediated …

One of the core standards of biochemistry is that the function of a protein relies on its 3D
structure. This idea posits that all the information required for a protein to perform its …

A single retroviral protein, Gag, is sufficient for virus particle assembly. While Gag is capable
of specifically packaging the genomic RNA into the particle, this RNA species is …

Retrovirus particles each contain two copies of the viral genome in the form of a
noncovalently linked RNA dimer. Earlier studies have mapped a cis-acting region near the …

The prokaryotic translation elongation factors were identified as essential cofactors for RNA-
dependent RNA polymerase activity of the bacteriophage Qβ more than 40 years ago. A …

Intrinsically disordered proteins (IDPs) possess the property of inherent flexibility and can be
distinguished from other proteins in terms of lack of any fixed structure. Such dynamic …

Retroviral Gag polyproteins drive virion assembly by polymerizing to form a spherical shell
that lines the inner membrane of nascent virions. Deletion of the nucleocapsid (NC) domain …

Publisher Summary This chapter describes the assembly, release, and maturation of human
immunodeficiency virus type 1 (HIV-1). The HIV‐1 replication cycle has the potential to …