Změnit instituci
Pokročilé nano a mikrotechnologie Pokročilé materiály Strukturní biologie Gen. a prot. rostlin. systémů Molekulární medicína Výzkum mozku a lidské mysli Molekulární vet. medicína

Glykobiochemie - Michaela Wimmerová

Vedoucí výzkumné skupiny
Researcher ID
Telefon: +420 54949 3805, +420 54949 8166
E-mail:
Kancelář:

Research areas

  • Carbohydrate-binding proteins involved in host-pathogen interactions
  • Human glycosyltransferases and their role in cancerogenesis
  • Glycosyltransferases participating in mycobacterial cell wall synthesis
  • Protein engineering of lectins
  • Biomolecular interactions

Main objectives

  • To study the therapeutical aspects of recognition and adhesion phenomena in host-pathogen interactions.
  • Investigations of the structures and interactions of biomacromolecules and their relations to the functions of living systems, disease and therapy.

Content of research

Research focusses on structure-function studies of proteins which participate in oligo-saccharide syntheses (glycosyltransferases), or specific recognition (lectins). Carbohydrates are essential for life and, in addition to their conventional role as structural and energy storage components, they play crucial roles in many recognition events. Specific recognition of glycoconjugates is an important event in biological systems and participates in numerous physiological and pathophysiological processes including cell signalling, differentiation, fertilization, infl ammatory response, as well as in cancerogenesis or pathogen-cell adhesion and recognition. The multiple roles of carbohydrates arise from the stability and the stereochemical diversity of glycosidic bonds.

The life cycles of pathogenic bacteria, fungi and viruses require the specific recognition of host tissue for adhesion and subsequent invasion. A common strategy often used by pathogens involves binding to the host glycoconjugates through sugar-binding proteins that can display exquisite specificity for the target tissue. For many pathogenic organisms, the ability to adhere to host tissues is essential to initiate an infection. Oligosaccharide-mediated recognition and adhesion are, for example, key points in the early steps of P. aeruginosa infection because they are followed by processes such as chronic colonization and biofilm formation together with alginate production under the control of quorum sensing. These last adaptive changes by the bacteria make their eradication difficult because, when in the biofilm phenotype, the bacteria become resistant to antibiotic drugs. This brings new challenges into the therapeutical area because the inhibition of protein-carbohydrate interaction could lead to the inhibition of pathogen recognition and adhesion to the host cell.

One of the groups of proteins we are interested in is a group of lectins from human opportunistic pathogens, such as Pseudomonas aeruginosa, Burkholderia cepacia complex, Aspergillus fumigatus, etc. These organisms are usually widely spread around the population and are not dangerous to healthy individuals. On the other hand, they become highly virulent in contact with immunocompromised patients. Infections developed are associated with high morbidity and mortality in the infected people, especially in individuals under mechanical ventilation and in patients suffering from cystic fibrosis.

Carbohydrate-binding proteins

A) Schematic representation of carbohydrate-binding proteins at the top of pili and flagella responsible for the attachment of the pathogenic bacteria to the epitelial host cell carbohydrates.
B) Crystals of several protein/carbohydrate complexes allowing their structure determination using X-ray.
C) X-ray structure of PA-IIL lectin from Pseudomonas aeruginosa complexed with sugar epitope LNnFP-V (PDB 1W8F).

We use a multidisciplinary approach to study the recognition and adhesion phenomena of pathogens including bacteria, viruses, and fungi to human tissue. We have been identifying new potential protein targets using bioinformatics tools, and they have been prepared in recombinant form using molecular biology approaches. The complementary techniques of binding experiments, isothermal titration microcalorimetry, surface plasmon resonance and high resolution X-ray crystallography are used to decipher the thermodynamic and structural basis for the unusually high-affinity binding of lectins from pathogens to their host carbohydrates. In addition, site-directed mutagenesis in combination with structural and functional studies allow us to understand the roles of particular amino acids in the fine definition of sugar specificity and preference.

Such a structure-function correlation of protein/carbohydrate interaction forms the basis for the rational design of carbohydrate-based drugs directed against adhesion and virulence.

seznam / vizitky

Michaela Wimmerová

prof. RNDr. Michaela Wimmerová, Ph.D.

docentka, manažerka pro koordinaci a správu projektů, vedoucí pracoviště
Lenka Malinovská

Mgr. Lenka Malinovská, Ph.D.

odborná pracovnice ve výzkumu
Atul Kumar

Atul Kumar, Ph.D.

odborný pracovník ve výzkumu - postdoc
Eva Dubská

Mgr. Eva Dubská

odborná pracovnice
Marie Pokorná

Mgr. Marie Pokorná

odborná pracovnice
Peter Kyseľ

Mgr. Peter Kyseľ

odborný pracovník - PhD student
Eva Fujdiarová

MVDr. Eva Fujdiarová

odborná pracovnice - PhD student
Jan Komárek

Mgr. Jan Komárek

odborný pracovník - PhD student
Josef Houser

Mgr. Josef Houser, Ph.D.

odborný pracovník ve výzkumu
Gita Jančaříková

Mgr. Gita Jančaříková

odborná pracovnice - PhD student
Deepti Mishra

Deepti Mishra, Ph.D.

odborná pracovnice ve výzkumu - postdoc
Jitka Ždánská

Mgr. Jitka Ždánská

odborná pracovnice
Jana Kosourová

Mgr. Jana Kosourová

odborná pracovnice

VYBRANÉ PUBLIKACE

2017

  • HOUSER, J; KOZMON, S; MISHRA, D; MISHRA, SK; ROMANO, PR; WIMMEROVA, M; KOCA, J, 2017:Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL. PLOS ONE 12 (12)
  • JANCARIKOVA, G; HOUSER, J; DOBES, P; DEMO, G; HYRSL, P; WIMMEROVA, M, 2017:Characterization of novel bangle lectin from Photorhabdus asymbiotica with dual sugar-binding specificity and its effect on host immunity. PLOS PATHOGENS 13 (8)

2016

  • FUJDIAROVA, E; GAJDOS, L; WIMMEROVA, M, 2016:Study of lectins from Photorhabdus luminescens to reveal their function in P. luminescens life cycle. FEBS JOURNAL 283 , p. 152 - 152.
  • KERR, SC; FISCHER, GJ; SINHA, M; MCCABE, O; PALMER, JM; CHOERA, T; LIM, FY; WIMMEROVA, M; CARRINGTON, SD; YUAN, SP; LOWELL, CA; OSCARSON, S; KELLER, NP; FAHY, JV, 2016:FleA Expression in Aspergillus fumigatus Is Recognized by Fucosylated Structures on Mucins and Macrophages to Prevent Lung Infection. PLOS PATHOGENS 12 (4)
  • KUMAR, A; SYKOROVA, P; DEMO, G; DOBES, P; HYRSL, P; WIMMEROVA, M, 2016:A Novel Fucose-binding Lectin from Photorhabdus luminescens (PLL) with an Unusual Heptabladed beta-Propeller Tetrameric Structure. JOURNAL OF BIOLOGICAL CHEMISTRY 291 (48), p. 25032 - 25049.
  • NORTON, P; COMUNALE, MA; HERRERA, H; WANG, MJ; HOUSER, J; WIMMEROVA, M; ROMANO, PR; MEHTA, A, 2016:Development and application of a novel recombinant Aleuria aurantia lectin with enhanced core fucose binding for identification of glycoprotein biomarkers of hepatocellular carcinoma. PROTEOMICS 16 (24), p. 3126 - 3136.

2015

  • HOUSER, J; KOMAREK, J; CIOCI, G; VARROT, A; IMBERTY, A; WIMMEROVA, M, 2015:Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 71 , p. 442 - 453.
  • SEHNAL, D; VAREKOVA, RS; PRAVDA, L; IONESCU, CM; GEIDL, S; HORSKY, V; JAISWAL, D; WIMMEROVA, M; KOCA, J, 2015:ValidatorDB: database of up-to-date validation results for ligands and non-standard residues from the Protein Data Bank. NUCLEIC ACIDS RESEARCH 43 (D1), p. D369 - D375.
  • SINHA, S; RAXWAL, VK; JOSHI, B; JAGANNATH, A; KATIYAR-AGARWAL, S; GOEL, S; KUMAR, A; AGARWAL, M, 2015:De novo transcriptome profiling of cold-stressed siliques during pod filling stages in Indian mustard (Brassica juncea L.). FRONTIERS IN PLANT SCIENCE 6

2014

  • ADAMOVA, L; MALINOVSKA, L; WIMMEROVA, M, 2014:New Sensitive Detection Method for Lectin Hemagglutination using Microscopy. MICROSCOPY RESEARCH AND TECHNIQUE 77 (10), p. 841 - 849.
  • DEMO, G; PAPOUSKOVA, V; KOMAREK, J; KADERAVEK, P; OTRUSINOVA, O; SRB, P; RABATINOVA, A; KRASNY, L; ZIDEK, L; SKLENAR, V; WIMMEROVA, M, 2014:X-ray vs. NMR structure of N-terminal domain of delta-subunit of RNA polymerase. JOURNAL OF STRUCTURAL BIOLOGY 187 (2), p. 174 - 186.
  • JEREMIAS, L; DEMO, G; KUBAT, V; TRAVNICEK, Z; NOVOSAD, J, 2014:Synthesis and X-Ray Structures of Zinc(II) and Cadmium(II) Heteroleptic Complexes Involving 1,1-Dithiolate and N-Donor Ligands. PHOSPHORUS SULFUR AND SILICON AND THE RELATED ELEMENTS 189 (10), p. 1475 - 1488.
  • KRIZ, Z; ADAM, J; MRAZKOVA, J; ZOTOS, P; CHATZIPAVLOU, T; WIMMEROVA, M; KOCA, J, 2014:Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity. JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN 28 (9), p. 951 - 960.
  • VAREKOVA, RS; JAISWAL, D; SEHNAL, D; IONESCU, CM; GEIDL, S; PRAVDA, L; HORSKY, V; WIMMEROVA, M; KOCA, J, 2014:MotiveValidator: interactive web-based validation of ligand and residue structure in biomolecular complexes. NUCLEIC ACIDS RESEARCH 42 (W1), p. W227 - W233.

2013

  • DEMO, G; FLIEDROVA, B; WEIGNEROVA, L; WIMMEROVA, M, 2013:Crystallization and preliminary X-ray crystallographic analysis of recombinant -mannosidase from Aspergillus niger. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 69 , p. 288 - 291.
  • HOUSER, J; KOMAREK, J; KOSTLANOVA, N; CIOCI, G; VARROT, A; KERR, SC; LAHMANN, M; BALLOY, V; FAHY, JV; CHIGNARD, M; IMBERTY, A; WIMMEROVA, M, 2013:A Soluble Fucose-Specific Lectin from Aspergillus fumigatus Conidia - Structure, Specificity and Possible Role in Fungal Pathogenicity. PLOS ONE 8 (12)
  • KUBAT, V; DEMO, G; JEREMIAS, L; NOVOSAD, J, 2013:Synthesis and structure of tris(dimethyldithiocarbamato) (1,10-phenanthroline)lanthanide complexes. ZEITSCHRIFT FUR KRISTALLOGRAPHIE 228 (8), p. 369 - 373.
  • NOVOTNA, J; GUST, B; KULIK, A; SPIZEK, J; HEIDE, L, 2013:Five gene products are required for assembly of the central pyrrole moiety of coumermycin A(1). JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY 40 (8), p. 915 - 925.
  • NOVOTNA, J; OLSOVSKA, J; NOVAK, P; MOJZES, P; CHALOUPKOVA, R; KAMENIK, Z; SPIZEK, J; KUTEJOVA, E; MARECKOVA, M; TICHY, P; DAMBORSKY, J; JANATA, J, 2013:Lincomycin Biosynthesis Involves a Tyrosine Hydroxylating Heme Protein of an Unusual Enzyme Family. PLOS ONE 8 (12)
  • TVAROSKA, I; KOZMON, S; WIMMEROVA, M; KOCA, J, 2013:A QM/MM Investigation of the Catalytic Mechanism of Metal-Ion-Independent Core 2 beta 1,6-N-Acetylglucosaminyltransferase. CHEMISTRY-A EUROPEAN JOURNAL 19 (25), p. 8153 - 8162.

2012

  • AUDFRAY, A; CLAUDINON, J; ABOUNIT, S; RUVOEN-CLOUET, N; LARSON, G; SMITH, DF; WIMMEROVA, M; LE PENDU, J; ROMER, W; VARROT, A; IMBERTY, A, 2012:Fucose-binding Lectin from Opportunistic Pathogen Burkholderia ambifaria Binds to Both Plant and Human Oligosaccharidic Epitopes. JOURNAL OF BIOLOGICAL CHEMISTRY 287 (6), p. 4335 - 4347.
  • CECIONI, S; PRALY, JP; MATTHEWS, SE; WIMMEROVA, M; IMBERTY, A; VIDAL, S, 2012:Rational Design and Synthesis of Optimized Glycoclusters for Multivalent Lectin-Carbohydrate Interactions: Influence of the Linker Arm. CHEMISTRY-A EUROPEAN JOURNAL 18 (20), p. 6250 - 6263.
  • FROMMEL, J; SOURAL, M; TYLICHOVA, M; KOPECNY, D; DEMO, G; WIMMEROVA, M; SEBELA, M, 2012:Plant aminoaldehyde dehydrogenases oxidize a wide range of nitrogenous heterocyclic aldehydes. AMINO ACIDS 43 (3), p. 1189 - 1202.
  • HOUSER, J.;J. KOMAREK;N. KOSTLANOVA;G. CIOCI;A. IMBERTY;M. WIMMEROVA., 2012:Protein oligomerization in Aleuria aurantia lectin family - importance and difficulties. Materials Structure in Chemistry 19 , p. 20 - 21.
  • MARCHETTI, R; MALINOVSKA, L; LAMEIGNERE, E; ADAMOVA, L; DE CASTRO, C; CIOCI, G; STANETTY, C; KOSMA, P; MOLINARO, A; WIMMEROVA, M; IMBERTY, A; SILIPO, A, 2012:Burkholderia cenocepacia lectin A binding to heptoses from the bacterial lipopolysaccharide. GLYCOBIOLOGY 22 (10), p. 1387 - 1398.
  • MISHRA, S; ADAMOVA, L; ADAM, J; WIMMEROVA, M; KOCA, J, 2012:Comparison of Docking Software to Predict Saccharide Binding to Proteins Combination with In silico Protein Engineering. GLYCOBIOLOGY 22 (11), p. 1648 - 1649.
  • MISHRA, SK; ADAM, J; WIMMEROVA, M; KOCA, J, 2012:In Silico Mutagenesis and Docking Study of Ralstonia solanacearum RSL Lectin: Performance of Docking Software To Predict Saccharide Binding. JOURNAL OF CHEMICAL INFORMATION AND MODELING 52 (5), p. 1250 - 1261.
  • SEHNAL, D; VAREKOVA, RS; HUBER, HJ; GEIDL, S; IONESCU, CM; WIMMEROVA, M; KOCA, J, 2012:SiteBinder: An Improved Approach for Comparing Multiple Protein Structural Motifs. JOURNAL OF CHEMICAL INFORMATION AND MODELING 52 (2), p. 343 - 359.
  • TVAROSKA, I; KOZMON, S; WIMMEROVA, M; KOCA, J, 2012:Substrate-Assisted Catalytic Mechanism of O-GIcNAc Transferase Discovered by Quantum Mechanics/Molecular Mechanics Investigation. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY 134 (37), p. 15563 - 15571.
  • VICHA, J; DEMO, G; MAREK, R, 2012:Platinum-Modified Adenines: Unprecedented Protonation Behavior Revealed by NMR Spectroscopy and Relativistic Density-Functional Theory Calculations. INORGANIC CHEMISTRY 51 (3), p. 1371 - 1379.
  • VISACKA, K; HOFR, C; WILLCOX, S; NECASOVA, I; PAVLOUSKOVA, J; SEPSIOVA, R; WIMMEROVA, M; SIMONICOVA, L; NOSEK, J; FAJKUS, J; GRIFFITH, JD; TOMASKA, L, 2012:Synergism of the Two Myb Domains of Tay1 Protein Results in High Affinity Binding to Telomeres. JOURNAL OF BIOLOGICAL CHEMISTRY 287 (38), p. 32206 - 32215.
  • WIMMEROVA, M; KOZMON, S; NECASOVA, I; MISHRA, SK; KOMAREK, J; KOCA, J, 2012:Stacking Interactions between Carbohydrate and Protein Quantified by Combination of Theoretical and Experimental Methods. PLOS ONE 7 (10)

