Pertussis toxin enhances human immunodeficiency virus type 1 replication.
Pertussis toxin (PTX) has been used as a reagent to identify involvement of the G protein-mediated signal transduction pathway. In this study, we found that PTX enhanced HIV-1 replication in acute infection systems at a high dose (1-10 microg/ml) in vitro. PTX treatment enhanced the infectivity of HIV-1-based pseudovirus enveloped with HIV-1 or amphotropic murine leukemia virus (A-MuLV), but not with vesicular stomatitis virus (VSV). This high dose of PTX treatment did not affect HIV-1 gene expression. These data suggested that the effect was virus envelope dependent and that PTX acted on an early stage of viral infection. Treatment with B-oligomer, a nonenzymatic subunit of PTX, mimicked this enhancing effect of PTX. However, desialylation of viral and cellular surface glycoproteins, which are receptors for B-oligomer, did not affect the augmentation induced by PTX. These results indicate that the enhancement of HIV-1 replication is mediated through an unknown biological function of B-oligomer.
Momoi
Y
Y
Department of Microbiology, Tokyo Medical and Dental University, Japan.
Ichiyama
K
K
Chowdhury
I H
IH
Koyanagi
Y
Y
Yamamoto
N
N
D015704:CD4 Antigens / Q000378:metabolism; D002455:Cell Division / Q000187:drug effects; D002460:Cell Line; D005434:Flow Cytometry; D015497:HIV-1 / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D037342:Pertussis Toxin; D019718:Receptors, CXCR4 / Q000378:metabolism; D010566:Virulence Factors, Bordetella / Q000494:pharmacology*; D014779:Virus Replication / Q000187:drug effects*
D015704:CD4 Antigens; D019718:Receptors, CXCR4; D010566:Virulence Factors, Bordetella; D037342:Pertussis Toxin