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Specific infection of CD4+ target cells by recombinant rabies virus pseudotypes carrying the HIV-1 envelope spike protein
Pages 11366-11370

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From page 11366...
... The possibility of directing the cell tropism of RV by replacement of the RV G with proteins of defined receptor specificity should prove useful for future development of targetable gene delivery vectors. The host range of viruses is determined primarily by the interaction of viral envelope ,lycoproteins with specific proteins on the host cell surface that act as receptors.
From page 11367...
... To analyze expression of the recombinant glycoproteins on the cell surface, which represents a prerequisite for incorporation into RV particles, plasmids were transfected into BSR cells that had been infected with the recombinant vaccinia virus vTF7-3 providing T7 RNA polymerase (20~. Surface expression was compared by indirect immunofluorescence with human antiHIV IgG (18)
From page 11368...
... As for BSR cells, infection of HeLa cells was found to require the presence of the viral spike protein. To determine whether any of the mutant Env proteins could rescue the infectivity of SAD l\G, BSR cells were infected with both G-complemented SAD !
From page 11369...
... The data presented here demonstrate that the cytoplasmic tail of the RV G contains a signal sufficient and necessary to direct a chimeric HIV Env spike protein, Env-RVG, into the envelope of "rabies" virus particles in the absence of G or of parts of it. In contrast to RV, which is able to infect all culture cells analyzed so far, the tropism of the pseudotype particles is restricted and is obviously determined by the specificity of the incorporated spike protein and its interaction with the HIV-1 CD4 receptor complex.
From page 11370...
... Since the infectivity of viruses is largely governed by the features of their spike proteins and the interaction with receptors, the discrepancy in infectious titers may not directly reflect the efficiency by which the hybrid protein can substitute for RV G in formation of infectious virions. It is not known so far whether oligomerization has an influence on the putative interaction of the cytoplasmic tail with internal virus proteins.


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