2011

  • CECIONI, S; FAURE, S; DARBOST, U; BONNAMOUR, I; PARROT-LOPEZ, H; ROY, O; TAILLEFUMIER, C; WIMMEROVA, M; PRALY, JP; IMBERTY, A; VIDAL, S, 2011:Selectivity among Two Lectins: Probing the Effect of Topology, Multivalency and Flexibility of "Clicked" Multivalent Glycoclusters. CHEMISTRY-A EUROPEAN JOURNAL 17 (7), p. 2146 - 2159.
  • DASTYCH, D; ROTTER, P; DEMO, G; DASTYCHOVA, L, 2011:Di-mu-chlorido-bis[diacetonitrilechloridooxidovanadium(IV)]. ACTA CRYSTALLOGRAPHICA SECTION E-STRUCTURE REPORTS ONLINE 67 , p. M1398 - U940.
  • GILBOA-GARBER, N; ZINGER-YOSOVICH, KD; SUDAKEVITZ, D; LERRER, B; IMBERTY, A; WIMMEROVA, M; WU, AM; GARBER, NC, 2011:The Five Bacterial Lectins: PA-II, PA-III, RSL, RS-III and CV-III Interactions with Diverse Animal Cells and Glycoproteins. Advances in Experimental Medicine and Biology 705 , p. 155 - 211.
  • HAVEL, V; SVEC, J; WIMMEROVA, M; DUSEK, M; POJAROVA, M; SINDELAR, V, 2011:Bambus[n]urils: a New Family of Macrocyclic Anion Receptors. ORGANIC LETTERS 13 (15), p. 4000 - 4003.
  • REVESZ, A; SCHRODER, D; SVEC, J; WIMMEROVA, M; SINDELAR, V, 2011:Anion Binding by Bambus[6]uril Probed in the Gas Phase and in Solution. JOURNAL OF PHYSICAL CHEMISTRY A 115 (41), p. 11378 - 11386.
  • SULAK, O; CIOCI, G; LAMEIGNERE, E; BALLOY, V; ROUND, A; GUTSCHE, I; MALINOVSKA, L; CHIGNARD, M; KOSMA, P; AUBERT, DF; MAROLDA, CL; VALVANO, MA; WIMMEROVA, M; IMBERTY, A, 2011:Burkholderia cenocepacia BC2L-C Is a Super Lectin with Dual Specificity and Proinflammatory Activity. PLOS PATHOGENS 7 (9)

2010

  • KLUMPLER, T; SEDLACEK, V; MAREK, J; WIMMEROVA, M; KUCERA, I, 2010:Crystallization and initial X-ray diffraction studies of the flavoenzyme NAD(P)H:(acceptor) oxidoreductase (FerB) from the soil bacterium Paracoccus denitrificans. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 66 , p. 431 - 434.
  • LAMEIGNERE, E; SHIAO, TC; ROY, R; WIMMEROVA, M; DUBREUIL, F; VARROT, A; IMBERTY, A, 2010:Structural basis of the affinity for oligomannosides and analogs displayed by BC2L-A, a Burkholderia cenocepacia soluble lectin. GLYCOBIOLOGY 20 (1), p. 87 - 98.
  • MISHRA, NK; KRIZ, Z; WIMMEROVA, M; KOCA, J, 2010:Recognition of selected monosaccharides by Pseudomonas aeruginosa Lectin II analyzed by molecular dynamics and free energy calculations. CARBOHYDRATE RESEARCH 345 (10), p. 1432 - 1441.
  • SULAK, O; CIOCI, G; DELIA, M; LAHMANN, M; VARROT, A; IMBERTY, A; WIMMEROVA, M, 2010:A TNF-like Trimeric Lectin Domain from Burkholdeda cenocepacia with Specificity for Fucosylated Human Histo-Blood Group Antigens. STRUCTURE 18 (1), p. 59 - 72.

