姓名：Andrey ZAVIALOV (Zaviyalov)

邮箱：hy0322025@hainmc.edu.cn

教育经历：

1999年2月，俄罗斯门捷列夫化工大学，工业生物技术，硕士

2005年4月，乌普萨拉大学，分子生物学，博士

工作经历：

2022年—至今，mg4355线路检测官网，衰老与肿瘤国际研究中心，PI

2017年-2022年，广州医科大学附属广州市妇女儿童医疗中心，儿科研究所，PI

2011年-2016年，芬兰图尔库大学，生物技术中心，研究员

2010年-2012年，夏威夷大学马诺阿分校John A. Burns医学院，公共卫生，青年教师

研究内容：

1. 腺苷脱氨酶2(ADA2)在免疫和癌症中的作用及其潜在的治疗应用

Name: Andrey ZAVIALOV (Zaviyalov)

Email: hy0322025@hainmc.edu.cn

Education background:

02/1999, D.I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia, Industrial Biotechnology

, M.S.

04/2005, Uppsala University, Uppsala, Sweden (Top 100 Universities), Molecular Biology, Ph.D.

Work experience:

2022-present  Principal Investigator, International Center for Aging and Cancer, Hainan Medical University, Haikou,   (China)

2017-2022       Principal Investigator, Guangzhou Institute of Pediatrics, Guangzhou Women and Children’s Medical Center (China). Professor, Guangzhou Medical University http://www.gzfezx.com/a/202001/2587440.html

2016            Consultant: Halozyme Therapeutics (San Diego, USA)

2011-2016       Academy of Finland Research Fellow (group leader), Centre for Biotechnology, University of Turku (Finland)

2010-2012       Junior Faculty, Department of Public Health, John A. Burns School of Medicine, the University of Hawaii at Manoa (U.S.A.)             

2009-2010       Research scientist, Singapore Immunology Network (SIgN), A*-STAR research company (Singapore)

2005-2009       EMBO and HFSP Postdoctoral Fellow, INSERM U924, IPMC, Université de Nice-Sophia Antipolis (France)

1999-2005       Ph.D. student, Department of Cell and Molecular Biology.  Uppsala University (Sweden)

Honors:

2022-present   Associate editor. Frontiers in Pharmacology

2021                National High-end Foreign Expert award, China

2018-present   Scientific advisor. DADA2 foundation, USA

2011-2016         Research Fellow of the Finnish Academy of Science.

2009                Selected for the ATIP CNRS grant, France

2006-2009          Awarded Human Frontiers of Science Program (HFSP) long-term fellowship

2006                Awarded the EMBO long-term fellowship

2005         Selected for the Damon Runyon Cancer Research long-term Fellowships (USA, Harvard University),    declined

2005               Selected for the Cancer Research Institute long-term Fellowships (USA, Harvard University), declined

2003                Harold M. Weintraub graduate student Award (Fred Hutchinson Cancer Research Center,                             Seattle, USA). Top 15 Ph.D. students in Biosciences from North America and Europe.

1999                Top student at D.I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia

A. Brief description of current research

Adenosine is vital in regulating immune responses. Adenosine accumulates at inflammation and tumor growth sites and binds to adenosine receptors expressed by immune cells in response to activation signals. However, the role of adenosine deaminases, which decrease the local concentration of adenosine, still needs to be determined. Moreover, it remains puzzling why humans possess two enzymes, ADA1 and ADA2, with adenosine deaminase activity. ADA1 is primarily an intracellular enzyme that breaks down adenosine and reduces the concentration of the toxic adenosine derivatives in the cells. It has been found that mutations in the ADA1 gene lead to a severe combined immunodeficiency that is characterized by decreased antibody production and lower numbers of T and B cells. In contrast to ADA1, ADA2 is a secreted protein expressed mainly by cells of the myeloid lineage, such as macrophages and dendritic cells. Clinical studies have shown that the levels of ADAs in biological fluids are altered in pathophysiological conditions, suggesting that ADA activity could be a convenient marker for diagnosing immune diseases such as tuberculosis and oral cancer. We have identified the gene encoding ADA2 and shown that it belongs to a new adenosine deaminase growth factors (ADGFs) family. Furthermore, the crystal structure of ADA2 reveals it to be a dimer with two chemokine-like domains that could potentially bind a putative ADA2 receptor. In 2014, patients with mutations in the gene encoding ADA2 (DADA2 patients) were identified. These patients display health problems, such as early onset systemic inflammation, ischemic strokes, panlymphopenia, and hypogammaglobinemia. Recently, we found that ADA2 is a DNA-binding lysosomal protein that controls the activation of Toll-like receptor 9 in response to DNA in plasmacytoid cells and M1/M2 polarization of macrophages. My project aims to further shed light on the function of ADA2, the enzyme currently thought to be a drug candidate to combat solid tumors, and find its clinical applications.

