Abstract
HIV-1 viral protein U (Vpu) facilitates virus particle release. To determine whether Gag is sufficient for generation of a target for Vpu-mediated particle release, we expressed HIV-1 Gag protein in the absence of the other viral genes. The resulting particles were still Vpu responsive. Mutational analysis of Gag indicated that the matrix domain (MA) is required for Vpu responsiveness. However, additional mutations in other domains of Gag, which affect the formation of stable virus particles, also abrogate Vpu responsiveness on total Gag release. Coexpression of the wild-type gag gene and a gag mutant lacking the MA domain renders the MA- mutant Vpu responsive. This indicates that Gag molecules lacking MA are still incorporated into particles through association with wild-type Gag molecules and that the resulting composite particles are sufficient for Vpu-mediated exit.
| Original language | English |
|---|---|
| Pages (from-to) | 46-55 |
| Number of pages | 10 |
| Journal | Virology |
| Volume | 237 |
| Issue number | 1 |
| DOIs | |
| State | Published - 13 Oct 1997 |
| Externally published | Yes |
Bibliographical note
Funding Information:The authors thank Dr. M. Scott McBride for providing pCMV(/1)MSMBA and pD1469Xba, Diccon Fiore for maintaining cell lines and antibody preparations, and Dr. Hui-Ju Chen, Dr. Mark Hanley, and Michael Callahan for helpful discussions and support. This work was supported by a research grant (R01-AI36174) from the NIH.
Funding
The authors thank Dr. M. Scott McBride for providing pCMV(/1)MSMBA and pD1469Xba, Diccon Fiore for maintaining cell lines and antibody preparations, and Dr. Hui-Ju Chen, Dr. Mark Hanley, and Michael Callahan for helpful discussions and support. This work was supported by a research grant (R01-AI36174) from the NIH.
| Funders | Funder number |
|---|---|
| National Institutes of Health | |
| National Institute of Allergy and Infectious Diseases | R01AI036174 |
