Samuel Pažický

ORCID: 0000-0002-4674-9784
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About
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Research Areas
  • Malaria Research and Control
  • Immune Cell Function and Interaction
  • Trypanosoma species research and implications
  • Cardiomyopathy and Myosin Studies
  • Monoclonal and Polyclonal Antibodies Research
  • T-cell and B-cell Immunology
  • Biochemical and Molecular Research
  • Mosquito-borne diseases and control
  • Immunotherapy and Immune Responses
  • Glycosylation and Glycoproteins Research
  • Computational Drug Discovery Methods
  • HIV Research and Treatment
  • Carbohydrate Chemistry and Synthesis
  • Supramolecular Self-Assembly in Materials
  • Toxoplasma gondii Research Studies
  • SARS-CoV-2 and COVID-19 Research
  • Hemoglobin structure and function
  • Gene expression and cancer classification
  • Multiple Myeloma Research and Treatments
  • CAR-T cell therapy research
  • Signaling Pathways in Disease
  • thermodynamics and calorimetric analyses
  • Vector-borne infectious diseases
  • Polyamine Metabolism and Applications
  • Peptidase Inhibition and Analysis

Nanyang Technological University
2025

Centre for Structural Systems Biology
2018-2022

Deutsches Elektronen-Synchrotron DESY
2019-2022

Charles University
2017-2022

European Molecular Biology Laboratory
2021-2022

European Molecular Biology Laboratory
2018-2020

Abstract The coronavirus SARS-CoV-2 is the cause of ongoing COVID-19 pandemic. Therapeutic neutralizing antibodies constitute a key short-to-medium term approach to tackle COVID-19. However, traditional antibody production hampered by long development times and costly production. Here, we report rapid isolation characterization nanobodies from synthetic library, known as sybodies (Sb), that target receptor-binding domain (RBD) spike protein. Several binders with low nanomolar affinities...

10.1038/s41467-020-19204-y article EN cc-by Nature Communications 2020-11-04

<title>Abstract</title> Protein complexes are central to all cellular processes and their regulation. Here, we introduce the meltome-assisted profiling of protein (MAP-X) that maps complexome through thermal proteome in native environment. Applied across blood stages malaria parasite P. falciparum, MAP-X resolved conserved complexes, reproduced previously identified interactions found new associations. Among those, discovered missing subunits RNA exosome reconstructed its structure, further...

10.21203/rs.3.rs-5659511/v1 preprint EN Research Square (Research Square) 2025-04-08

The inner membrane complex (IMC) is a defining feature of apicomplexan parasites, which confers stability and shape to the cell, functions as scaffolding compartment during formation daughter cells plays an important role in motility invasion different life cycle stages these single-celled organisms. To explore IMC proteome malaria parasite Plasmodium falciparum we applied proximity-dependent biotin identification (BioID)-based proteomics approach, using established marker protein...

10.1111/cmi.13341 article EN Cellular Microbiology 2021-04-08

Abstract The coronavirus SARS-CoV-2 is the cause of ongoing COVID-19 pandemic. Therapeutic neutralizing antibodies constitute a key short-to-medium term approach to tackle COVID-19. However, traditional antibody production hampered by long development times and costly production. Here, we report rapid isolation characterization nanobodies from synthetic library, known as sybodies (Sb), that target receptor-binding domain (RBD) spike protein. Several binders with low nanomolar affinities...

10.1101/2020.06.23.165415 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2020-06-23

Abstract Signaling by the human C-type lectin-like receptor, natural killer (NK) cell inhibitory receptor NKR-P1, has a critical role in many immune-related diseases and cancer. receptors have weak affinities to their ligands; therefore, setting up comprehensive model of NKR-P1-LLT1 interactions that considers state on surface is necessary understand its functions. Here we report crystal structures NKR-P1 NKR-P1:LLT1 complexes, which provides evidence forms homodimers an unexpected...

10.1038/s41467-022-32577-6 article EN cc-by Nature Communications 2022-08-26

Abstract Gliding, a type of motility based on an actin-myosin motor, is specific to apicomplexan parasites. Myosin A binds two light chains which further interact with glideosome associated proteins and assemble into the glideosome. The role individual unclear due lack structures larger assemblies. Here, we investigate essential (ELCs) in Toxoplasma gondii Plasmodium falciparum present their crystal as part trimeric sub-complexes. We show that although ELCs bind conserved MyoA sequence, P....