Selected publications:

1. *Zavialov, A.V., Buckingham, R.H., and Ehrenberg, M. (2001). A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell 107, 115-124. IF=64.5 (271)

2. *Zavialov, A.V., Mora, L., Buckingham, R.H., and Ehrenberg, M. (2002). Release of Peptide Promoted by the GGQ-Motif of Class 1 Release Factors Regulates the GTPase Activity of RF3. Molecular Cell 10, 789-798 IF=16 (250)

3. #Rawat, U.B.S., #Zavialov, A.V., Sengupta, J., Valle, M., Grassucci, R.A., Linde, J., Vestergaard, B., Ehrenberg, M. and Frank, J (2003) A cryo-electron microscopic study of ribosome-bound termination factor RF2. Nature 421,87-90. IF=64.8 (294)

4. Klaholz, B.P., Pape, T., Zavialov, A.V., Myasnikov, A.G., Orlova, E.V., Vestergaard, B., Ehrenberg, M. and van Heel, M. (2003) Structure of the E. coli ribosomal termination complex with release factor 2. Nature 421, 90-94. IF=64.8 (249)

5. Pedersen, K., Zavialov, A., Pavlov, M., Elf, K., Gerdes, K. and Ehrenberg, M. (2003). The bacterial toxin RelE displays codon specific cleavage of mRNAs in the ribosomal A-site. Cell. 112, 131-140. IF=64.5 (626)

6. *Zavialov, A., and Ehrenberg, M. (2003) Peptidyl-tRNA regulates the GTPase activity of bacterial translation factors. Cell, 113, 113-22. IF=64.5 (166)

7. Valle, M., Zavialov, A., Sengupta, J., Rawat, U., Ehrenberg, M., and Frank, J. (2003) Locking and unlocking of ribosomal motions. Cell, 113, 123-34. IF=64.5 (694)

8. Valle, M., Zavialov, A., Li, W., Stagg, S., Sengupta, J., Nielsen, R., Nissen, P., Harvey, S., Ehrenberg, M., and Frank, J. (2003). Incorporation of Aminoacyl-tRNA into the Ribosome as Seen by Cryo-EM. Nat. Struct. Biol. 10, 899-906. IF=16.8 (424)

9. Mora, L., Zavialov, A., Ehrenberg, M., and Buckingham, R. (2003). Stop codon recognition and interactions with peptide release factor RF3 of RF1/RF2 chimers from Escherichia coli. Mol. Microbiol., 50, 1467-76 IF=3.6 (64)

10. Frank, J., Sengupta, J., Gao, H., Li, W., Valle, M., Zavialov, A., and Ehrenberg, M. (2005). The role of tRNA as a molecular spring in decoding, accommodation, and peptidyl transfer. FEBS Lett 579, 959-962. IF=3.5 (123)

11. *Zavialov, A. V., Hauryliuk, V. V., and Ehrenberg, M. (2005). Guanine nucleotide exchange on ribosome bound elongation factor EF-G initiates translocation of tRNAs. Journal of Biology (now BMC Biology) 4, 9. IF=5.4 (84)

12. Gao, N., Zavialov, A. V., Li, W., Sengupta, J., Valle, M., Gursky, R. P., Ehrenberg, M., and Frank, J. (2005). Mechanism for the Disassembly of the Post-termination Complex Inferred from Cryo-EM studies. Mol. Cell 18, 663-674.  IF=16 (144)

13. Allen, G. S., Zavialov, A., Gursky, R., Ehrenberg, M., and Frank, J. (2005). The Solution Structure of a Translation Initiation Complex from Escherichia coli at 13.8 Å. Cell  121, 703-12 IF=64.5 (331)

14. Zavialov, A. V., Hauryliuk, V. V., and Ehrenberg, M. (2005). Splitting of the post-termination ribosome into subunits by the concerted action of RRF and EF-G. Mol. Cell 18, 675-686. IF=16 (169)

15. *Zavialov, A. V., and Engström, Å. (2005). Human ADA2 belongs to a new family of growth factors with adenosine deaminase activity. Biochemical J 391, 51-57. IF=4.1 (222)