HIV-2 protease as a chemotherapeutic target
dc.contributor.advisor | Tőzsér, József | |
dc.contributor.author | Mahdi, Mohamed | |
dc.contributor.department | Molekuláris sejt- és immunbiológia doktori iskola | hu |
dc.date.accessioned | 2016-08-18T08:21:35Z | |
dc.date.available | 2016-08-18T08:21:35Z | |
dc.date.created | 2016 | hu_HU |
dc.date.defended | 2016-09-05 | |
dc.description.abstract | In summary, we presented a comprehensive analysis of HIV-2 protease and its susceptibility to the currently marketed PIs. Such data are really scarce, and given the ever increasing incidence of HIV-2 infection, it is wise to characterize the viral responsiveness to combination therapies containing PIs. Having optimized the expression and stability of the viral protease, we can conclude from our comparative enzymatic and cell culture inhibition profiling that lopinavir, darunavir, indinavir sulfate and saquinavir are indeed highly potent HIV-2 protease inhibitors. Tipranavir and nelfinavir on the other hand, showed a significantly lower efficacy when compared to the others. While amprenavir consistently was proven to be a weak inhibitor, the variable results obtained for atazanavir sulfate; enzymatically and in cell culture, incline us to doubt its reliability when used in HIV-2 infected patients. I54M-L90M mutations reduced the susceptibility of the protease to most of the inhibitors to variable degrees, with the exception of tipranavir. Perhaps the use of tipranavir in patients with such identified mutations is advantageous after all. We are confident that the use of such a standardized system capable of carrying out comparative analysis will prove beneficial in tailoring the use of protease inhibitors in HIV-2 infected patients. | hu_HU |
dc.description.corrector | de | |
dc.format.extent | 94 | hu_HU |
dc.identifier.uri | http://hdl.handle.net/2437/229850 | |
dc.language.iso | en | hu_HU |
dc.subject | HIV | hu_HU |
dc.subject | HIV-2 | |
dc.subject | AIDS | |
dc.subject | antiretroviral therapy | |
dc.subject | cassette | |
dc.subject | enzymatic assays | |
dc.subject | inhibition profiling | |
dc.subject | protease | |
dc.subject | protease inhibitors | |
dc.subject | HIV-2 modular system | |
dc.subject | susceptibility assays | |
dc.subject.discipline | Elméleti orvostudományok | hu |
dc.subject.sciencefield | Orvostudományok | hu |
dc.title | HIV-2 protease as a chemotherapeutic target | hu_HU |
dc.title.translated | HIV-2 protease as a chemotherapeutic target | hu_HU |
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