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The term viral protein refers to both the products of the genome of a virus and any host proteins incorporated into the viral particle. Viral proteins are grouped according to their functions, and groups of viral proteins include structural proteins , nonstructural proteins , regulatory proteins , and accessory proteins. [ 1 ]
Vpr is a Human immunodeficiency virus gene and protein product. [1] [2] Vpr stands for "Viral Protein R".Vpr, a 96 amino acid 14-kDa protein, plays an important role in regulating nuclear import of the HIV-1 pre-integration complex, and is required for virus replication and enhanced gene expression from provirus in dividing or non-dividing cells such as T cells or macrophages. [3]
HBeAg is a hepatitis B viral protein, produced by the HBcAg reading frame. It is an indicator of active viral replication ; this means the person infected with Hepatitis B can likely transmit the virus on to another person (i.e. the person is infectious).
HBcAg, also called core protein (Cp), is a 21 kDa protein of 183–185 amino acids, depending on the genotype, and is the result of the second start codon in the open reading frame. [6] Once a threshold of HBcAg proteins are translated in the cytoplasm, the viral capsid will spontaneously into a T=3 or T=4 icosahedral capsid . [ 7 ]
Env is a viral gene that encodes the protein forming the viral envelope. [1] The expression of the env gene enables retroviruses to target and attach to specific cell types, and to infiltrate the target cell membrane. [2] Analysis of the structure and sequence of several different env genes suggests that Env proteins are type 1 fusion machines. [3]
The p24 capsid protein (CA) is a 24 kDa protein fused to the C-terminus of MA in the unprocessed HIV Gag polyprotein. After viral maturation, CA forms the viral capsid. CA has two generally recognized domains, the C-terminal domain (CTD) and the N-terminal domain (NTD). The CA CTD and NTD have distinct roles during HIV budding and capsid structure.
Major capsid protein VP1 is a viral protein that is the main component of the polyomavirus capsid. VP1 monomers are generally around 350 amino acids long and are capable of self-assembly into an icosahedral structure consisting of 360 VP1 molecules organized into 72 pentamers .
Loss of membrane polarization can promote viral yields through a variety of mechanisms that operate throughout the viral life cycle. In enveloped viruses , viroporins are not highly concentrated in the viral envelope, but nevertheless their presence may promote viral entry into the cell; the influenza A virus provides a well-studied example.