Complete mutagenesis of the HIV-1 protease - PubMed (original) (raw)
. 1989 Aug 3;340(6232):397-400.
doi: 10.1038/340397a0.
Affiliations
- PMID: 2666861
- DOI: 10.1038/340397a0
Complete mutagenesis of the HIV-1 protease
D D Loeb et al. Nature. 1989.
Abstract
Retroviruses encode a protease which needs to be active for the production of infectious virions. A disabling mutation in the protease results in the production of non-infectious virus particles and examination of proteins from these mutant virions reveals unprocessed Gag and Gag-Pol precursor proteins, the substrates of the viral protease. Each amino acid of the HIV-1 protease was individually mutated using a simple mutagenesis procedure which is capable of introducing and identifying missense mutations in each residue of a protein. Phenotypic screening of these mutants in a heterologous assay system reveals three regions within the protease where multiple consecutive amino-acid residues are sensitive to mutation. These results show that random mutagenesis can be used to identify functionally important regions within a protein. Mutants with conditional phenotypes have also been identified within this collection.
Similar articles
- Characterization and autoprocessing of precursor and mature forms of human immunodeficiency virus type 1 (HIV 1) protease purified from Escherichia coli.
Strickler JE, Gorniak J, Dayton B, Meek T, Moore M, Magaard V, Malinowski J, Debouck C. Strickler JE, et al. Proteins. 1989;6(2):139-54. doi: 10.1002/prot.340060205. Proteins. 1989. PMID: 2695927 - Naturally occurring amino acid polymorphisms in human immunodeficiency virus type 1 (HIV-1) Gag p7(NC) and the C-cleavage site impact Gag-Pol processing by HIV-1 protease.
Goodenow MM, Bloom G, Rose SL, Pomeroy SM, O'Brien PO, Perez EE, Sleasman JW, Dunn BM. Goodenow MM, et al. Virology. 2002 Jan 5;292(1):137-49. doi: 10.1006/viro.2001.1184. Virology. 2002. PMID: 11878916 - Specificity of retroviral proteases: an analysis of viral and nonviral protein substrates.
Tomasselli AG, Heinrikson RL. Tomasselli AG, et al. Methods Enzymol. 1994;241:279-301. doi: 10.1016/0076-6879(94)41069-0. Methods Enzymol. 1994. PMID: 7854182 Review. No abstract available. - Expression systems for retroviral proteases.
Stebbins J, Debouck C. Stebbins J, et al. Methods Enzymol. 1994;241:3-16. doi: 10.1016/0076-6879(94)41055-0. Methods Enzymol. 1994. PMID: 7854184 Review. No abstract available.
Cited by
- Ancient Loss of Catalytic Selenocysteine Spurred Convergent Adaptation in a Mammalian Oxidoreductase.
Rees J, Sarangi G, Cheng Q, Floor M, Andrés AM, Oliva Miguel B, Villà-Freixa J, Arnér ESJ, Castellano S. Rees J, et al. Genome Biol Evol. 2024 Mar 2;16(3):evae041. doi: 10.1093/gbe/evae041. Genome Biol Evol. 2024. PMID: 38447079 Free PMC article. - OPUS-Mut: Studying the Effect of Protein Mutation through Side-Chain Modeling.
Xu G, Wang Q, Ma J. Xu G, et al. J Chem Theory Comput. 2023 Mar 14;19(5):1629-1640. doi: 10.1021/acs.jctc.2c00847. Epub 2023 Feb 22. J Chem Theory Comput. 2023. PMID: 36813264 Free PMC article. - HIV-1 is dependent on its immature lattice to recruit IP6 for mature capsid assembly.
Renner N, Kleinpeter A, Mallery DL, Albecka A, Rifat Faysal KM, Böcking T, Saiardi A, Freed EO, James LC. Renner N, et al. Nat Struct Mol Biol. 2023 Mar;30(3):370-382. doi: 10.1038/s41594-022-00887-4. Epub 2023 Jan 9. Nat Struct Mol Biol. 2023. PMID: 36624347 Free PMC article. - Effectively predicting HIV-1 protease cleavage sites by using an ensemble learning approach.
Hu L, Li Z, Tang Z, Zhao C, Zhou X, Hu P. Hu L, et al. BMC Bioinformatics. 2022 Oct 27;23(1):447. doi: 10.1186/s12859-022-04999-y. BMC Bioinformatics. 2022. PMID: 36303135 Free PMC article. - Genome interpretation using in silico predictors of variant impact.
Katsonis P, Wilhelm K, Williams A, Lichtarge O. Katsonis P, et al. Hum Genet. 2022 Oct;141(10):1549-1577. doi: 10.1007/s00439-022-02457-6. Epub 2022 Apr 30. Hum Genet. 2022. PMID: 35488922 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources