József Dobó

Summary

Affiliation: Hungarian Academy of Sciences
Country: Hungary

Publications

  1. pmc Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region
    József Dobó
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Acta Crystallogr Sect F Struct Biol Cryst Commun 64:781-4. 2008
  2. doi request reprint MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity
    József Dobó
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    J Immunol 183:1207-14. 2009
  3. pmc Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1
    József Dobó
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary
    PLoS ONE 6:e20036. 2011
  4. doi request reprint Serum MASP-1 in complex with MBL activates endothelial cells
    Márton Megyeri
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Mol Immunol 59:39-45. 2014
  5. doi request reprint Dissociation and re-association studies on the interaction domains of mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, provide evidence for heterodimer formation
    Katalin Paréj
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 29 Karolina Street, H 1113 Budapest, Hungary
    Mol Immunol 59:1-9. 2014
  6. pmc Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway
    Márton Megyeri
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 29 Karolina Street, H 1113 Budapest, Hungary
    J Biol Chem 288:8922-34. 2013
  7. pmc Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2
    Dávid Héja
    Department of Biochemistry, Eotvos Lorand University, 1 C Pázmány Péter Street, H 1117, Budapest, Hungary
    J Biol Chem 287:20290-300. 2012
  8. pmc MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked
    József Dobó
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H 1117, Budapest, Hungary
    Sci Rep 6:31877. 2016
  9. ncbi request reprint Localization of the flagellum-specific secretion signal in Salmonella flagellin
    Barbara M Végh
    Institute of Enzymology, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Biochem Biophys Res Commun 345:93-8. 2006
  10. doi request reprint Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation
    Andrea Kocsis
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    J Immunol 185:4169-78. 2010

Collaborators

  • Peter Gal
  • László Beinrohr
  • Orsolya Toke
  • József Kardos
  • Marius Ueffing
  • Anne Zeck
  • Steffen Thiel
  • Gabor Juhasz
  • Matthias Wilmanns
  • Peter Zavodszky
  • Márton Megyeri
  • Ráchel Sajó
  • Katalin Paréj
  • Gabor Pal
  • Péter K Jani
  • Dávid Héja
  • Ferenc Vonderviszt
  • Andrea Kocsis
  • Gábor Oroszlán
  • Barbara M Végh
  • Laszlo Cervenak
  • Erika Kajdacsi
  • Balázs Major
  • Veronika Harmat
  • Júlia Balczer
  • Katalin A Kekesi
  • Sascha Dammeier
  • Hajnalka Jankovics
  • Elod Kortvely
  • András Micsonai
  • István Hajdú
  • Dávid Szakács
  • Veronika Makó
  • Nóra Donáth
  • Janos Rigo
  • Krisztina Futosi
  • Csaba I Timár
  • Endre Schwaner
  • Karoly Liliom
  • Zoltán Doleschall
  • Agnes Hermann
  • Attila Mocsai
  • Adél Muskotál
  • Agnes Klein
  • Katalin Szilágyi
  • Dániel Datz
  • Adám Végh
  • Krisztian Fodor
  • Robert Szasz

