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The circular genome of a representative polyomavirus, WU polyomavirus, with the late region at right indicating positions of the VP1, VP2, and VP3 genes. [4]All three capsid proteins are expressed from alternative start sites on a single transcript of the "late region" of the circular viral chromosome (so named because it is transcribed late in the process of viral infection).
FMDV structural proteins VP1, VP2, VP3, and VP4 form the biological protomer and icosahedral capsid. Picornaviruses are nonenveloped, with an icosahedral capsid. [4] The capsid is an arrangement of 60 protomers in a tightly packed icosahedral structure. Each protomer consists of four polypeptides known as VP (viral protein) 1, 2, 3 and 4. VP2 ...
The genetic material of a virus is stored within a viral protein structure called the capsid. The capsid is a "shield" that protects the viral nucleic acids from getting degraded by host enzymes or other types of pesticides or pestilences.
VP2 forms the core layer of the virion and binds the RNA genome. [39] VP3 is part of the inner core of the virion and is an enzyme called guanylyl transferase. This is a capping enzyme that catalyses the formation of the 5' cap in the post-transcriptional modification of mRNA. [40]
VP2 is the major capsid protein, and comprises approximately 95% of the total virus particle. VP1-proteins are incorporated into the capsid structure in a non- stoichiometrical relation (based on antibody -binding analysis and X-ray structural analysis the VP1-unique (VP1u) region is assumed to be exposed at the surface of the virus particle ...
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VP4 protein is involved in generating VP2 and VP3. [5] recombinant VP3 is more immunogenic than recombinant VP2. [6] Infectious pancreatic necrosis virus (IPNV), a birnavirus, is an important pathogen in fish farms. Analyses of viral proteins showed that VP2 is the major structural and immunogenic polypeptide of the virus.
Human rhinoviruses (HRVs) contain four structural proteins labeled VP1-VP4. Proteins VP1, VP2 and VP3 are eight stranded anti-parallel β-barrels. VP4 is an extended polypeptide chain on the viral capsid inner surface. [8] Pleconaril binds to a hydrophobic pocket in the VP1 protein.