A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein gp140 and Escherichia coli Aspartate Transcarbamoylase
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https://doi.org/10.1128/JVI.78.9.4508-4516.2004Metadata
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Chen, B., Y. Cheng, L. Calder, S. C. Harrison, E. L. Reinherz, J. J. Skehel, and D. C. Wiley. 2004. “A Chimeric Protein of Simian Immunodeficiency Virus Envelope Glycoprotein Gp140 and Escherichia Coli Aspartate Transcarbamoylase.” Journal of Virology 78 (9): 4508–16. doi:10.1128/JVI.78.9.4508-4516.2004.Abstract
The envelope glycoproteins of the human immunodeficiency virus and the related simian immunodeficiency virus (SIV) mediate viral entry into host cells by fusing viral and target cell membranes. We have reported expression, purification, and characterization of gp140 (also called gp160e), the soluble, trimeric ectodomain of the SIV envelope glycoprotein, gp160 (B. Chen et al., J. Biol. Chem. 275:34946-34953, 2000). We have now expressed and purified chimeric proteins of SIV gp140 and its variants with the catalytic subunitTerms of Use
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