2009

  • HANSEN, SF; BETTLER, E; WIMMEROVA, M; IMBERTY, A; LEROUXEL, O; BRETON, C, 2009:Combination of Several Bioinformatics Approaches for the Identification of New Putative Glycosyltransferases in Arabidopsis. JOURNAL OF PROTEOME RESEARCH 8 (2), p. 743 - 753.
  • HOFR, C., SULTESOVA, P., ZIMMERMANN, M., MOZGOVA, I., SCHRUMPFOVA, P. P., WIMMEROVA, M., FAJKUS, J.,, 2009:Single-Myb-histone proteins from Arabidopsis thaliana: a quantitative study of telomere-binding specificity and kinetics. BIOCHEMICAL JOURNAL 419 , p. 221 - 228.
  • CHEMANI, C; IMBERTY, A; DE BENTZMANN, S; PIERRE, M; WIMMEROVA, M; GUERY, BP; FAURE, K, 2009:Role of LecA and LecB Lectins in Pseudomonas aeruginosa-Induced Lung Injury and Effect of Carbohydrate Ligands. INFECTION AND IMMUNITY 77 (5), p. 2065 - 2075.
  • MATEJKOVA, M; ZIDKOVA, J; ZIDEK, L; WIMMEROVA, M; CHMELIK, J; SKLENAR, V, 2009:Investigation of Thermal Denaturation of Barley Nonspecific Lipid Transfer Protein 1 (ns-LTP1b) by Nuclear Magnetic Resonance and Differential Scanning Calorimetry. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 57 (18), p. 8444 - 8452.
  • TESARIK, R; SEDLACEK, V; PLOCKOVA, J; WIMMEROVA, M; TURANEK, J; KUCERA, I, 2009:Heterologous expression and molecular characterization of the NAD(P)H:acceptor oxidoreductase (FerB) of Paracoccus denitrificans. PROTEIN EXPRESSION AND PURIFICATION 68 (2), p. 233 - 238.
  • WIMMEROVA, M; MISHRA, NK; POKORNA, M; KOCA, J, 2009:Importance of oligomerisation on Pseudomonas aeruginosa Lectin-II binding affinity. In silico and in vitro mutagenesis. JOURNAL OF MOLECULAR MODELING 15 (6), p. 673 - 679.

GRANTY

  • Glykoklastry kalix[4]aren/C-oligosacharidy pro studium selektivity interakcí s lektiny (GA15-17572S), Czech Science Foundation - Standard Grants, 2015 - 2017
  • Příprava lektinů s vysokou specifitou a afinitou (GPP207/11/P185), Czech Science Foundation - Postdoc Grants, 2011 - 2013
  • Identification, caractérisation et détermination du rôle des lectines impliquées dans l’adhésion des champignons filamenteux Aspergillus fumigatus et Scedosporium apiospermum (RF20110600501), Vaincre la Mucoviscidose, 2011 - 2013
  • Enzymy metabolismu mannosidů v přípravě N-acetyl-mannosaminových struktur (GAP207/10/0321), Czech Science Foundation - Standard Grants, 2010 - 2013
  • Structure-function studies on lectins and adhesins from microbial patogens (GA303/06/0570), Czech Science Foundation - Standard Grants, 2006 - 2008
  • Lectins from human pathogens – structure, function, engineering (GA303/09/1168), Czech Science Foundation - Standard Grants, 2009 - 2012
  • Design of Carbohydrates and Glycomimetics as Antibacterial and Antiviral Drugs (ME08008), MEYS - KONTAKT, 2008 - 2012
  • Structure-functional characterisation of oxidoreductases acting on nitrogenous regulatory compounds in plants (GA522/08/0555), Czech Science Foundation - Standard Grants, 2008 - 2012
  • CIISB - České centrum pro integrativní strukturní biologii (LM2015043), MEYS, 2016 - 2019

CURRENT RESEARCH INFRASTRUCTURE

The current infrastructure includes SPR Biacore 3000,  isothermal titration calorimeters, AutoITC200, VP-DSC differential scanning calorimeter, DynaPro Plate Reader dynamic light scattering plate reader, Jasco 850 CD spectrophotometer, ProteomLab XL-1 analytical ultracentrifuge, Mosquito crystallization robot, Rigaku Desktop Minstrel UV + Plate Hotel Gallery 160 automatic visualization and documentation system for crystallization, Tecan Evo150 automatic pipetting station, PM-1s automatic colony picker, AKTA Purifier, AKTA FPLC, common equipment for molecular biology and biochemistry work.

1. Structure-functional study of proteins involved in host cell recognition

Supervisor:  prof. RNDr. Michaela Wimmerová, Ph.D.

Annotation 

Lectins are ubiquitous carbohydrate-binding proteins, which play a key role in various processes including cell-cell communication and host-pathogen interaction, but also serve as a valuable tool for medicine and life sciences research. Carbohydrate-mediated recognition plays an important role in the ability of pathogenic bacteria to adhere to the surface of the host cell in the first step of their invasion and infectivity. Lectin-carbohydrate interactions are usually characterised by a low affinity for monovalent ligands that is balanced by multivalency resulting in high avidity for complex glycans or cell surfaces.
The main aim of the PhD work will be the structure-functional studies of carbohydrate binding proteins involved in a bacterial pathogenesis and/or their application as the bioanalytical tool to study a specific glycosylation related to cell specific tissues.

Keywords: lectins, pathogens, X-ray crystallography, biomolecular interactions, tissue specific glycosylation

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