10.1038/s42003-020-01283-8 article EN cc-by Communications Biology 2020-10-13

NKp30 is one of the main human natural killer (NK) cell activating receptors used in directed immunotherapy. The oligomerization ligand binding domain depends on length C-terminal stalk region, but our structural knowledge and its role signal transduction remains limited. Moreover, affected by presence type N-glycosylation. In this study, we assessed whether Our results show that forms oligomers when expressed HEK293S GnTI− lines with simple N-glycans. However, was detected only as monomers...

10.3390/cancers12071998 article EN Cancers 2020-07-21

Abstract Apicomplexan parasites, such as Plasmodium falciparum and Toxoplasma gondii , traverse the host tissues invade cells exhibiting a specific type of motility called gliding. The molecular mechanism gliding lies in actin-myosin motor localized to intermembrane space between plasma membrane inner complex (IMC) parasites. Myosin A (MyoA) is part glideosome, large multi-protein complex, which anchored outer IMC. MyoA bound proximal essential light chain (ELC) distal myosin (MLC1), further...

10.1101/867499 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2019-12-06

Peptidyl-prolyl isomerases (PPIases) catalyze intrinsically slow and often rate-limiting isomerization of prolyl-peptide bonds in unfolded or partially folded proteins, thereby speeding up the folding process preventing misfolding. They possess binding chaperone domains addition to domain carrying activity. Although generally, their substrates display no identity amino acid sequence upstream downstream proline with 20 possibilities for each residue, PPIases are efficient enzymes. SlyD is a...

10.1007/s00018-022-04179-4 article EN cc-by Cellular and Molecular Life Sciences 2022-02-19

As the decline of malaria cases stalled over last five years, novel targets in Plasmodium falciparum are necessary for development new drugs. Glycogen Synthase Kinase (PfGSK3) has been identified as a potential target, since its selective inhibitors were shown to disrupt parasitès life cycle. In uncanonical N-terminal region parasite enzyme, we several autophosphorylation sites and probed their role activity regulation PfGSK3. By combining molecular modeling with experimental small-angle...

10.1042/bcj20210829 article EN cc-by Biochemical Journal 2022-01-13

Malaria is responsible for hundreds of thousands deaths every year. The lack an effective vaccine and the global spread multidrug resistant parasites hampers fight against disease underlines need new antimalarial drugs. Central to pathogenesis malaria proliferation Plasmodium within human erythrocytes. Parasites invade erythrocytes via a coordinated sequence receptor-ligand interactions between parasite host cell. Posttranslational modifications such as protein phosphorylation are known be...

10.1016/j.jbc.2022.102360 article EN cc-by Journal of Biological Chemistry 2022-08-10

ABSTRACT The inner membrane complex (IMC) is a defining feature of apicomplexan parasites, which confers stability and shape to the cell, functions as scaffolding compartment during formation daughter cells plays an important role in motility invasion different life cycle stages these single celled organisms. To explore IMC proteome malaria parasite Plasmodium falciparum we applied proximity-dependent biotin identification (BioID)-based proteomics approach, using established marker protein...

10.1101/2021.02.03.428885 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-02-03

Abstract Human NKR-P1 (CD161, KLRB1 ) and its ligand LLT1 ( CLEC2D are a prototypical inhibitory C-type lectin-like receptor:ligand pair of NK cells with critical role in homing lymphocytes to immune-privileged sites, particularly multiple sclerosis, rheumatoid arthritis, Crohn’s disease. Furthermore, NKR-P1:LLT1 signaling is associated glioblastoma, non-Hodgkin’s lymphoma, breast, prostate cancer. However, the lack structural data on formation complex limits our understanding this...

10.1101/2021.06.16.448687 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-06-16

Natural killer (NK) cells are a type of lymphocytes able to kill tumour and virally infected cells.Human NKR-P1 is one the plenty receptors anchored in membrane cell LLT1 its ligand on partner cell.Both have extracellular part with C-type lectin like fold.The domains been expressed characterised.1,2The crystal structures oligomers published3 NKR-P1:LLT1 deposited.We discovered that form chain structure complex.In order study interaction solution, we performed small angle X-ray scattering...

10.1107/s2053273319094944 article EN Acta Crystallographica Section A Foundations and Advances 2019-08-18
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