Anton Zavialov
PhD, Head of Laboratory
anton.zavialov@utu.fi +358 29 450 3211 +358 50 328 6112 Arcanuminkuja 1 Turku ORCID-tunniste: https://orcid.org/orcid.org/0000-0001-6191-5931 |
Structural biology and structure-based drug design; X-ray crystallography; Cryo-electron microscopy; Microbiology and cell biology; Biochemistry; Protein chemistry; Protein engineering; Molecular chaperones; Secretion; Assembly.
Bacterial attachment, biofilm formation, and host tissue invasion. Cell-signalling mechanism of adenosine deaminase growth factor ADA2.
We work in the field of structural biology and structure-based drug design. Our main methods are x-ray crystallography and cryo-electron microscopy. The main focus of our research is the unraveling of molecular mechanisms governing the interplay between microbial pathogens and their hosts, and the exploitation of these finding in medicine. We are particularly interested in host-pathogen interactions during the early steps of infection: bacterial attachment and biofilm formation mediated by fimbrial adhesins and host tissue invasion mediated by the Type III secretion system. Blocking these steps could prevent infections caused by antibiotic-resistant pathogens. Another line of our research explores the intricate cell signaling mechanism of the novel growth factor-enzyme, adenosine deaminase type 2 (ADA2). This study paves the way for the development of novel means to treat blood cancers and vascular disorders, including a genetic disease called deficiency of ADA2 (DADA2). In addition, we develop a novel ADA-based immuno-oncological therapy of advanced cancers.
- Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin (2005)
- Molecular Microbiology
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Resolving the energy paradox of chaperone/usher-mediated fibre assembly. (2005)
- Biochemical Journal
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Mutagenesis elucidates the assembly pathway and structure of Yersinia pestis F1 polymer (2003)
- Advances in Experimental Medicine and BiologyInternational Journal of Biological Macromolecules
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the F1 antigen Caf1M-Caf1 chaperone-subunit pre-assembly complex from Yersinia pestis (2003)
- Acta crystallographica section D : structural biology
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: Preserved folding energy drives fiber formation (2003)
- Cell
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Secretion of recombinant proteins via the chaperone/usher pathway in Escherichia coli (2001) Zavialov AV, Batchikova NV, Korpela T, Petrovskaya LE, Korobko VG, Kersley J, MacIntyre S, Zav'yalov VP
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Novel fusion proteins in the analysis of diabetes-associated autoantibodies to GAD65 and IA-2 (2000) Zavialov A, Ankelo M, Westerlund-Kaplsson A, Knip M, Ilonen J, Hinkkanen A
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Structural and functional significance of the FGL sequence of the periplasmic chaperone Caf1M of Yersinia pestis (1999)
- Journal of Bacteriology
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25 (1998)
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä ) - Thiol/disulfide exchange between small heat shock protein 25 and glutathione (1998)
- Biochimica et Biophysica Acta: Protein Structure and Molecular Enzymology
(A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä )



