Vaheh has more than 25 years of experience in protein crystallography as a major expertise, including the last nine years in industry settings.
Early in his education, Vaheh knew he wanted to pursue a career that combined his interests in both physics and biology. This led him to Moscow’s Russian Academy of Sciences where he received his PhD in protein crystallography working in the laboratory of Boris Weinstein, and then to the Max Planck Institute for Biochemistry for postdoctoral work in the laboratory of Nobel Laureate Robert Huber. Later, his work at the Oklahoma Medical Research Foundation and then the Berkeley Structural Genomics Center enabled investigations into the X-ray structure determination of proteins from minimal organisms, Mycoplasma genitalium and Mycoplasma pneumonia; and the purification, crystallization, and structure determination of protein and protein complexes from human and bovine blood.
Vaheh came to MedImmune in 2006 to help build and develop its program in protein crystallography, including using it as a tool for understanding how and why a drug works. In his current role as a Senior Scientist in the department of Antibody Discovery and Protein Engineering, Vaheh is involved in multiple crystallography projects that cross all therapeutic areas of the organization.
A day in the life
Crystals and Structure of a Human IgG Fc Variant (AEFC-202, 2009); Crystals and Structure of a Human IgG Fc Variant with Enhanced FcRn (AEFC-110, 2010)
Oklahoma Medical Research Foundation: Purification and crystallization of proteins and protein complexes from human and bovine blood and their structure determination
Lawrence Berkeley National Laboratory: X-ray structure determination of proteins from minimal organisms, Mycoplasma genitalium and Mycoplasma pneumoniae
Structural insights into neonatal Fc receptor-based recycling mechanisms
Oganesyan V, Damschroder MM, Cook KE, Li Q, Gao C, Wu H, Dall'Acqua WF. J Biol Chem. 2014 Mar 14;289(11):7812-24. doi: 10.1074/jbc.M113.537563. Epub 2014 Jan 27.
Mechanisms of neutralization of a human anti-α-toxin antibody
Oganesyan V, Peng L, Damschroder MM, Cheng L, Sadowska A, Tkaczyk C, Sellman BR, Wu H, Dall'Acqua WF. J Biol Chem. 2014 Oct 24;289(43):29874-80. doi: 10.1074/jbc.M114.601328. Epub 2014 Sep 10.
pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling
Borrok MJ, Wu Y, Beyaz N, Yu XQ, Oganesyan V, Dall'Acqua WF, Tsui P. J Biol Chem. 2015 Feb 13;290(7):4282-90. doi: 10.1074/jbc.M114.603712. Epub 2014 Dec 23.
Molecular basis for antagonistic activity of anifrolumab, an anti-interferon-α receptor 1 antibody
Peng L, Oganesyan V, Wu H, Dall'Acqua WF, Damschroder MM. MAbs. 2015;7(2):428-39. doi:10.1080/19420862.2015.1007810.
Improving target cell specificity using a novel monovalent bispecific IgG design
Mazor Y, Oganesyan V, Yang C, Hansen A, Wang J, Liu H, Sachsenmeier K, Carlson M, Gadre DV, Borrok MJ, Yu XQ, Dall'Acqua W, Wu H, Chowdhury PS. MAbs. 2015;7(2):377-89. doi: 10.1080/19420862.2015.1007816.
Structural Insights into the Neutralization Properties of the Fully Human, Anti-interferon Monoclonal Antibody Sifalimumab
Oganesyan V, Peng L, Woods RM, Wu H, Dall'Acqua WF. J Biol Chem. 2015 Jun 12;290(24):14979-85. doi: 10.1074/jbc.M115.652156. Epub 2015 Apr 29.
Fibronectin type III domains engineered to bind CD40L: cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of two complexes.
Oganesyan V, Ferguson A, Grinberg L, Wang L, Phipps S, Chacko B, Drabic S, Thisted T, Baca M. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):1045-8. doi: 10.1107/S1744309113022847.
Crystallization and Preliminary X-ray Diffraction Analysis of the Complex Between a Human Anti-Alpha Toxin Antibody Fragment and Alpha Toxin
Vaheh Oganesyan, Arnita Barnes, Christine Tkaczyk, Andrew Ferguson, Herren Wu, William F. Dall’Acqua. Acta Crystallogr Sect F Struct Biol Cryst Comm, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):302-5. doi: 10.1107/S1744309113002881. Epub 2013 Feb 23.
Structural and functional characterization of an agonistic anti-human EphA2 monoclonal antibody
Peng L, Oganesyan V, Damschroder MM, Wu H, Dall'Acqua WF. J. Mol. Biol. 2011 Oct 21; 413(2):390-405. Epub 2011 Aug 16.
Crystallization and preliminary X-ray diffraction analysis of the complex of a human anti-ephrin type-A receptor 2 antibody fragment and its cognate antigen.
Oganesyan V, Damschroder MM, Phipps S, Wilson SD, Cook KE, Wu H, Dall'Acqua WF. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):730-3. Epub 2010 May 29.
Structural characterization of a human Fc fragment engineered for extended serum half-life
Oganesyan V, Damschroder MM, Woods RM, Cook KE, Wu H, Dall'acqua WF. Mol Immunol. 2009 May;46(8-9):1750-5. Epub 2009 Feb 27.
Crystallization and preliminary X-ray diffraction analysis of the complex between a human anti-interferon antibody fragment and human interferon alpha-2A
Oganesyan V, Damschroder MM, Cook KE, Wu H, Dall'Acqua WF. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jan 1;65(Pt 1):14-6. Epub 2008 Dec 25.
Structural Characterization of a Human Fc Fragment Engineered for Lack of Effector Functions
Vaheh Oganesyan, Changshou Gao, Lena Shirinian, Herren Wu1, William F. Dall’Acqua. Acta Cryst., Section D: Biological Crystallography, 2008, v. D64, p. 700-4.
Structural characterization of a mutated, ADCC-enhanced human Fc fragment
Oganesyan V, Damschroder MM, Leach W, Wu H, Dall'acqua WF. Mol Immunol. 2008 Apr; 45(7):1872-82.
Structural Genomics of Minimal Organism and Protein Fold Space
Sung-Hou Kim, Dong Hae Shin, Jinyu Liu, Vaheh Oganesyan, Shengfeng Chen, Qian Steven Xu, Jeong-Sun Kim, Debanu Das, Ursula Schulze-Gahmen, Stephen R. Holbrook, Elizabeth L. Holbrook, Bruno A. Martinez, Natalia Oganesyan, Andy DeGiovanni, Yun Lou, Marlene Henriquez, Candice Huang, Jaru Jancarik, Ramona Pufan, In-Geol Choi, John-Marc Chandonia, Jingtong Hou, Barbara Gold, Hisao Yokota, Steven E. Brenner, Paul D. Adams and Rosalind Kim. Journal of Structural and Functional Genomics (2005), vol. 6, ##2-3, 63-70.
Crystal structure of the probable novel fold phosphodiesterase from Aquifex aeolicus at resolution 2.0Å
Vaheh Oganesyan, Paul D. Adams, Jaru Jancarik, Hisao A. Yokota, Rosalind Kim and Sung-Hou Kim. Acta Cryst. (2007) F63 May 1; 63(Pt 5):369-74.
Crystal structure of the probable inorganic polyphosphate/ATP-NAD kinase from Thermotoga maritima at resolution 2.3Å
Vaheh Oganesyan, Candice Huang, Paul D. Adams, Jaru Jancarik, Hisao A. Yokota, Rosalind Kim and Sung-Hou Kim. Acta Cryst. (2005). F61, 640-646.
Crystal structure of the “PhoU-like” phosphate uptake regulator from Aquifex aeolicus
Vaheh Oganesyan, Natalia Oganesyan, Paul D. Adams, Jaru Jancarik, Hisao A. Yokota, Rosalind Kim and Sung-Hou Kim. C J Bacteriol. 2005 Jun; 187(12):4238-44.
Structure of the putative DNA-binding protein SP_1288 from Streptococcus pyogenes
Oganesyan V, Pufan R, DeGiovanni A, Yokota H, Kim R, Kim SH. Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1266-71.
