COVID-19 interview

Inforadio asked Beáta Vértessy about current questions related to COVID-19 and its causativa agent, the SARS-CoV-2 virus (the interview is in Hungarian)

The main points of the interview:


Broadcast in the Szigma, The World of Science magazine:




Vértessy Beáta nyilatkozata az Inforádióban

Vértessy Beáta nyilatkozata az Inforádióban: az egészséges emberi 
magzatokon végzett CRISPR kísérletek felelőletlenek és feleslegesek, 
ezeket elutasítja a tudományos világ.

A Hong Kongban 2018. november 27-28 között megszervezett Second 
International Summit on Human Genome Editing konferencia előestéjén egy 
kínai kutató azt állította, hogy egészséges emberi magzatokon CRISPR 
eljárással génszerkesztést végzett. Az állítások egyelőre nincsenek 
tudományosan alátámasztva. A tudományos világ egységesen elutasítja az 
ilyen etikátlan és felelőtlen kísérleteket. Vértessy Beátát az Inforádió 
riportere kérdezte meg ebben az ügyben.



New laboratory for malaria research

Our new laboratory was recently set up focusing on malaria research. For that reason we had an opening ceremony to celebrate the first malaria laboratory in the middle-East Europe. The laboratory is co-operated by the Budapest University of Technology and Economics (BUTE), and the Research Centre for Natural Sciences, Hungarian Academy of Sciences (RCNS, HAS). 

Photos: (source:


Our group in K&H Marathon relay

Our group has again considered an athletic challenge with success - six of us ran a marathon relay on June 11, 2017 in the Városliget, Budapest. Each of us (Beáta Vértessy, Anett Stéger, Kinga Nagy, Gergely Koppány, Judit Matejka and Hajnalka Németh)  ran 7 km thus completing together the 42 km race in the beautiful, although rather hot weather.




Great participation at Student's Association Conference

The Student's Association Conference is organized every year at universities in Hungary, under this programme students compete their research work with each other in different fields of studies. 

Our research group performed excellently in this year's conference at Budapest University of Technology and Economics.

Fanni Hajdú 1. award  - supervisors Gergely Nagy & Lívia Marton

Gergely Tihanyi 2. award - supervisors Hajnalka Pálinkás & Gergely Róna 

Viktória Herczeg prize of merit award - supervisor Kinga Nagy 

Gergely Takács prize of merit award - supervisor Ildikó Scheer 

Congratulation for their great preformance to all of them and their supervisors!


Our recent review in a BBA Special Issue

Kinga Nyíri and Beáta Vértessy recently published a review in Science for Life Special Issue of BBA General Subjects about the

Perturbation of genome integrity to fight pathogenic microorganisms.

The review summarizes the current advances of thymidylate biosynthesis inhibition in challenging pathogens.

Resistance against antibiotics is unfortunately still a major biomedical challenge for a wide range of pathogens responsible for potentially fatal diseases.

Scope of review
In this study, we aim at providing a critical assessment of the recent advances in design and use of drugs targeting genome integrity by perturbation of thymidylate biosynthesis.

Major conclusion
We find that research efforts from several independent laboratories resulted in chemically highly distinct classes of inhibitors of key enzymes within the routes of thymidylate biosynthesis. The present article covers numerous studies describing perturbation of this metabolic pathway in some of the most challenging pathogens like Mycobacterium tuberculosis, Plasmodium falciparum, and Staphylococcus aureus.

General significance
Our comparative analysis allows a thorough summary of the current approaches to target thymidylate biosynthesis enzymes and also include an outlook suggesting novel ways of inhibitory strategies.

 Nyiri Fig1 Nyiri Fig3



New article published in PLos One

Mária Pukáncsik and Kinga Nagy article is published in PLos One.

Hereby you may find some highlights making you eager to read this very interesting article.

A novel uracil-DNA degrading protein factor (termed UDE) was identified in Drosophila melanogaster with no significant structural and functional homology to other uracil-DNA binding or processing factors. Determination of the 3D structure of UDE is excepted to provide key information on the description of the molecular mechanism of action of UDE catalysis, as well as in general uracil-recognition and nuclease action. Towards this long-term aim, the random library ESPRIT technology was applied to the novel protein UDE to overcome problems in identifying soluble expressing constructs given the absence of precise information on domain content and arrangement. Nine constructs of UDE were chosen to decipher structural and functional relationships. Vacuum ultraviolet circular dichroism (VUVCD) spectroscopy was performed to define the secondary structure content and location within UDE and its truncated variants. The quantitative analysis demonstrated exclusive α-helical content for the full-length protein, which is preserved in the truncated constructs. Arrangement of α-helical bundles within the truncated protein segments suggested new domain boundaries which differ from the conserved motifs determined by sequence-based alignment of UDE homologues. Here we demonstrate that the combination of ESPRIT and VUVCD spectroscopy provides a new structural description of UDE and confirms that the truncated constructs are useful for further detailed functional studies.

nagy kinga cikk jo

A) Secondary structure content determination of UDE and its fragments using VUVCD and SELCON3 program. Vacuum-ultraviolet circular dichroism (Δε) spectra of the UDE protein and some of its truncated fragments measured over the wavelength region of λ=170-255 nm. spectrum of UDE is shown in red. B) Final estimate for the secondary structure of UDE obtained as an average of the structure of full-length UDE protein and in its nine truncated fragments were determined from the CD spectra and the amino acid sequence using a neural network algorithm. The α-helical segments and β-strands are displayed in blue and red, respectively, while both turns and disordered parts appear in yellow.

Article of Judit Szabó et al. published in Scientific Reports

Article of Judit Szabó et al. is published in Scientific Reports      
Scientific Reports

Hereby you may find some highlights making you eager to read this very interesting article.

