Rotavirus VP6

The inner capsid protein, VP6, is a trimer representing 51% of the virion mass. According to the antigenic variation of VP6, RVs are classified into seven groups (A to G). Depending on the presence or absence of two different epitopes in the VP6 protein, group A RV strains are further divided into subgroups (Sb) I, II, I+II, and no I no II. Despite the different subgroups mentioned, VP6 is a strongly conserved protein among all group A RVs (>90% amino acid homology). It is highly immunogenic and constitutes the target antigen of most immunodiagnosis tests for group A RV detection

Rotavirus VP6

Intermediate capsid protein that self assembles to form an icosahedral capsid with a T=13 symmetry, which consists of 230 trimers of VP6, with channels at each of its five-fold vertices (PubMed:11285213).
This capsid constitutes the middle concentric layer of the viral mature particle (PubMed:11285213).
The innermost VP2 capsid and the intermediate VP6 capsid remain intact following cell entry to protect the dsRNA from degradation and to prevent unfavorable antiviral responses in the host cell during all the replication cycle of the virus. Nascent transcripts are transcribed within the structural confines of this double-layered particle (DLP) and are extruded through the channels at the five-fold axes (By similarity).
VP6 is required for the transcription activity of the DLP (PubMed:12097594).

Fusion of virus membrane with host plasma membrane

Virion
Component of the intermediate capsid (PubMed:11285213).
Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (Potential)

The N-terminus is blocked.
Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins seems to have a positive role on viral replication.