11th International AIDS Conference Vancouver, British Columbia — July 7-12, 1996

Int Conf AIDS 1996 Jul 7-12; 11:217 (abstract no. Th.A.385)
Bosch V, Henriksson P, Pfeiffer T, Wilk T; ATV, DKFZ, Heidelberg, Germany. Fax: 06221.424932. E-mail: V.Bosch@dkfz-heidelberg.de.

OBJECTIVE: To determine which domains are necessary and sufficient for the incorporation of glycoprotein into HIV-1 particles.

METHODS: Vectors encoding mutated and chimeric HIV-1 Env gene products were coexpressed with a vector encoding all the HIV-1 structural proteins except Env and resulting in the production and release of virus-like particles. Sedimented virus-like particles from the cotransfections were examined in Western blot analyses as to the presence of incorporated recombinant glycoproteins. In addition selected Env mutations were introduced into an infectious proviral construct and the potential infectivities of the recombinant viruses examined.

RESULTS: Env glycoproteins lacking almost the entire cytoplasmic C-terminus or with a heterologous membrane anchor were still incorporated into virus-like particles and recombinant virions were still infectious. Mutated noncleavable gp160 was not incorporated into virus-like particles nor was a non-cleavable derivative lacking almost the entire cytoplasmic C-terminus.

CONCLUSIONS: Neither the cytoplasmic C-terminus nor the homologous membrane anchor of HIV-1 Env are required for incorporation. This indicates that a distinguishing incorporation feature may be in the extracellular domain of HIV-1 Env and of further heterologous viral glycoproteins with short C-termini which, as has been shown by others, can be incorporated into HIV-1 particles. In the case of HIV-1 Env, proteolytic processing is required to generate the appropriate incorporation signal even when the C-terminus is lacking.

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ThA385

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