Pertussis toxin (PTX) has been used as a reagent to identify involvement of
the G protein-mediated signal transduction pathway, In this study, me foun
d that PTX enhanced HIV-1 replication in acute infection systems at a high
dose (1-10 mu g/ml) in vitro, PTX treatment enhanced the infectivity of HIV
-l-based pseudovirus enveloped with HIV-1 or amphotropic murine leukemia vi
rus (A-MuLV), but not with vesicular stomatitis virus (VSV), This high dose
of PTX treatment did not affect HIV-1 gene expression. These data suggeste
d that the effect was virus envelope dependent and that PTX acted on an ear
ly stage of viral infection. Treatment with B-oligomer, a nonenzymatic subu
nit of PTX, mimicked this enhancing effect of PTX, However, desialylation o
f viral and cellular surface glycoproteins, which are receptors for B-oligo
mer, did not affect the augmentation induced by PTX, These results indicate
that the enhancement of HIV-1 replication is mediated through an unknown b
iological function of B-oligomer.