Code | CSB-EP755262VAQ |
Abbreviation | Recombinant Varicella-zoster virus gH protein, partial |
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Size | $388 |
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The production of recombinant Varicella-zoster virus Envelope glycoprotein H (gH) in E. coli involves several steps. First, the gene encoding the partial HHV-3 gH protein (243-611aa) is cloned into an expression vector with an N-terminal 6xHis-tag gene and transformed into E. coli cells. The bacteria are grown under conditions that induce protein expression. After sufficient growth, the cells are lysed to release the recombinant gH protein, which undergoes affinity chromatography purification. Protein purity is assessed using SDS-PAGE, reaching up to 85%.
Varicella-zoster virus Envelope glycoprotein H (gH) is a crucial component of the viral structure. The gH protein plays a significant role in Varicella-zoster virus infection [1]. Additionally, gH has been identified as a factor that mediates clathrin-dependent and antibody-independent endocytosis, highlighting its importance in the viral entry process [2].
Furthermore, studies have shown that the glycoproteins gE, gH, and gB of the Varicella-zoster virus are incorporated into the virion envelope, with all three glycoproteins containing functional tyrosine-based endocytosis motifs in their cytoplasmic tails [3]. This incorporation into the virion envelope underscores the significance of gH in the viral life cycle and pathogenesis. The interaction between gH and gL glycoproteins of VZV has been analyzed, uncovering details about their processing and trafficking in infected cells [4].
References:
[1] Y. Akahori, K. Suzuki, T. Daikoku, M. Iwai, Y. Yoshida, Y. Asanoet al., Characterization of neutralizing epitopes of varicella-zoster virus glycoprotein h, Journal of Virology, vol. 83, no. 4, p. 2020-2024, 2009. https://doi.org/10.1128/jvi.02097-08
[2] T. Pasieka, L. Marešová, & C. Grose, A functional ynki motif in the short cytoplasmic tail of varicella-zoster virus glycoprotein gh mediates clathrin-dependent and antibody-independent endocytosis, Journal of Virology, vol. 77, no. 7, p. 4191-4204, 2003. https://doi.org/10.1128/jvi.77.7.4191-4204.2003
[3] L. Marešová, T. Pasieka, E. Homan, E. Gerday, & C. Grose, Incorporation of three endocytosed varicella-zoster virus glycoproteins, ge, gh, and gb, into the virion envelope, Journal of Virology, vol. 79, no. 2, p. 997-1007, 2005. https://doi.org/10.1128/jvi.79.2.997-1007.2005
[4] L. Marešová, L. Kutinová, V. Ludvíková, R. Zak, M. Mareš, & Š. Němečková, Characterization of interaction of gh and gl glycoproteins of varicella-zoster virus: their processing and trafficking, Journal of General Virology, vol. 81, no. 6, p. 1545-1552, 2000. https://doi.org/10.1099/0022-1317-81-6-1545
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