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. 1987 Oct;84(19):6924–6928. doi: 10.1073/pnas.84.19.6924

Humoral immune response to the entire human immunodeficiency virus envelope glycoprotein made in insect cells.

J R Rusche 1, D L Lynn 1, M Robert-Guroff 1, A J Langlois 1, H K Lyerly 1, H Carson 1, K Krohn 1, A Ranki 1, R C Gallo 1, D P Bolognesi 1, et al.
PMCID: PMC299197  PMID: 3477816

Abstract

The human immunodeficiency virus envelope gene was expressed in insect cells by using a Baculovirus expression vector. The protein has an apparent molecular mass of 160 kDa, appears on the surface of infected insect cells, and does not appear to be cleaved to glycoproteins gp120 and gp41. Goats immunized with the 160-kDa protein have high titers of antibody that neutralizes virus infection as measured by viral gene expression or cell cytolysis. In addition, immune sera can block fusion of human immunodeficiency virus-infected cells in culture. Both neutralization and fusion-blocking activities are bound to and eluted from immobilized gp120.

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