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1.A.96 The Polyoma Virus Viroporin (PVVP) Family 

The agnoprotein viroporin (Suzuki et al. 2010) alters the structure of the nuclear envelope by interacting with host CBX5, disrupting CBX5 associations (Okada et al. 2001) and transporting Ca2+ (Hyser and Estes 2015). It is involved in the perinuclear-nuclear localization of the capsid protein VP1 during virion assembly and maturation. It also plays a role in the release of progeny virions from infected cells and in viral propagation by acting as a viral ionic channel in the host plasma membrane. It mediates influx of extracellular calcium ions in the host cell and may contribute to viral genome transcription and translation of viral late proteins (Suzuki et al. 2010). 

Virus-host protein interactions allow the host to regulate viroporin activity and suggest that viroporins may be regulated by specific interactions with host cell proteins (Suzuki et al. 2013).

References associated with 1.A.96 family:

Hyser, J.M. and M.K. Estes. (2015). Pathophysiological Consequences of Calcium-Conducting Viroporins. Annu Rev Virol 2: 473-496. 26958925
Okada, Y., S. Endo, H. Takahashi, H. Sawa, T. Umemura, and K. Nagashima. (2001). Distribution and function of JCV agnoprotein. J Neurovirol 7: 302-306. 11517407
Suzuki, T., Y. Orba, Y. Makino, Y. Okada, Y. Sunden, H. Hasegawa, W.W. Hall, and H. Sawa. (2013). Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3. Proc. Natl. Acad. Sci. USA 110: 18668-18673. 24167297
Suzuki, T., Y. Orba, Y. Okada, Y. Sunden, T. Kimura, S. Tanaka, K. Nagashima, W.W. Hall, and H. Sawa. (2010). The human polyoma JC virus agnoprotein acts as a viroporin. PLoS Pathog 6: e1000801. 20300659