During retrovirus maturation, cleavage of the precursor structural Gag polyprotein by the
viral protease induces architectural rearrangement of the virus particle from an immature into …

Structural virology reveals the architecture underlying infection. While notably electron
microscopy images have provided an atomic view on viruses which profoundly changed our …

The packaging and budding of Gag polyprotein and viral RNA is a critical step in the HIV-1
life cycle. High-resolution structures of the Gag polyprotein have revealed that the capsid …

HIV-1 protease (PR) cleavage of the Gag polyprotein triggers the assembly of mature,
infectious particles. Final cleavage of Gag occurs at the junction helix between the capsid …

Monitoring virus assembly at the nanoscale in host cells remains a major challenge. Human
immunodeficiency virus type 1 (HIV-1) components are addressed to the plasma membrane …

Maturation of HIV-1 particles encompasses a complex morphological transformation of Gag
via an orchestrated series of proteolytic cleavage events. A longstanding question concerns …

Techniques for atomic-resolution structural biology have evolved during the past several
decades. Breakthroughs in instrumentation, sample preparation, and data analysis that …

The capsid core of HIV-1 is a large macromolecular assembly that surrounds the viral
genome and is an essential component of the infectious virus. In addition to its multiple roles …

The assembly of an orthoretrovirus such as HIV-1 requires the coordinated functioning of
multiple biochemical activities of the viral Gag protein. These activities include membrane …

HIV-1 virions assemble as immature particles containing Gag polyproteins that are
processed by the viral protease into individual components, resulting in the formation of …