Members of the dUTPase superfamily play an important role in the maintenance of the pyrimidine nucleotide balance and of genome integrity. dCTP deaminases and the bifunctional dCTP deaminase-dUTPases are cooperatively regulated by dTTP. However, the manifestation of allosteric behavior within the same trimeric protein architecture of dUTPases, the third member of the superfamily, has been a question of debate for decades. Therefore, we designed hybrid dUTPase trimers to access conformational states potentially mimicking the ones observed in the cooperative relatives. We studied how the interruption of different steps of the enzyme cycle affects the active site cross talk. We found that subunits work independently in dUTPase. The experimental results combined with a comparative structural analysis of dUTPase superfamily enzymes revealed that subtile structural differences within the allosteric loop and the central channel in these enzymes give rise to their dramatically different cooperative behavior. We demonstrate that the lack of allosteric regulation in dUTPase is related to the functional adaptation to more efficient dUTP hydrolysis which is advantageous in uracil-DNA prevention.

Asymmetric hybrid enzymes exhibit non-cooperative kinetics in the different reaction steps.

SZJ SciRep Fig

(a) Schematic representation of the created hybrids (covalent heterotrimers). Blue, red and yellow spheres represent dUTPase protomers containing the D102N, A98F and T148STOP mutations, respectively. Note, that all protomers contain the F158W mutation as well, except for the T148STOP mutant. Grey areas indicate enzymatic inactivity. (b) Steady-state kinetics of human dUTPase constructs: WWW (solid square), WWN (solid triangles), WNN (open triangles), WWF (solid stars), WWS (solid circle). Smooth lines through the data are hyperbolic fits yielding Vmax= 7.9 ± 0.5 s−1 for WWW, Vmax = 4.4 ± 0.2 s−1 for WWF, Vmax = 3.8 ± 0.2 s−1 for WWN, Vmax = 1.8 ± 0.1 s−1 for WNN, Vmax = 2.9 ± 0.3 s−1 for WWS. KM values are listed in Table 1. (c) Comparison of the catalytic constants (striped bar) and apparent catalytic constants (grey bar) for determined by single turnover (transient kinetics) and steady-state experiments, respectively. See also Table 1 for the data. (d) Fluorescence intensity titrations upon dUTP binding to the various dUTPase constructs measured by stopped-flow (the symbol code is identical to that in panel (b). Smooth lines through data are hyperbolic fits yielding Kd values summarized in Table 1.

Five members of the laboratory were awarded by Richter Gedeon Short Term Research Grant

András Benedek, Kinga Nyíri, Veronika Papp-Kádár, Hajnalka Pálinkás and Judit Eszter Szabó 

were awarded by Richter Gedeon Short Term Research Grant.

The Awardees thank to Richter Gedeon Ltd. for supporting their attendance at international conferences and courses.

logo richter


Beáta G. Vértessy, Chair of Board of the US-Hungarian Fulbright Foundation, signed agreement with Prof László Lovász, President of the Hungarian Academy of Sciences for joint support

The Hungarian Academy of Sciences, represented by its President, Professor László Lovász, and the Hungarian-American Fulbright Commission, represented by Board Chair Professor Beáta Vértessy and Károly Jókay, Executive Director, signed a multi-year agreement on March 23, 2016, in the the ornate concert hall in the Academy’s main building. Fulbright Board members Tamás MagyaricsTibor Frank and Eric Watnik (representing the US Embassy) also took part in the ceremony.

MTA Fulbright

The agreement will support Hungarian scholars who are employees of the Academy’s research network, on various “Momentum” (Lendület) teams, or are active in Academy-funded projects at Hungary’s universities. During the upcoming academic year 2016-17, two Hungarian researchers will be in the US on jointly-funded Fulbrights: one geophysicist and one astrophysicist. US scholars will also be eligible for the joint grants, and in 2016-17, one US sociologist will arrive in Budapest.

The Academy and Fulbright expect that up to 4 additional scholars per year will be able to conduct research in the US and in Hungary based on the terms of the agreement just signed.

For US scholars interested in applying for the 2017-18 Academic Year, see the CIES catalog of awards at:

Hungarian researchers affiliated with the Academy please see:

For further information contact the Fulbright Commission in Budapest at: This email address is being protected from spambots. You need JavaScript enabled to view it.

New paper published in Structural Chemistry

Our paper entitled "Exploring the role of the phage-specific insert of
bacteriophage Φ11 dUTPase" has been published in Structural Chemistry.

dUTPases are essential for maintaining genome integrity. Recently, in the case of a dUTPase from a Staphylococcal phage, another different physiological function was also suggested. Namely, it was shown that dUTPase from the Staphylococcus aureus bacteriophage Ф11 is capable of binding to the Staphylococcal Stl repressor protein. This binding interferes with the function of Stl. In the present study, we investigated the putative role of a phage dUTPase-specific peptide segment in the interaction of dUTPase with Stl and in impeding Stl–DNA complex formation. We show that dUTPase from Mycobacterium tuberculosis that lacks the phage-specific insert is also capable of disrupting the complexation between Stl and DNA. Hence, the insert segment is not essential for perturbation of the Stl function. However, we also demonstrate that in case of the phage dUTPase, the insert-lacking construct is deficient in perturbation of Stl activity. These findings clearly indicate that the phage-specific insert has a well-defined role only in the context of the phage dUTPase. Structural Chemistry, 30 August 2015, doi: 10.1007/s11224-015-0652-2



Genome Metabolism and Biostruct Laboratory

Budapest University of Technology, Ch building
Szt. Gellért square 4.

RCNS Institute of Enzymology
Magyar tudosok korutja 2.