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Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases
BACKGROUND: The foamy virus Pol protein is translated independently from Gag using a separate mRNA. Thus, in contrast to orthoretroviruses no Gag-Pol precursor protein is synthesized. Only the integrase domain is cleaved off from Pol resulting in a mature reverse transcriptase harboring the protease...
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2010
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2835651/ https://www.ncbi.nlm.nih.gov/pubmed/20113504 http://dx.doi.org/10.1186/1742-4690-7-5 |
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author | Hartl, Maximilian J Mayr, Florian Rethwilm, Axel Wöhrl, Birgitta M |
author_facet | Hartl, Maximilian J Mayr, Florian Rethwilm, Axel Wöhrl, Birgitta M |
author_sort | Hartl, Maximilian J |
collection | PubMed |
description | BACKGROUND: The foamy virus Pol protein is translated independently from Gag using a separate mRNA. Thus, in contrast to orthoretroviruses no Gag-Pol precursor protein is synthesized. Only the integrase domain is cleaved off from Pol resulting in a mature reverse transcriptase harboring the protease domain at the N-terminus (PR-RT). Although the homology between the PR-RTs from simian foamy virus from macaques (SFVmac) and the prototype foamy virus (PFV), probably originating from chimpanzee, exceeds 90%, several differences in the biophysical and biochemical properties of the two enzymes have been reported (i.e. SFVmac develops resistance to the nucleoside inhibitor azidothymidine (AZT) whereas PFV remains AZT sensitive even if the resistance mutations from SFVmac PR-RT are introduced into the PFV PR-RT gene). Moreover, contradictory data on the monomer/dimer status of the foamy virus protease have been published. RESULTS: We set out to purify and directly compare the monomer/dimer status and the enzymatic behavior of the two wild type PR-RT enzymes from SFVmac and PFV in order to get a better understanding of the protein and enzyme functions. We determined kinetic parameters for the two enzymes, and we show that PFV PR-RT is also a monomeric protein. CONCLUSIONS: Our data show that the PR-RTs from SFV and PFV are monomeric proteins with similar biochemical and biophysical properties that are in some aspects comparable with MLV RT, but differ from those of HIV-1 RT. These differences might be due to the different conditions the viruses are confronted with in dividing and non-dividing cells. |
format | Text |
id | pubmed-2835651 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-28356512010-03-10 Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases Hartl, Maximilian J Mayr, Florian Rethwilm, Axel Wöhrl, Birgitta M Retrovirology Research BACKGROUND: The foamy virus Pol protein is translated independently from Gag using a separate mRNA. Thus, in contrast to orthoretroviruses no Gag-Pol precursor protein is synthesized. Only the integrase domain is cleaved off from Pol resulting in a mature reverse transcriptase harboring the protease domain at the N-terminus (PR-RT). Although the homology between the PR-RTs from simian foamy virus from macaques (SFVmac) and the prototype foamy virus (PFV), probably originating from chimpanzee, exceeds 90%, several differences in the biophysical and biochemical properties of the two enzymes have been reported (i.e. SFVmac develops resistance to the nucleoside inhibitor azidothymidine (AZT) whereas PFV remains AZT sensitive even if the resistance mutations from SFVmac PR-RT are introduced into the PFV PR-RT gene). Moreover, contradictory data on the monomer/dimer status of the foamy virus protease have been published. RESULTS: We set out to purify and directly compare the monomer/dimer status and the enzymatic behavior of the two wild type PR-RT enzymes from SFVmac and PFV in order to get a better understanding of the protein and enzyme functions. We determined kinetic parameters for the two enzymes, and we show that PFV PR-RT is also a monomeric protein. CONCLUSIONS: Our data show that the PR-RTs from SFV and PFV are monomeric proteins with similar biochemical and biophysical properties that are in some aspects comparable with MLV RT, but differ from those of HIV-1 RT. These differences might be due to the different conditions the viruses are confronted with in dividing and non-dividing cells. BioMed Central 2010-01-29 /pmc/articles/PMC2835651/ /pubmed/20113504 http://dx.doi.org/10.1186/1742-4690-7-5 Text en Copyright ©2010 Hartl et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Hartl, Maximilian J Mayr, Florian Rethwilm, Axel Wöhrl, Birgitta M Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
title | Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
title_full | Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
title_fullStr | Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
title_full_unstemmed | Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
title_short | Biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
title_sort | biophysical and enzymatic properties of the simian and prototype foamy virus reverse transcriptases |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2835651/ https://www.ncbi.nlm.nih.gov/pubmed/20113504 http://dx.doi.org/10.1186/1742-4690-7-5 |
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