Detail Information

Publications23

  1. pmc Purification, crystallization and preliminary X-ray analysis of human mannose-binding lectin-associated serine protease-1 (MASP-1) catalytic region
    József Dobó
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Acta Crystallogr Sect F Struct Biol Cryst Commun 64:781-4. 2008
    ..55 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 68.4, b = 70.4, c = 121.4 A. The crystal structure of MASP-1 may help in understanding the function of this mysterious serine protease...
  2. doi request reprint MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity
    József Dobó
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    J Immunol 183:1207-14. 2009
    ..The structure shows that its substrate binding groove is accessible; however, its reactivity could be modulated by an unusually large 60-loop and an internal salt bridge involving the S1 Asp...
  3. pmc Cleavage of kininogen and subsequent bradykinin release by the complement component: mannose-binding lectin-associated serine protease (MASP)-1
    József Dobó
    Institute of Enzymology, Hungarian Academy of Sciences, Budapest, Hungary
    PLoS ONE 6:e20036. 2011
    ....
  4. doi request reprint Serum MASP-1 in complex with MBL activates endothelial cells
    Márton Megyeri
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Mol Immunol 59:39-45. 2014
    ..Our results strengthen the view that MASP-1 plays a central role in the early innate immune response. ..
  5. doi request reprint Dissociation and re-association studies on the interaction domains of mannan-binding lectin (MBL)-associated serine proteases, MASP-1 and MASP-2, provide evidence for heterodimer formation
    Katalin Paréj
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 29 Karolina Street, H 1113 Budapest, Hungary
    Mol Immunol 59:1-9. 2014
    ..The existence of heterodimers influences the current view on the composition of lectin pathway complexes and their activation. ..
  6. pmc Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway
    Márton Megyeri
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, 29 Karolina Street, H 1113 Budapest, Hungary
    J Biol Chem 288:8922-34. 2013
    ..In summary, autoactivation of MASP-1 is crucial for the activation of MBL/ficolin·MASP complexes, and in the proenzymic phase zymogen MASP-1 controls the process...
  7. pmc Monospecific inhibitors show that both mannan-binding lectin-associated serine protease-1 (MASP-1) and -2 Are essential for lectin pathway activation and reveal structural plasticity of MASP-2
    Dávid Héja
    Department of Biochemistry, Eotvos Lorand University, 1 C Pázmány Péter Street, H 1117, Budapest, Hungary
    J Biol Chem 287:20290-300. 2012
    ..The 1.28 Å resolution MASP-2 structure reveals significant plasticity of the protease, suggesting that either an induced fit or a conformational selection mechanism should contribute to the extreme specificity of the enzyme...
  8. pmc MASP-3 is the exclusive pro-factor D activator in resting blood: the lectin and the alternative complement pathways are fundamentally linked
    József Dobó
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok körútja 2, H 1117, Budapest, Hungary
    Sci Rep 6:31877. 2016
    ..For this study we evolved a specific MASP-3 inhibitor and unambiguously proved that activated MASP-3 is the exclusive pro-FD activator in resting blood, which demonstrates a fundamental link between the lectin and alternative pathways. ..
  9. ncbi request reprint Localization of the flagellum-specific secretion signal in Salmonella flagellin
    Barbara M Végh
    Institute of Enzymology, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    Biochem Biophys Res Commun 345:93-8. 2006
    ..Our results demonstrate that the 22-residue long 26-47 segment within the disordered N-terminal region of Salmonella flagellin contains the recognition signal for the flagellar export machinery...
  10. doi request reprint Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation
    Andrea Kocsis
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    J Immunol 185:4169-78. 2010
    ..Because the lectin pathway has been implicated in several life-threatening pathological states, these inhibitors should be considered as lead compounds toward developing lectin pathway blocking therapeutics...
  11. ncbi request reprint C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease
    László Beinrohr
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina ut 29, H 1113 Budapest, Hungary
    J Biol Chem 282:21100-9. 2007
    ..These results may help to improve therapeutic C1 inhibitor preparations used in the treatment of hereditary angioedema, organ transplant rejection, and heart attack...
  12. doi request reprint C1, MBL-MASPs and C1-inhibitor: novel approaches for targeting complement-mediated inflammation
    László Beinrohr
    Institute of Enzymology, Karolina ut 29, H 1113 Budapest, Hungary
    Trends Mol Med 14:511-21. 2008
