Viral and Microbial Proteins | Iva Pichová Group

About our group

The research of our laboratory focuses mainly on functional and structural studies of key proteins from Hepatitis B virus and Mycobacteria spp and their interactions with cellular proteins. We also study proteins from pathogenic yeasts and cooperate with chemical ecologists on insect pheromone biosynthetic enzymes.

Research projects involve protein engineering, protein purification, protein characterization, enzymology, NMR and X-ray protein structure solution, isolation and analysis of complexes of cellular and pathogenic proteins, various molecular biological methods, and electron microscopy analysis. Our close cooperation with organic chemists facilitates multidisciplinary research focused on identification and characterization of enzymes involved in drug metabolism and testing of potential inhibitors.

The group is a member of the Gilead Sciences & IOCB Research Centre, NPU 1 and OPVVV projects.

News

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2 December 2019

New Ph.D. students

28 November 2019

Dája placed third in high school student competition

Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p from <i>Candida parapsilosis</i>

Structural determinants for subnanomolar inhibition of the secreted aspartic protease Sapp1p from Candida parapsilosis

J. Dostál J. Brynda L. Vaňková S. R. Zia O. Heidingsfeld M. Lepšík

Journal of Enzyme Inhibition and Medicinal Chemistry 36 (1): 914-921 (2021)

Pathogenic Candida albicans yeasts frequently cause infections in hospitals. Antifungal drugs lose effectiveness due to other Candida species and resistance. New medications are thus required. Secreted aspartic protease of C. parapsilosis (Sapp1p) is a promising target. We have thus solved the crystal structures of Sapp1p complexed to four peptidomimetic inhibitors. Three potent inhibitors (K_i: 0.1, 0.4, 6.6 nM) resembled pepstatin A (K_i: 0.3 nM), a general aspartic protease inhibitor, in terms of their interactions with Sapp1p. However, the weaker inhibitor (Ki: 14.6 nM) formed fewer nonpolar contacts with Sapp1p, similarly to the smaller HIV protease inhibitor ritonavir (K_i: 1.9 µM), which, moreover, formed fewer H-bonds. The analyses have revealed the structural determinants of the subnanomolar inhibition of C. parapsilosis aspartic protease. Because of the high similarity between Saps from different Candida species, these results can further be used for the design of potent and…

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Desaturase specificity is controlled by the physicochemical properties of a single amino acid residue in the substrate binding tunnel

A. Buček M. Vazdar M. Tupec A. Svatoš I. Pichová

Computational and Structural Biotechnology Journal 18: 1202-1209 (2020)

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Hepatitis B Core Protein Is Post-Translationally Modified through K29-Linked Ubiquitination