1.J.1 The Archaeal Virus-Associated Pyramid (A-VAP) Family Some viruses of Archaea use an unusual egress mechanism that involves the formation of virus-associated pyramids (VAPs) on the host cell surface. At the end of the infection cycle, these structures open outward and create apertures through which mature virions escape from the cell. Quax et al. (2011) described the structure and composition of VAPs formed by the Sulfolobus islandicus rod-shaped virus 2 (SIRV2) in cells of its hyperthermophilic archaeal host. They found that the VAPs are stable and autonomous assemblies that can be isolated from membranes of infected cells and purified without affecting their structure. The purified VAPs are heterogeneous in size, reflecting the dynamics of VAP development in a population of infected cells; however, they have a uniform geometry, consisting of seven isosceles triangular faces forming a baseless pyramid. Biochemical and immunoelectron microscopy analyses revealed that the 10-kDa P98 protein encoded by the SIRV2 virus is the sole component of the VAPs. The VAPs were produced in Sulfolobus acidocaldarius and Escherichia coli by heterologous expression of the SIRV2-P98 gene. The results confirm that P98 is the only constituent of the VAPs and demonstrate that no other viral protein is involved in the assembly of pyramids. P98 was able to produce stable structures under conditions ranging from moderate to extremely high temperatures (80 °C) and from neutral to extremely acidic pH (pH 2), demonstrating another remarkable property of this exceptional viral protein. A-VAPs belong to the PHA01757 superfamily of CDD. They are formed in archaeal viruses, SIRV1, SIRV2, Sulfolobus turreted icosahedral virus (STIV) and Stygiolobus rod-shaped virus (SRSV). The protein is also homologous to an internal segment/residues 47-144) of the phage tail length tape measure protein of Candidatus Nitrospira defluvii (length, 871aas; D8P844). The reaction catalyzed by the SIRV2 P98 pyramids is: virus particle (cytoplasm) ^{_P98 pyrimidal structure} → virus particle (external medium)
References:
Quax, T.E., S. Lucas, J. Reimann, G. Pehau-Arnaudet, M.C. Prevost, P. Forterre, S.V. Albers, and D. Prangishvili. (2011). Simple and elegant design of a virion egress structure in Archaea. Proc. Natl. Acad. Sci. USA 108: 3354-3359.
Snyder, J.C., S.K. Brumfield, N. Peng, Q. She, and M.J. Young. (2011). Sulfolobus turreted icosahedral virus c92 protein responsible for the formation of pyramid-like cellular lysis structures. J. Virol. 85: 6287-6292.
Examples:
TC#	Name	Organismal Type	Example
1.J.1.1.1	*P98 virion egress pyrimidal structure forming protein of 98 aas and one N-terminal TMS (Quax et al., 2011).*	Archaeal virus	*P98 of Sulfolobus islandicus* rod-shaped virus 2 (Q8V9M0)**

1.J.1.1.2	Sulfolobus turreted icosahedral virus (STIV) c92 pyrimidal protein of 92 aas and one N-terminal TMS (Snyder et al. 2011). This protein alone is responsible for the formation of the pyramidal lysis structure in the cell membrane and is essential for virus replication.	Archaeal virus	*c92 protein of Sulfolobus sulfataricus* turreted icosahedral virus (Q6Q0L7)**

1.J.1.1.3	SRSV P92 pyrimidal protein of 92 aas and 1 N-terminal TMS.	Archaeal virus	*P92 of Stygiolobus* rod-shaped virus (B6EFE0)**