This Recombinant Feline calicivirus capsid protein (ORF2) is a semi-custom product. There are 5 expression system options: Yeast, E. coli, In Vivo Biotinylation in E. coli, Baculovirus, and Mammalian cell. Your requirements will be given top priority in determining the protein tags. For proteins within 800 aa, risk-free custom service is guaranteed. It means you will not be charged if the protein cannot be delivered.
Feline calicivirus Capsid protein (ORF2), encoded by the open reading frame 2 (ORF2), is crucial for the virus's structure. This protein is a major structural protein of the virus and is essential for the production of infectious virions [1][2][3]. The capsid protein precursor is processed posttranslationally to release the mature capsid protein (VP1) and a small protein known as the leader of the capsid (LC) [3]. The feline calicivirus capsid protein is a polyprotein produced from a subgenomic-sized mRNA [2].
The capsid protein of feline calicivirus plays a critical role in the virus's life cycle. It is involved in receptor engagement, endocytosis, and the formation of a portal-like assembly following receptor engagement [4]. Additionally, the capsid protein is associated with cytopathic effects and is required for viral replication [3][5]. Studies have shown that the feline calicivirus capsid protein is part of the icosahedral capsid structure that encapsulates the viral RNA genome [6][7]. The capsid protein is also implicated in releasing the viral RNA genome by puncturing the endosome membrane of infected cells [8].
References:
[1] S. Sosnovtsev, G. Belliot, K. Chang, O. Onwudiwe, & K. Green, Feline calicivirus vp2 is essential for the production of infectious virions, Journal of Virology, vol. 79, no. 7, p. 4012-4024, 2005. https://doi.org/10.1128/jvi.79.7.4012-4024.2005
[2] S. Sosnovtsev, S. Sosnovtseva, & K. Green, Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase, Journal of Virology, vol. 72, no. 4, p. 3051-3059, 1998. https://doi.org/10.1128/jvi.72.4.3051-3059.1998
[3] E. Abente, S. Sosnovtsev, C. Sandoval-Jaime, G. Parra, K. Bok, & K. Green, The feline calicivirus leader of the capsid protein is associated with cytopathic effect, Journal of Virology, vol. 87, no. 6, p. 3003-3017, 2013. https://doi.org/10.1128/jvi.02480-12
[4] M. Conley, M. McElwee, L. Azmi, M. Gabrielsen, O. Byron, I. Goodfellowet al., Calicivirus vp2 forms a portal-like assembly following receptor engagement, Nature, vol. 565, no. 7739, p. 377-381, 2019. https://doi.org/10.1038/s41586-018-0852-1
[5] V. Shivanna, Y. Kim, & K. Chang, Endosomal acidification and cathepsin l activity is required for calicivirus replication, Virology, vol. 464-465, p. 287-295, 2014. https://doi.org/10.1016/j.virol.2014.07.025
[6] H. Aboubakr, S. Mor, L. Higgins, A. Armién, M. Youssef, P. Bruggemanet al., Cold argon-oxygen plasma species oxidize and disintegrate capsid protein of feline calicivirus, Plos One, vol. 13, no. 3, p. e0194618, 2018. https://doi.org/10.1371/journal.pone.0194618
[7] W. Burmeister, M. Buisson, L. Estrozi, G. Schoehn, O. Billet, Z. Hannaset al., Structure determination of feline calicivirus virus-like particles in the context of a pseudo-octahedral arrangement, Plos One, vol. 10, no. 3, p. e0119289, 2015. https://doi.org/10.1371/journal.pone.0119289
[8] W. Sun, Vp2 mediates the release of the feline calicivirus rna genome by puncturing the endosome membrane of infected cells, Journal of Virology, vol. 98, no. 5, 2024. https://doi.org/10.1128/jvi.00350-24
