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001-es BibID:	BIBFORM133841
035-os BibID:	(scopus)105022657619 (wos)001621166300002
Első szerző:	Al-Muffti, Aya S.
Cím:	Modulation of transferrin receptor by HIV-2 / Al-Muffti Aya Shamal, Kiarie Irene Wanjiru, Tőzsér József, Mahdi Mohamed
Dátum:	2025
ISSN:	1743-422X
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Virology Journal. - 22 : 1 (2025), p. 1-10. -
További szerzők:	Kiarie, Irene Wanjiru Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM089444
035-os BibID:	(WOS)000595728400003 (Scopus)85096570971
Első szerző:	Mahdi, Mohamed (orvos, tudományos segédmunkatárs)
Cím:	Analysis of the efficacy of HIV protease inhibitors against SARS-CoV-2·s main protease / Mahdi Mohamed, Mótyán János András, Szojka Zsófia Ilona, Golda Mária, Miczi Márió, Tőzsér József
Dátum:	2020
ISSN:	1743-422X
Megjegyzések:	Background: The pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has resulted in millions of infections worldwide. While the search for an effective antiviral is still ongoing, experimental therapies based on repurposing of available antivirals is being attempted, of which HIV protease inhibitors (PIs) have gained considerable interest. Inhibition profiling of the PIs directly against the viral protease has never been attempted in vitro, and while few studies reported an efficacy of lopinavir and ritonavir in SARS-CoV-2 context, the mechanism of action of the drugs remains to be validated. Methods We carried out an in-depth analysis of the efficacy of HIV PIs against the main protease of SARS-CoV-2 (Mpro) in cell culture and in vitro enzymatic assays, using a methodology that enabled us to focus solely on any potential inhibitory effects of the inhibitors against the viral protease. For cell culture experiments a dark-to-bright GFP reporter substrate system was designed. Results Lopinavir, ritonavir, darunavir, saquinavir, and atazanavir were able to inhibit the viral protease in cell culture, albeit in concentrations much higher than their achievable plasma levels, given their current drug formulations. While inhibition by lopinavir was attributed to its cytotoxicity, ritonavir was the most effective of the panel, with IC50 of 13.7 ?M. None of the inhibitors showed significant inhibition of SARS-CoV-2 Mpro in our in vitro enzymatic assays up to 100 ?M concentration. Conclusion Targeting of SARS-CoV-2 Mpro by some of the HIV PIs might be of limited clinical potential, given the high concentration of the drugs required to achieve significant inhibition. Therefore, given their weak inhibition of the viral protease, any potential beneficial effect of the PIs in COVID-19 context might perhaps be attributed to acting on other molecular target(s), rather than SARS-CoV-2 Mpro.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk SARS-CoV-2 Inhibition profling In vitro assay HIV protease inhibitors Protease
Megjelenés:	Virology Journal. - 17 : 1 (2020), p. 1-8. -
További szerzők:	Mótyán János András (1981-) (biokémikus, molekuláris biológus) Szojka Zsófia (1991-) (molekuláris biológus) Golda Mária (1986-) (molekuláris biológus) Miczi Márió Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	NKFIH-1150?6/2019 Egyéb NKFI 125238 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM073421
035-os BibID:	(WoS)000437375800031 (Scopus)85049171612
Első szerző:	Mahdi, Mohamed (orvos, tudományos segédmunkatárs)
Cím:	Inhibitory effects of HIV-2 Vpx on replication of HIV-1 / Mohamed Mahdi, Zsófia Szojka, János András Mótyán, József Tőzsér
Dátum:	2018
ISSN:	0022-538X
Megjegyzések:	The human immunodeficiency viruses type 1 and 2 share a striking genomic resemblance, however, variability in the genetic sequence accounts for the presence of unique accessory genes; such as viral protein x (vpx) in HIV-2. Dual infection with both viruses has long been described in the literature, yet the molecular mechanism of how dually infected patients tend to do better than those who are mono-infected with HIV-1 has not yet been explored. We hypothesized that in addition to extracellular mechanisms, an HIV-2 accessory gene is the culprit, and interference at viral accessory/regulatory protein level is perhaps responsible for the attenuated pathogenicity of HIV-1 observed in dually infected patients. Following simulation of dual infection in cell culture experiments, we found that pre-transduction of cells with HIV-2 significantly protects against HIV-1 transduction. Importantly, we have found that this dampening of HIV-1's infectivity was a result of inter-viral interference carried out by the viral protein X of HIV-2, resulting in a severe hindrance to HIV-1's replication dynamics, influencing both its early- and late-phase of the viral life-cycle. Our findings shed light on potential intracellular interactions between the two viruses, and broaden our understanding of the observed clinical spectrum in dually infected patients, highlighting HIV-2 Vpx as a potential candidate worth exploring in the fight against HIV-1.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	Journal of Virology. - 92 : 14 (2018), p. 1-46. -
További szerzők:	Szojka Zsófia (1991-) (molekuláris biológus) Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	125238 NKFI
Internet cím:	DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM136091
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	Molecular mechanisms of protease precursor autoprocessing of RNA viruses : a comprehensive review / Mótyán János András, Golda Mária, Mahdi Mohamed, Nashed Nashaat T., Louis John M., Tőzsér József
Dátum:	2026
ISSN:	1743-422X
Megjegyzések:	Many viruses express their proteins in the form of large polyproteins comprising structural and non-structural (e.g. enzymatic) units that are released from the precursor through ordered proteolysis. Proteolytic processing of polyproteins is an indispensable regulatory step for virus maturation and replication that is carried out by the virus-encoded and/or cellular proteases. The activity of a viral protease that is expressed as a part of a polyprotein is controlled in part by the self-cleavage (autoprocessing) from the precursor. The mechanism of protease precursor processing has been established at the molecular level for various RNA virus proteases, including human immunodeficiency virus (HIV) and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Both viral protease precursors are processed via intra- (in cis) and intermolecular (in trans) cleavages at the N- and C-termini, respectively, yielding the mature enzyme. The remarkably similar activation mechanisms of HIV and SARS-CoV-2 PRs suggest that other viral proteases are activated similarly. In this review, we provide a detailed overview on the protease precursor autoprocessing mechanism of HIV-1 and SARS-CoV-2 proteases and compare those to the activation mechanism of non-viral proteases from their zymogens. Also, we review the activation mechanism of other ss(+)RNA viruses that utilize the polyprotein pathway for their replication. Based on such comparison, it appears that the protease activation mechanisms of most enveloped ss(+)RNA viruses from their precursors share many common features, although they do not correlate directly with the evolutionary relationships, the presence or absence of viral envelope or the catalytic mechanism of the viral protease.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk SARS-CoV-2 HIV-1 HIV virus Polyprotein Self-cleavage Autoprocessing Protease precursor Protease RNA virus Proteolysis
Megjelenés:	Virology Journal. - [Epub ahead of print] (2026). -
További szerzők:	Golda Mária (1986-) (molekuláris biológus) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Nashed, Nashaat T. Louis, John M. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:	BO/00110/23/5 MTA ADVANCED_150532 OTKA TKP2021-EGA-20 Egyéb
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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