    ..Complement-mediated inflammation has been linked to ischemia-reperfusion injury, organ graft rejection and even neurodegeneration, so targeting this process has direct clinical implications...
  13. doi request reprint The control of the complement lectin pathway activation revisited: both C1-inhibitor and antithrombin are likely physiological inhibitors, while α2-macroglobulin is not
    Katalin Paréj
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Karolina ut 29, Budapest H 1113, Hungary
    Mol Immunol 54:415-22. 2013
    ..Although α(2)M formed complex with MASP-1 in fluid phase, it could not abolish lectin pathway activation on activator surfaces...
  14. ncbi request reprint Inhibition of the serine proteases of the complement system
    Peter Gal
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
    Adv Exp Med Biol 735:23-40. 2013
    ..A promising approach to yield more specific compounds is the alteration of natural protease inhibitors through engineering or directed evolution resulting in new variants with fine-tuned specificity and enhanced affinity...
  15. ncbi request reprint Inhibition of the serine proteases of the complement system
    Peter Gal
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
    Adv Exp Med Biol 734:23-40. 2013
    ..A promising approach to yield more specific compounds is the alteration of natural protease inhibitors through engineering or directed evolution resulting in new variants with fine-tuned specificity and enhanced affinity...
  16. doi request reprint The emerging roles of mannose-binding lectin-associated serine proteases (MASPs) in the lectin pathway of complement and beyond
    József Dobó
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
    Immunol Rev 274:98-111. 2016
    ..Defect or more likely over-activation of MASPs may culminate into diseases such as ischemia-reperfusion injury (IRI); hence, MASPs are all potential targets of drug development...
  17. doi request reprint MASP-1 and MASP-2 Do Not Activate Pro-Factor D in Resting Human Blood, whereas MASP-3 Is a Potential Activator: Kinetic Analysis Involving Specific MASP-1 and MASP-2 Inhibitors
    Gábor Oroszlán
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, H 1117 Budapest, Hungary
    J Immunol 196:857-65. 2016
    ..Combining our quantitative data, MASP-1 and MASP-2 can be ruled out as direct pro-FD activators in resting blood; however, active MASP-3 is a very likely physiological activator...
  18. doi request reprint Multiple roles of complement MASP-1 at the interface of innate immune response and coagulation
    József Dobó
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt 2, H 1113 Budapest, Hungary
    Mol Immunol 61:69-78. 2014
    ..Due to the relaxed specificity, MASP-1 interacts with the coagulation cascade and the kinin generating system, and it can also activate endothelial cells eliciting pro-inflammatory signaling. ..
  19. doi request reprint Soluble components of the flagellar export apparatus, FliI, FliJ, and FliH, do not deliver flagellin, the major filament protein, from the cytosol to the export gate
    Ráchel Sajó
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Magyar tudósok krt 2, H 1117 Budapest, Hungary
    Biochim Biophys Acta 1843:2414-23. 2014
    ..It seems that the abundantly produced flagellin does not require the assistance of the soluble export components to efficiently reach the export gate. ..
  20. pmc MASP-1 induces a unique cytokine pattern in endothelial cells: a novel link between complement system and neutrophil granulocytes
    Péter K Jani
    3rd Department of Internal Medicine, Semmelweis University, Budapest, Hungary
    PLoS ONE 9:e87104. 2014
    ..Our results implicate that besides initializing the complement lectin pathway, MASP-1 may activate neutrophils indirectly, via the endothelial cells, which link these effective antimicrobial host defense mechanisms. ..
  21. doi request reprint Early complement proteases: C1r, C1s and MASPs. A structural insight into activation and functions
    Peter Gal
    Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary
    Mol Immunol 46:2745-52. 2009
    ..We also discuss some open questions and debated issues that need to be resolved in the future...
  22. pmc Application of a short, disordered N-terminal flagellin segment, a fully functional flagellar type III export signal, to expression of secreted proteins
    József Dobó
    Institute of Enzymology, BRC, Hungarian Academy of Sciences, Budapest, Hungary
    Appl Environ Microbiol 76:891-9. 2010
    ..Certain fusion proteins that are easily degraded within the cells were found to be intact in the medium, implying a potential application of this expression system for proteins with high proteolytic susceptibility...
  23. doi request reprint Structural plasticity of the Salmonella FliS flagellar export chaperone
    Ráchel Sajó
    Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
    FEBS Lett 590:1103-13. 2016
    ..As FliS has several binding partners within the cell, conformational adaptability seems to be an essential requirement to fulfill its multiple roles. ..