Structure of the hypothetical protein AQ_1354 from Aquifex aeolicus
Oganesyan V, Busso D, Brandsen J, Chen S, Jancarik J, Kim R, Kim SH. Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1219-23.
The crystal structure of the endothelial protein C receptor and a bound phospholipid
Oganesyan V, Oganesyan N, Terzyan S, Qu D, Dauter Z, Esmon NL, Esmon CT. J Biol Chem. 2002 Jul 12;277(28):24851-4.
Modulation of redox potential in electron transfer proteins: effects of complex formation on the active site microenvironment of cytochrome b5
Wirtz M, Oganesyan V, Zhang X, Studer J, Rivera M. Faraday Discuss. 2000;(116):221-34; discussion 257-68.
Three-dimensional structures of mutant forms of E. coli inorganic pyrophosphatase with Asp-->Asn single substitution in positions 42, 65, 70, and 97
Avaeva SM, Rodina EV, Vorobyeva NN, Kurilova SA, Nazarova TI, Sklyankina VA, Oganesyan VY, Samygina VR, Harutyunyan EH. Biochemistry (Mosc). 1998 Jun;63(6):671-84.
Changes I n E. coli inorganic pyrophosphatase structure induced by binding of metal activators
Avaeva SM, Rodina EV, Vorobyeva NN, Kurilova SA, Nazarova TI, Sklyankina VA, Oganesyan VY, Harutyunyan EH. Biochemistry (Mosc). 1998 May;63(5):592-9.
Crystal structure of Escherichia coli inorganic pyrophosphatase complexed with SO4(2-). Ligand-induced molecular asymmetry
Avaeva S, Kurilova S, Nazarova T, Rodina E, Vorobyeva N, Sklyankina V, Grigorjeva O, Harutyunyan E, Oganesyan V, Wilson K, Dauter Z, Huber R, Mather T. FEBS Lett. 1997 Jun 30;410(2-3):502-8.
Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis
Harutyunyan EH, Oganesyan VY, Oganessyan NN, Avaeva SM, Nazarova TI, Vorobyeva NN, Kurilova SA, Huber R, Mather T. iochemistry. 1997 Jun 24;36(25):7754-60.
The 2.8 A crystal structure of Gla-domainless activated protein C
Mather T, Oganesyan V, Hof P, Huber R, Foundling S, Esmon C, Bode W. EMBO J. 1996 Dec 16;15(24):6822-31.
Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor
Bergner A, Oganesyan V, Muta T, Iwanaga S, Typke D, Huber R, Bode W. EMBO J. 1996 Dec 16;15(24):6789-97.
Escherichia coli inorganic pyrophosphatase: site-directed mutagenesis of the metal binding sites
Avaeva S, Ignatov P, Kurilova S, Nazarova T, Rodina E, Vorobyeva N, Oganesyan V, Harutyunyan E. FEBS Lett. 1996 Dec 9;399(1-2):99-102.
Mg2+ activation of Escherichia coli inorganic pyrophosphatase
Avaeva SM, Rodina EV, Kurilova SA, Nazarova TI, Vorobyeva NN, Harutyunyan EH, Oganesyan VYu.FEBS Lett. 1995 Dec 11;377(1):44-6.
X-ray crystallographic studies of recombinant inorganic pyrophosphatase from Escherichia coli
Oganesyan V, YuKurilova SA, Vorobyeva NN, Nazarova TI, Popov AN, Lebedev AA, Avaeva SM, Harutyunyan EH. FEBS Lett. 1994 Jul 18;348(3):301-4.
Awards and honors
MedImmune Directors Award, 2011 (successful structure determination of complex formed between anti EphA2 monoclonal antibody Fab fragment and EphA2 receptor)
Outstanding Performance Award; Lawrence Berkeley National Laboratory
Shubnikov Award; Moscow Institute of Crystallography, 1996 (detailed characterization of the action mechanism of E. coli inorganic pyrophosphatase)
Crystallography is both art and science, and the amazing result allows us to get a much closer look at how a drug works. It’s an important element toward our mission, which is ultimately achievable through science and scientific excellence.
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