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1.

001-es BibID:BIBFORM088520
035-os BibID:(scopus)85092599352 (wos)000583012300001
Első szerző:Bozóki Beáta (molekuláris biológus)
Cím:Specificity Studies of the Venezuelan Equine Encephalitis Virus Non-Structural Protein 2 Protease Using Recombinant Fluorescent Substrates / Bozóki Beáta, Mótyán János András, Hoffka Gyula, Waugh David S., Tőzsér József
Dátum:2020
ISSN:1661-6596 1422-0067
Megjegyzések:The non-structural protein 2 (nsP2) of alphavirus Venezuelan equine encephalitis virus (VEEV) is a cysteine protease that is responsible for processing of the viral non-structural polyprotein and is an important drug target owing to the clinical relevance of VEEV. In this study we designed two recombinant VEEV nsP2 constructs to study the effects of an N-terminal extension on the protease activity and to investigate the specificity of the elongated enzyme in vitro. The N-terminal extension was found to have no substantial effect on the protease activity. The amino acid preferences of the VEEV nsP2 protease were investigated on substrates representing wild-type and P5, P4, P2, P1, P1·, and P2· variants of Semliki forest virus nsP1/nsP2 cleavage site, using a His6-MBP-mEYFP recombinant substrate-based protease assay which has been adapted for a 96-well plate-based format. The structural basis of enzyme specificity was also investigated in silico by analyzing a modeled structure of VEEV nsP2 complexed with oligopeptide substrate. To our knowledge, in vitro screening of P1· amino acid preferences of VEEV nsP2 protease remains undetermined to date, thus, our results may provide valuable information for studies and inhibitor design of different alphaviruses or other Group IV viruses.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
VEEV
Venezuelan equine encephalitis virus
nsp2
protease
alphavirus
alphaviral protease
non-structural protein
group IV virus
specificity
Megjelenés:International Journal Of Molecular Sciences. - 21 : 20 (2020), p. 1-26. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Hoffka Gyula (1992-) (vegyész) Waugh, David S. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:NKFI-125238
Egyéb
GINOP-2.3.2-15-2016-00044
GINOP
TÁMOP 4.2.4B/2-11/1-2012-0001
Egyéb
NKFIH-1150-6/2019
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM076746
Első szerző:Bozóki Beáta (molekuláris biológus)
Cím:Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation / Bozóki Beáta, Mótyán János András, Miczi Márió, Gazda Lívia Diána, Tőzsér József
Dátum:2019
ISSN:1940-087X
Megjegyzések:Proteases are intensively studied enzymes due to their essential roles in several biological pathways of living organisms and in pathogenesis; therefore, they are important drug targets. We have developed a magnetic-agarose-bead-based assay platform for the investigation of proteolytic activity, which is based on the use of recombinant fusion protein substrates. In order to demonstrate the use of this assay system, a protocol is presented on the example of human immunodeficiency virus type 1 (HIV-1) protease. The introduced assay platform can be utilized efficiently in the biochemical characterization of proteases, including enzyme activity measurements in mutagenesis, kinetic, inhibition, or specificity studies, and it may be suitable for high-throughput substrate screening or may be adapted to other proteolytic enzymes. In this assay system, the applied substrates contain N-terminal hexahistidine (His6) and maltose-binding protein (MBP) tags, cleavage sites for tobacco etch virus (TEV) and HIV-1 proteases, and a C-terminal fluorescent protein. The substrates can be efficiently produced in Escherichia coli cells and easily purified using nickel (Ni)-chelate-coated beads. During the assay, the proteolytic cleavage of bead-attached substrates leads to the release of fluorescent cleavage fragments, which can be measured by fluorimetry. Additionally, cleavage reactions can be analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). A protocol for the in-gel renaturation of assay components is also described, as partial renaturation of fluorescent proteins enables their detection based on molecular weight and fluorescence.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
recombinant fusion protein substrate
protease assay
Ni-NTA magnetic agarose beads
fluorescent protein
in-gel renaturation
human immunodeficiency virus type 1 protease
Megjelenés:Journal of Visualized Experiments. - 143 (2019), p. 1-15. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Miczi Márió Gazda Lívia Diána (1989-) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

3.

001-es BibID:BIBFORM072540
Első szerző:Bozóki Beáta (molekuláris biológus)
Cím:A recombinant fusion protein-based, fluorescent protease assay for high throughput-compatible substrate screening / Beáta Bozóki, Lívia Gazda, Ferenc Tóth, Márió Miczi, János András Mótyán, József Tőzsér
Dátum:2018
ISSN:0003-2697
Megjegyzések:In connection with the intensive investigation of proteases, several methods have been developed for analysis of the substrate specificity. Due to the great number of proteases and the expected target molecules to be analyzed, time- and cost-efficient high-throughput screening (HTS) methods are preferred. Here we describe the development and application of a separation-based HTS-compatible fluorescent protease assay, which is based on the use of recombinant fusion proteins as substrates of proteases. The protein substrates used in this assay consists of N-terminal (hexahistidine and maltose binding protein) fusion tags, cleavage sequences of the tobacco etch virus (TEV) and HIV-1 proteases, and a C-terminal fluorescent protein (mApple or mTurquoise2). The assay is based on the fluorimetric detection of the fluorescent proteins, which are released from the magnetic bead-attached substrates by the proteolytic cleavage. The protease assay has been applied for activity measurements of TEV and HIV-1 proteases to test the suitability of the system for enzyme kinetic measurements, inhibition studies, and determination of pH optimum. We also found that denatured fluorescent proteins can be renatured after SDS-PAGE of denaturing conditions, but showed differences in their renaturation abilities. After in-gel renaturation both substrates and cleavage products can be identified by in-gel UV detection.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Analytical Biochemistry. - 540-541 (2018), p. 52-63. -
További szerzők:Gazda Lívia Diána (1989-) Tóth Ferenc (1980-) (molekuláris biológus) Miczi Márió Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

4.

001-es BibID:BIBFORM082814
035-os BibID:(WOS)000534341100013 (Scopus)85077691494
Első szerző:Gazda Lívia Diána
Cím:Biochemical characterization of Ty1 retrotransposon protease / Lívia Diána Gazda, Krisztina Joóné Matúz, Tibor Nagy, János András Mótyán, József Tőzsér
Dátum:2020
ISSN:1932-6203
Megjegyzések:Ty1 is one of the many transposons in the budding yeast Saccharomyces cerevisiae. The life-cycle of Ty1 shows numerous similarities with that of retroviruses, e.g. the initially synthesized polyprotein precursor undergoes proteolytic processing by the protease. The retroviral proteases have become important targets of current antiretroviral therapies due to the critical role of the limited proteolysis of Gag-Pol polyprotein in the replication cycle and they therefore belong to the most well-studied enzymes. Comparative analyses of retroviral and retroviral-like proteases can help to explore the key similarities and differences which may help understanding how resistance is developed against protease inhibitors, but the available information about the structural and biochemical characteristics of retroviral-like, and especially retrotransposon, proteases is limited. To investigate the main characteristics of Ty1 retrotransposon protease of Saccharomyces cerevisiae, untagged and His6-tagged forms of Ty1 protease were expressed in E. coli. After purification of the recombinant proteins, activity measurements were performed using synthetic oligopeptide and fluorescent recombinant protein substrates, which represented the wild-type and the modified forms of naturally occurring cleavage sites of the protease. We investigated the dependence of enzyme activity on different reaction conditions (pH, temperature, ionic strength, and urea concentration), and determined enzyme kinetic parameters for the studied substrates. Inhibitory potentials of 10 different protease inhibitors were also tested. Ty1 protease was not inhibited by the inhibitors which have been designed against human immunodeficiency virus type 1 protease and are approved as antiretroviral therapeutics. A quaternary structure of homodimeric Ty1 protease was proposed based on homology modeling, and this structure was used to support interpretation of experimental results and to correlate some structural and biochemical characteristics with that of other retroviral proteases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
retrotransposon
Ty1
protease
retrovirus
homology modeling
ty1 protease
retroviral protease
retrotransposon protease
yeast
biochemical characterization
Megjelenés:Plos One. - 15 : 1 (2020), p. 1-24. -
További szerzők:Matúz Krisztina (1980-) (vegyész, biokémikus) Nagy Tibor (1988-) (vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
GINOP-2.3.3-15-2016-00021
GINOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

5.

001-es BibID:BIBFORM120789
035-os BibID:(Scopus)85191248548 (WoS)001208395200001
Első szerző:Golda Mária (molekuláris biológus)
Cím:P1' specificity of the S219V/R203G mutant tobacco etch virus protease / Mária Golda, Gyula Hoffka, Scott Cherry, Joseph E. Tropea, George T. Lountos, David S. Waugh, Alexander Wlodawer, József Tőzsér, János András Mótyán
Dátum:2024
ISSN:0887-3585
Megjegyzések:Proteases that recognize linear amino acid sequences with high specificity became indispensable tools of recombinant protein technology for the removal of various fusion tags. Due to its stringent sequence specificity, the catalytic domain of the nuclear inclusion cysteine protease of tobacco etch virus (TEV PR) is also a widely applied reagent for enzymatic removal of fusion tags. For this reason, efforts have been made to improve its stability and modify its specificity. For example, P1' autoproteolytic cleavage-resistant mutant (S219V) TEV PR was found not only to be nearly impervious to self-inactivation, but also exhibited greater stability and catalytic efficiency than the wild-type enzyme. An R203G substitution has been reported to further relax the P1' specificity of the enzyme, however, these results were obtained from crude intracellular assays. Until now, there has been no rigorous comparison of the P1' specificity of the S219V and S219V/R203G mutants in vitro, under carefully controlled conditions. Here, we compare the P1' amino acid preferences of these single and double TEV PR mutants. The in vitro analysis was performed by using recombinant protein substrates representing 20 P1' variants of the consensus TENLYFQ*SGT cleavage site, and synthetic oligopeptide substrates were also applied to study a limited set of the most preferred variants. In addition, the enzyme-substrate interactions were analyzed in silico. The results indicate highly similar P1' preferences for both enzymes, many side-chains can be accommodated by the S1' binding sites, but the kinetic assays revealed lower catalytic efficiency for the S219V/R203G than for the S219V mutant.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
tobacco etch virus
protein structure
molecular dynamics
fusion tag removal
enzymology
TEV protease
protease
Proteolysis
Megjelenés:Proteins-Structure Function And Bioinformatics. - 92 : 9 (2024), p. 1085-1096. -
További szerzők:Hoffka Gyula (1992-) (vegyész) Cherry, Scott Tropea, Joseph E. Lountos, George T. Waugh, David S. Wlodawer, Alexander Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:TKP2021-EGA-20
Egyéb
ÚNKP-23-5-DE-486
Egyéb
BO/00110/23/5
MTA
75N91019D00024
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
Borító:

6.

001-es BibID:BIBFORM086717
Első szerző:Golda Mária (molekuláris biológus)
Cím:Study of the Retrotransposon-Derived Human PEG10 Protease / Mária Golda, János András Mótyán, Mohamed Mahdi, József Tőzsér
Dátum:2020
Megjegyzések:Paternally expressed gene 10 (PEG10) is a human retrotransposon-derived imprinted gene. Previous works have demonstrated that a mutation in the coding sequence of this gene is lethal with regard to embryological age due to defects of placental development. In addition, PEG10 is implicated in several malignancies, such as pancreatic cancer and hepatocellular carcinoma. The PEG10 gene encodes two protein isoforms, which are translated by a typical retroviral frameshift mechanism. The Gag-like protein (RF1PEG10) is encoded by reading frame 1, whilst reading frames 1 and 2 accounts for the Gag-Pol-like polyprotein (RF1/RF2PEG10). The protease (PR) domain of RF2PEG10 contains an -Asp-Ser-Gly- sequence, which refers to the conservative -Asp-Ser/Thr-Gly- active-site motif of retroviral aspartic proteases. The function of the aspartic protease domain of RF2PEG10 remains unclear. In order to further investigate the function of the PEG10 protease (PRPEG10), a frameshift mutant was generated (fsRF1/RF2PEG10) for comparison with the RF1/RF2PEG10 form. To study the effects of PRPEG10 on cellular proliferation and viability, mammalian HEK293T and HaCaT cells were transfected with plasmids encoding for either the frameshift mutant (fsRF1/RF2PEG10) or a PR active-site (D370A) mutant fsRF1/RF2PEG10. Based on our findings, an fsRF1/RF2PEG10 overexpression resulted in an increased cellular proliferation, compared to the mutant form. Interestingly, transfection with fsRF1/RF2PEG10 had a detrimental effect on cell viability. We hypothesize that PRPEG10 may play a cardinal role in the function of this retroviral remnant, possibly implicated in cellular proliferation and the inhibition of apoptosis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
folyóiratcikk
PEG10
paternally expressed gene 10
cell viability
cell proliferation
cis protease activity
ubiquitination
homology modeling
retroviral-like protease
retrotransposon
protease
Megjelenés:Proceedings. - 50 : 1 (2020), p. 110. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
K-101591
OTKA
NKFIH-1150-6/2019
Egyéb
NKFI-125238
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

7.

001-es BibID:BIBFORM086709
035-os BibID:(WoS)000557707400001 (Scopus)85087574382
Első szerző:Golda Mária (molekuláris biológus)
Cím:Biochemical characterization of human retroviral-like aspartic protease 1 (ASPRV1) / Mária Golda, János András Mótyán, Katalin Nagy, Krisztina Matúz, Tibor Nagy, József Tőzsér
Dátum:2020
ISSN:2218-273X
Megjegyzések:The human retroviral-like aspartic protease 1 (ASPRV1) is a mammalian retroviral-like enzyme that catalyzes a critical proteolytic step during epidermal differentiation; therefore, it is also referred as skin-specific aspartic protease (SASPase). Neutrophil granulocytes were also found recently to express ASPRV1 that is involved in the progression of acute chronic in?ammation in the central nervous system, especially in autoimmune encephalomyelitis. Thus, investigation of ASPRV1 is important due to its therapeutic or diagnostic potential. We investigated the structural characteristics of ASPRV1 by homology modeling; analysis of the proposed structure was used for interpretation of in vitro specificity studies. For in vitro characterization, activities of SASP28 and SASP14 enzyme forms were measured using synthetic oligopeptide substrates. We demonstrated that self-processing of SASP28 precursor causes autoactivation of the protease. Highest activity was measured for GST-SASP14 at neutral pH and at high ionic strength, and we proved that pepstatin A and acetyl-pepstatin can also inhibit the protease. In agreement with the structural characteristics, the relatively lower urea dissociation constant implied lower dimer stability of SASP14 compared to that of HIV-1 protease. The obtained structural and biochemical characteristics help better understanding of ASPRV1 function in skin and central nervous system
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
ASPRV1
SASPase
protease
retroviral-like protease
retroviral-like aspartic protease 1
skin-specific aspartic protease
homology modeling
protease inhibitor
Megjelenés:Biomolecules. - 10 : 7 (2020), p. 1-25. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Nagy Katalin Matúz Krisztina (1980-) (vegyész, biokémikus) Nagy Tibor (1988-) (vegyész) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
TÁMOP 4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.D-15/1/KONV-2015-0016
TÁMOP
GINOP-2.3.3-15-2016-00021
GINOP
NKFIH-1150-6/2019
Egyéb
K-101591
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

8.

001-es BibID:BIBFORM084537
035-os BibID:(scopus)85083042118 (wos)000535574200166
Első szerző:Golda Mária (molekuláris biológus)
Cím:Functional Study of the Retrotransposon-Derived Human PEG10 Protease / Mária Golda, János András Mótyán, Mohamed Mahdi, József Tőzsér
Dátum:2020
ISSN:1661-6596 1422-0067
Megjegyzések:Paternally expressed gene 10 (PEG10) is a human retrotransposon-derived imprinted gene. The mRNA of PEG10 encodes two protein isoforms: the Gag-like protein (RF1PEG10) is coded by reading frame 1, while the Gag-Pol-like polyprotein (RF1/RF2PEG10) is coded by reading frames 1 and 2. The proteins are translated by a typical retroviral frameshift mechanism. The protease (PR) domain of RF2PEG10 contains an -Asp-Ser-Gly- sequence, which corresponds to the consensus -Asp-Ser/Thr-Gly- active-site motif of retroviral aspartic proteases. The function of the aspartic protease domain of RF2PEG10 remains unclear. To elucidate the function of PEG10 protease (PRPEG10), we designed a frameshift mutant (fsRF1/RF2PEG10) for comparison with the RF1/RF2PEG10 form. To study the effects of PRPEG10 on cellular proliferation and viability, mammalian HEK293T and HaCaT cells were transfected with plasmids coding for either RF1/RF2PEG10, the frameshift mutant (fsRF1/RF2PEG10), or a PR active-site (D370A) mutant fsRF1/RF2PEG10. Our results indicate that fsRF1/RF2PEG10 overexpression results in increased cellular proliferation. Remarkably, transfection with fsRF1/RF2PEG10 had a detrimental effect on cell viability. We hypothesize that PRPEG10 plays an important role in the function of this retroviral remnant, mediating the proliferation of cells and possibly implicating it in the inhibition of apoptosis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
PEG10
paternally expressed gene 10
cell viability
cell proliferation
cis protease activity
ubiquitination
homology modeling
retroviral-like protease
protease
retrotransposon
aspartic protease
Megjelenés:International Journal Of Molecular Sciences. - 21 : 7 (2020), p. 1-22. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Mahdi, Mohamed (1979-) (orvos, tudományos segédmunkatárs) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
101591
OTKA
NKFIH-1150-6/2019
Egyéb
NKFIH-125238
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

9.

001-es BibID:BIBFORM123925
035-os BibID:(Scopus)85205357357 (WoS)001333880100001
Első szerző:Hoffka Gyula (vegyész)
Cím:Modeling protease-sensitive human pancreatic lipase mutations in the mouse ortholog / Hoffka Gyula, Mhana Samara, Vas Marcell, Toldi Vanda, Mótyán János András, Tőzsér József, Szabó András
Dátum:2024
ISSN:0021-9258 1083-351X
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal Of Biological Chemistry. - 300 : 10 (2024), p. 1-13. -
További szerzők:Mhana, Samara (1994-) Vas Marcell Toldi Vanda (1992-) (molekuláris biológus) Mótyán János András (1981-) (biokémikus, molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Szabó András (1981-) (biokémikus)
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Intézményi repozitóriumban (DEA) tárolt változat
Borító:

10.

001-es BibID:BIBFORM108790
035-os BibID:(Scopus)85148381582 (WoS)000944102100001
Első szerző:Hoffka Gyula (vegyész)
Cím:Self-inhibited state of Venezuelan equine encephalitis virus (VEEV) nsP2 cysteine protease : a crystallographic and molecular dynamics analysis / Gyula Hoffka, George T. Lountos, Danielle Needle, Alexander Wlodawer, David S. Waugh, József Tőzsér, János András Mótyán
Dátum:2023
ISSN:0022-2836
Megjegyzések:The Venezuelan equine encephalitis virus (VEEV) belongs to the Togaviridae family and is pathogenic to both humans and equines. The VEEV non-structural protein 2 (nsP2) is a cysteine protease (nsP2pro) that processes the polyprotein and thus it is a drug target for inhibitor discovery. The atomic structure of the VEEV nsP2 catalytic domain was previously characterized by both X-ray crystallography and computational studies. A modified nsP2pro harboring a N475A mutation in the N terminus was observed to exhibit an unexpected conformation: the N-terminal residues bind to the active site, mimicking binding of a substrate. The large conformational change of the N terminus was assumed to be induced by the N475A mutation, as N475 has an important role in stabilization of the N terminus and the active site. This conformation was first observed in the N475A mutant, but we also found it while determining a crystal structure of the catalytically active nsP2pro containing the wild-type N475 active site residue and K741A/K767A surface entropy reduction mutations. This suggests that the N475A mutation is not a prerequisite for self-inhibition. Here, we describe a high resolution (1.46 ?A) crystal structure of a truncated nsP2pro (residues 463-785, K741A/K767A) and analyze the structure further by molecular dynamics to study the active and self-inhibited conformations of nsP2pro and its N475A mutant. A comparison of the different conformations of the N-terminal residues sheds a light on the interactions that play an important role in the stabilization of the enzyme.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Venezuelan equine encephalitis virus
protease
alphavirus
crystallography
molecular dynamics
Megjelenés:Journal Of Molecular Biology. - 435 : 6 (2023), p. 1-20. -
További szerzők:Lountos, George T. Needle, Danielle Wlodawer, Alexander Waugh, David S. Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Mótyán János András (1981-) (biokémikus, molekuláris biológus)
Pályázati támogatás:TKP2021-EGA-20 (Biotechnology)
Egyéb
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Intézményi repozitóriumban (DEA) tárolt változat
Borító:

11.

001-es BibID:BIBFORM091549
Első szerző:Kassay Norbert (biotechnológus)
Cím:Biochemical Characterization, Specificity and Inhibition Studies of HTLV-1, HTLV-2, and HTLV-3 Proteases / Kassay Norbert, Mótyán János András, Matúz Krisztina, Golda Mária, Tőzsér József
Dátum:2021
ISSN:2075-1729
Megjegyzések:The human T-lymphotropic viruses (HTLVs) are causative agents of severe diseases including adult T-cell leukemia. Similar to human immunodeficiency viruses (HIVs), the viral protease (PR) plays a crucial role in the viral life-cycle via the processing of the viral polyproteins. Thus, it is a potential target of anti-retroviral therapies. In this study, we performed in vitro comparative analysis of human T-cell leukemia virus type 1, 2, and 3 (HTLV-1, -2, and -3) proteases. Amino acid preferences of S4 to S1· subsites were studied by using a series of synthetic oligopeptide substrates representing the natural and modified cleavage site sequences of the proteases. Biochemical characteristics of the different PRs were also determined, including catalytic efficiencies and dependence of activity on pH, temperature, and ionic strength. We investigated the effects of different HIV-1 PR inhibitors (atazanavir, darunavir, DMP-323, indinavir, ritonavir, and saquinavir) on enzyme activities, and inhibitory potentials of IB-268 and IB-269 inhibitors that were previously designed against HTLV-1 PR. Comparative biochemical analysis of HTLV-1, -2, and -3 PRs may help understand the characteristic similarities and differences between these enzymes in order to estimate the potential of the appearance of drug-resistance against specific HTLV-1 PR inhibitors.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
human T-lymphotropic virus
human T-cell leukemia virus
HTLV
HTLV-1
HTLV-2
HTLV-3
protease
retroviral protease
protease inhibitor
inhibitor
HIV protease inhibitor
Megjelenés:Life. - 11 : 2 (2021), p. 1-21. -
További szerzők:Mótyán János András (1981-) (biokémikus, molekuláris biológus) Matúz Krisztina (1980-) (vegyész, biokémikus) Golda Mária (1986-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
125238
OTKA
TÁMOP 4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.D-15/1/KONV-2015-0016
TÁMOP
TKP2020-IKA-04
Egyéb
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

12.

001-es BibID:BIBFORM129865
Első szerző:Mahdi, Mohamed (orvos, tudományos segédmunkatárs)
Cím:Receptor Binding for the Entry Mechanisms of SARS-CoV-2 : Insights from the Original Strain and Emerging Variants / Mohamed Mahdi, Irene Wanjiru Kiarie, János András Mótyán, Gyula Hoffka, Aya Shamal Al-Muffti, Attila Tóth, József Tőzsér
Dátum:2026
ISSN:1999-4915
Megjegyzések:Since its emergence in late 2019, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has continuously evolved, giving rise to multiple variants that have significantly altered the trajectory of the COVID-19 pandemic. These variants have resulted in multiple waves of the pandemic, exhibiting characteristic mutations in the spike (S) protein that may have affected receptor interaction, tissue tropism, and cell entry mechanisms. While the virus was shown to primarily utilize the angiotensin-converting enzyme 2 (ACE2) receptor and host proteases such as transmembrane serine protease 2 (TMPRSS2) for entry into host cells, alterations in the S protein have resulted in changes to receptor binding affinity and use of alternative receptors, potentially expanding the virus's ability to infect different cell types or tissues, contributing to shifts in clinical presentation. These changes have been linked to variations in disease severity, the emergence of new clinical manifestations, and altered transmission dynamics. In this paper, we overview the evolving receptor utilization strategies of SARS-CoV-2, focusing on how mutations in the S protein may have influenced viral entry mechanisms and clinical outcomes across the ongoing pandemic waves.
Tárgyszavak:Orvostudományok Egészségtudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
coronaviruses
SARS-CoV-2
viral entry
receptor utilization
COVID-19
Megjelenés:Viruses-Basel. - 17 : 5 (2026), p. 1-25. -
További szerzők:Kiarie, Irene Wanjiru Mótyán János András (1981-) (biokémikus, molekuláris biológus) Hoffka Gyula (1992-) (vegyész) Al-Muffti, Aya S. (1990-) Tóth Attila (1971-) (biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
Pályázati támogatás:TKP2021-EGA-20
Egyéb
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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