Expression and processing of the AIDS virus reverse transcriptase in Escherichia coli - PubMed (original) (raw)
Expression and processing of the AIDS virus reverse transcriptase in Escherichia coli
W G Farmerie et al. Science. 1987.
Abstract
The ability to express the genes of pathogenic human viruses, such as the acquired immune deficiency syndrome (AIDS) virus (also called human immunodeficiency virus) in bacterial cells affords the opportunity to study proteins that are ordinarily difficult or inconvenient to obtain in amounts sufficient for detailed analysis. A segment of the AIDS virus pol gene was expressed in Escherichia coli. Expression resulted in the appearance of reverse transcriptase activity in the bacterial cell extracts. The extracts contained two virus-related polypeptides that have the same apparent molecular weights as the two processed forms of virion-derived reverse transcriptase (p66 and p51). The formation of these two polypeptides depended on the coexpression of sequences located near the 5' end of the pol gene, a region that is thought to encode a viral protease. This bacterial system appears to generate mature forms of the AIDS virus reverse transcriptase by a proteolytic pathway equivalent to that which occurs during virus infection of human cells.
Similar articles
- AIDS virus reverse transcriptase defined by high level expression in Escherichia coli.
Larder B, Purifoy D, Powell K, Darby G. Larder B, et al. EMBO J. 1987 Oct;6(10):3133-7. doi: 10.1002/j.1460-2075.1987.tb02623.x. EMBO J. 1987. PMID: 2446866 Free PMC article. - Biosynthesis and analysis of a genetically engineered HIV-1 reverse transcriptase/endonuclease polyprotein in Escherichia coli.
Leuthardt A, Le Grice SF. Leuthardt A, et al. Gene. 1988 Aug 15;68(1):35-42. doi: 10.1016/0378-1119(88)90596-3. Gene. 1988. PMID: 2464529 - Expression of the human immunodeficiency virus in Escherichia coli: chemotherapy.
Hizi A, Hughes SH. Hizi A, et al. Important Adv Oncol. 1989:29-39. Important Adv Oncol. 1989. PMID: 2468601 Review. No abstract available. - Human Immunodeficiency Virus type 1 reverse transcriptase.
Hottiger M, Hübscher U. Hottiger M, et al. Biol Chem Hoppe Seyler. 1996 Feb;377(2):97-120. Biol Chem Hoppe Seyler. 1996. PMID: 8868066 Review.
Cited by
- Mutational analysis of human immunodeficiency virus type 1 protease suggests functional homology with aspartic proteinases.
Loeb DD, Hutchison CA 3rd, Edgell MH, Farmerie WG, Swanstrom R. Loeb DD, et al. J Virol. 1989 Jan;63(1):111-21. doi: 10.1128/JVI.63.1.111-121.1989. J Virol. 1989. PMID: 2642305 Free PMC article. - Human immunodeficiency virus-like particles produced by a vaccinia virus expression vector.
Karacostas V, Nagashima K, Gonda MA, Moss B. Karacostas V, et al. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8964-7. doi: 10.1073/pnas.86.22.8964. Proc Natl Acad Sci U S A. 1989. PMID: 2479031 Free PMC article. - Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS.
Ghosh AK, Osswald HL, Prato G. Ghosh AK, et al. J Med Chem. 2016 Jun 9;59(11):5172-208. doi: 10.1021/acs.jmedchem.5b01697. Epub 2016 Jan 22. J Med Chem. 2016. PMID: 26799988 Free PMC article. Review. - Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.
Seelmeier S, Schmidt H, Turk V, von der Helm K. Seelmeier S, et al. Proc Natl Acad Sci U S A. 1988 Sep;85(18):6612-6. doi: 10.1073/pnas.85.18.6612. Proc Natl Acad Sci U S A. 1988. PMID: 3045820 Free PMC article. - Purification and structural characterization of the putative gag-pol protease of human immunodeficiency virus.
Lillehoj EP, Salazar FH, Mervis RJ, Raum MG, Chan HW, Ahmad N, Venkatesan S. Lillehoj EP, et al. J Virol. 1988 Aug;62(8):3053-8. doi: 10.1128/JVI.62.8.3053-3058.1988. J Virol. 1988. PMID: 3292793 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical