Yorgo Modis

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Yorgo Modis
Yorgo Modis.jpg
Yorgo Modis in 2016
Born
Yorgo Eugene Modis

1974 (age 48–49)
Geneva, Switzerland
Nationality Switzerland-United States-Greece
Alma mater International School of Geneva (IB)
University of Cambridge (BA, MA)
European Molecular Biology Laboratory, Heidelberg (PhD)
Scientific career
Fields Biochemistry
Structural Biology
Institutions European Molecular Biology Laboratory, Heidelberg
Harvard Medical School
Yale University
MRC Laboratory of Molecular Biology, University of Cambridge
Academic advisorsRik A. Wierenga
Stephen C. Harrison
Website www.mrc-lmb.cam.ac.uk/ymodis/

Yorgo E. Modis (born 1974) is Professor in Virology and Immunology, and a Wellcome Trust Senior Research Fellow at the Department of Medicine, University of Cambridge. [1] He is head of The Modis Lab in the Molecular Immunity Unit at the MRC Laboratory of Molecular Biology. He studies cellular mechanisms of viral gene sensing and silencing. His group employs a diverse set of complementary biophysical approaches including cryo-electron microscopy (cryoEM), X-ray crystallography, solution biophysics, fluorescence microscopy and cell biological approaches to understand the cellular mechanisms of viral gene sensing and silencing in molecular-level detail.

Contents

Education and early life

Modis received his International Baccalaureate from the International School of Geneva, Switzerland. He then studied Biochemistry at the University of Cambridge. He did his graduate work in Structural Biology with Rik A. Wierenga at the European Molecular Biology Laboratory Heidelberg obtaining his Ph.D. from the University of Leeds in 1999. For the next six years he worked as a Postdoctoral Fellow with Stephen C. Harrison at Harvard Medical School, Boston, U.S.A.

Research and professional experience

While at Harvard (1999–2005) Modis co-authored five publications that featured on the cover of international scientific journals. [2] [3] [4] [5] Among them was the subject of viral entry into host cells by the dengue virus, which became a cover story on Nature (journal). [6] The work gave rise to an award-winning animation Dengue Viral Fusion.
At Yale Modis was first Assistant Professor (2005–2010) and then Associate Professor (2010–2014) of Molecular Biophysics & Biochemistry. In those capacities he carried out research that led to numerous publications on which he was corresponding author and/or principal investigator. [7] [8] [9] [10] [11] [12] [13] [14] [15] [16] [17]
In 2014 Modis accepted a position as Wellcome Trust Senior Research Fellow at University of Cambridge. He became the head of research group The Modis Lab at MRC Laboratory of Molecular Biology. Two years later he was named University Reader in Virology and Immunology. In 2021 he was named Professor in Virology and Immunology.
In these capacities Modis has co-authored a number of publications as principal investigator. [18] [19] [20] [21] [22] [23] [24]
A full list of his publications (around 70) can be found here.
He has also been invited to, organized, or served as keynote speaker in over 100 seminars and conferences.
In May 2020 he helped Roger Highfield to set up a blog at the Science Museum Group with the theme Coronavirus: How the Virus Works.
In July 2020 he contributed graphics of the COVID-19 virus to the BBC News article by John Sudworth with title Wuhan: City of silence — Looking for answers in the place where coronavirus started.

Honors and awards

2019 Senior Research Fellowship from the Wellcome Trust 2014 Senior Research Fellowship from the Wellcome Trust 2009 CINE Golden Eagle Award for the animation “Dengue Virus Visualization” on Teachers’ Domain  2008 Nominated for the 2009 American Crystallography Association Margaret C. Etter Early Career Award (the award went to Dr. Svilen Bobev) 2007 Investigator in the Pathogenesis of Infectious Disease, Burroughs Wellcome Fund 2007 Anderson Endowed Bridge Fellowship Award, Yale University 2006 Anderson Endowed Fellowship Award, Yale University 2000-2004 Human Frontier Science Program Organization Long-Term Postdoctoral Fellowship 1999-2000 European Molecular Biology Organization Long-Term Fellowship 1999 Roche Foundation Postdoctoral Fellowship (declined) 1999 Swiss National Science Foundation Fellowship (declined) 1995-1999 Predoctoral Fellowship, European Molecular Biology Laboratory (4 years) 1995 Bateman Scholarship- First Class Honors Degree, Trinity Hall, University of Cambridge, U.K. 1995 Kareen Thorne Prize- Top First Class Honors Degree in Biological Sciences, Trinity Hall, University of Cambridge, U.K. 1995 First Class Honours (top grade) Bachelor of Arts degree in biochemistry, University of Cambridge, U.K. 1992 Top grade (7) in all six subjects of the International Baccalaureate at the International School of Geneva, Switzerland

Personal life

Modis is the son of Theodore Modis and Carole Gene Modis. He is the great-grandson of Theodoros Modis [25] [26] and grandnephew of Georgios Modis.

Related Research Articles

<span class="mw-page-title-main">Hepatitis C virus</span> Species of virus

The hepatitis C virus (HCV) is a small, enveloped, positive-sense single-stranded RNA virus of the family Flaviviridae. The hepatitis C virus is the cause of hepatitis C and some cancers such as liver cancer and lymphomas in humans.

<i>Dengue virus</i> Species of virus

Dengue virus (DENV) is the cause of dengue fever. It is a mosquito-borne, single positive-stranded RNA virus of the family Flaviviridae; genus Flavivirus. Four serotypes of the virus have been found, a reported fifth has yet to be confirmed, all of which can cause the full spectrum of disease. Nevertheless, scientists' understanding of dengue virus may be simplistic as, rather than distinct antigenic groups, a continuum appears to exist. This same study identified 47 strains of dengue virus. Additionally, coinfection with and lack of rapid tests for Zika virus and chikungunya complicate matters in real-world infections.

<span class="mw-page-title-main">Rubella virus</span> Species of virus

Rubella virus (RuV) is the pathogenic agent of the disease rubella, transmitted only between humans via the respiratory route, and is the main cause of congenital rubella syndrome when infection occurs during the first weeks of pregnancy.

<span class="mw-page-title-main">Viral protein</span>

A viral protein is both a component and a product of a virus. Viral proteins are grouped according to their functions, and groups of viral proteins include structural proteins, nonstructural proteins, regulatory proteins, and accessory proteins. Viruses are non-living and do not have the means to reproduce on their own, instead depending on their host cell's resources in order to reproduce. Thus, viruses do not code for many of their own viral proteins, and instead use the host cell's machinery to produce the viral proteins they require for replication.

VPg is a protein that is covalently attached to the 5′ end of positive strand viral RNA and acts as a primer during RNA synthesis in a variety of virus families including Picornaviridae, Potyviridae and Caliciviridae. There are some studies showing that a possible VPg protein is also present in astroviridae, however, experimental evidence for this has not yet been provided and requires further study. The primer activity of VPg occurs when the protein becomes uridylated, providing a free hydroxyl that can be extended by the virally encoded RNA-dependent RNA polymerase. For some virus families, VPg also has a role in translation initiation by acting like a 5' mRNA cap.

<i>Alphavirus</i> Genus of viruses

Alphavirus is a genus of RNA viruses, the sole genus in the Togaviridae family. Alphaviruses belong to group IV of the Baltimore classification of viruses, with a positive-sense, single-stranded RNA genome. There are 32 alphaviruses, which infect various vertebrates such as humans, rodents, fish, birds, and larger mammals such as horses, as well as invertebrates. Alphaviruses that could infect both vertebrates and arthropods are referred dual-host alphaviruses, while insect-specific alphaviruses such as Eilat virus and Yada yada virus are restricted to their competent arthropod vector. Transmission between species and individuals occurs mainly via mosquitoes, making the alphaviruses a member of the collection of arboviruses – or arthropod-borne viruses. Alphavirus particles are enveloped, have a 70 nm diameter, tend to be spherical, and have a 40 nm isometric nucleocapsid.

<span class="mw-page-title-main">Envelope glycoprotein GP120</span> Glycoprotein exposed on the surface of the HIV virus

Envelope glycoprotein GP120 is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Professors Tun-Hou Lee and Myron "Max" Essex of the Harvard School of Public Health in 1988. The 120 in its name comes from its molecular weight of 120 kDa. Gp120 is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate Proteoglycan and a specific interaction with the CD4 receptor, particularly on helper T-cells. Binding to CD4 induces the start of a cascade of conformational changes in gp120 and gp41 that lead to the fusion of the viral membrane with the host cell membrane. Binding to CD4 is mainly electrostatic although there are van der Waals interactions and hydrogen bonds.

<i>Pestivirus</i> Genus of viruses

Pestivirus is a genus of viruses, in the family Flaviviridae. Viruses in the genus Pestivirus infect mammals, including members of the family Bovidae and the family Suidae. There are 11 species in this genus. Diseases associated with this genus include: hemorrhagic syndromes, abortion, and fatal mucosal disease.

Rous sarcoma virus (RSV) is a retrovirus and is the first oncovirus to have been described. It causes sarcoma in chickens.

The murine leukemia viruses are retroviruses named for their ability to cause cancer in murine (mouse) hosts. Some MLVs may infect other vertebrates. MLVs include both exogenous and endogenous viruses. Replicating MLVs have a positive sense, single-stranded RNA (ssRNA) genome that replicates through a DNA intermediate via the process of reverse transcription.

<span class="mw-page-title-main">Viral envelope</span> Outermost layer of many types of the infectious agent

A viral envelope is the outermost layer of many types of viruses. It protects the genetic material in their life cycle when traveling between host cells. Not all viruses have envelopes.

<span class="mw-page-title-main">Spike protein</span> Glycoprotein spike on a viral capsid or viral envelope

In virology, a spike protein or peplomer protein is a protein that forms a large structure known as a spike or peplomer projecting from the surface of an enveloped virus. The proteins are usually glycoproteins that form dimers or trimers.

Env is a viral gene that encodes the protein forming the viral envelope. The expression of the env gene enables retroviruses to target and attach to specific cell types, and to infiltrate the target cell membrane.

Avian sarcoma leukosis virus (ASLV) is an endogenous retrovirus that infects and can lead to cancer in chickens; experimentally it can infect other species of birds and mammals. ASLV replicates in chicken embryo fibroblasts, the cells that contribute to the formation of connective tissues. Different forms of the disease exist, including lymphoblastic, erythroblastic, and osteopetrotic.

Bovine immunodeficiency virus (BIV) is a retrovirus belonging to the genus Lentivirus. It is similar to the human immunodeficiency virus (HIV) and infects cattle. The cells primarily infected are lymphocytes and monocytes/macrophages.

<span class="mw-page-title-main">Herpesvirus glycoprotein B</span> Viral glycoprotein

Herpesvirus glycoprotein B is a viral glycoprotein that is involved in the viral cell entry of Herpes simplex virus (HSV). Herpesviruses have a lipid bilayer, called the envelope, which contains twelve surface glycoproteins. For infectivity to be attained, the double stranded DNA genome of HSV must enter the host cell through means of fusion of its envelope with the cellular membrane or via endocytosis. Other viral glycoproteins involved in the process of viral cell entry include gC, gB, gD, gH, and gL, but only gC, gB, gD, and gH are required for the fusion of the HSV's envelope with the cellular membrane. It can be noted that all herpesviruses have glycoproteins gB, gH, and gL.

Eckard Wimmer is a German American virologist, organic chemist and distinguished professor of molecular genetics and microbiology at Stony Brook University. He is best known for his seminal work on the molecular biology of poliovirus and the first chemical synthesis of a viral genome capable of infection and subsequent production of live viruses.

Hussein Naim is a Lebanese-Swiss biochemist and molecular virologist, known for his research in cell biology and virology. He has held several leading positions at prominent universities and biotechnology centers.

<span class="mw-page-title-main">Stephen C. Harrison</span> American chemist and pharmacologist

Stephen C. Harrison is professor of biological chemistry and molecular pharmacology, professor of pediatrics, and director of the Center for Molecular and Cellular Dynamics of Harvard Medical School, head of the Laboratory of Molecular Medicine at Boston Children's Hospital, and investigator of the Howard Hughes Medical Institute.

Batai orthobunyavirus (BATV) is a RNA virus belonging to order Bunyavirales, genus Orthobunyavirus.

References

  1. ↑ "Professor Yorgo Modis". September 2014.
  2. ↑ Yorgo Modis, Benes L. Trus & Stephen C. Harrison (2002). An atomic model of the papillomavirus capsid. EMBO J., 21, 4754-4762
  3. ↑ Yorgo Modis, Steven Ogata, David Clements & Stephen C. Harrison (2003). A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc. Natl. Acad. Sci. U.S.A., 100, 6986-6991
  4. ↑ Bert van den Berg, William M. Clemons Jr., Ian Collinson, Yorgo Modis, Enno Hartmann, Stephen C. Harrison & Tom A. Rapoport (2004). X-ray structure of a protein-conducting channel. Nature, 427, 36-44
  5. ↑ Yorgo Modis, Steven Ogata, David Clements & Stephen C. Harrison (2005). Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J. Virol., 79, 1223-1231
  6. ↑ Yorgo Modis, Steven Ogata, David Clements & Stephen C. Harrison (2004). Structure of the dengue virus envelope protein after membrane fusion. Nature, 427, 313-319.
  7. ↑ Ryuta Kanai, Kalipada Kar, Karen Anthony, L. Hannah Gould, Michel Ledizet, Erol Fikrig, Wayne A. Marasco, Ray A. Koski & Yorgo Modis (2006). Crystal structure of West Nile virus envelope glycoprotein reveals viral surface epitopes. J. Virol., 80, 11000-8
  8. ↑ Alvaro Arjona, Michel Ledizet, Karen Anthony, Nathalie Bonafé, Yorgo Modis, Terrence Town & Erol Fikrig (2007). West Nile virus envelope protein inhibits dsRNA-induced innate immune responses. J. Immunol., 179, 8403-9
  9. ↑ Vinod Nayak, Moshe Dessau, Kaury Kucera, Karen Anthony, Michel Ledizet & Yorgo Modis (2009). Crystal structure of dengue type 1 envelope protein in the postfusion conformation and its implication for receptor binding, membrane fusion and antibody recognition. J. Virol., 83, 4338-44.
  10. ↑ Yue Li, Ian C. Berke & Yorgo Modis (2012). DNA binding to proteolytically activated TLR9 is sequence-independent and enhanced by DNA curvature. EMBO J. 31, 919-31.
  11. ↑ Ian C. Berke & Yorgo Modis (2012). MDA5 cooperatively forms dimers and ATP-sensitive filaments upon binding double-stranded RNA. EMBO J., 31, 1714-26.
  12. ↑ Ian C. Berke, Xiong Yu, Yorgo Modis & Edward H. Egelman (2012). MDA5 assembles into a polar helical filament on double-stranded RNA. Proc. Natl. Acad. Sci. U.S.A., 109, 18437-41.
  13. ↑ Moshe Dessau, Daniel Goldhill, Robert C. McBride, Paul E. Turner & Yorgo Modis (2012). Selective pressure causes an RNA virus to trade reproductive fitness for increased structural and thermal stability of a viral enzyme. PLoS Genet., 8, e1003102.
  14. ↑ Moshe Dessau & Yorgo Modis (2013). Crystal structure of glycoprotein C from Rift Valley fever virus. Proc. Natl. Acad. Sci. U.S.A., 110, 1696-1701.
  15. ↑ Yue Li, Jimin Wang, Ryuta Kanai & Yorgo Modis (2013). Crystal structure of glycoprotein E2 from bovine viral diarrhea virus. Proc. Natl. Acad. Sci. U.S.A., 110, 6805-10.
  16. ↑ Adel M. Nour, Yue Li, Joseph Wolenski & Yorgo Modis (2013). Viral membrane fusion and nucleocapsid delivery into the cytoplasm are distinct events in some flaviviruses. PLOS Pathog., 9, e1003585.
  17. ↑ Danillo L.A. Espósito, Jennifer B. Nguyen, David C. DeWitt, Elizabeth Rhoades & Yorgo Modis (2015). Physico-chemical requirements and kinetics of membrane fusion of flavivirus-like particles. J. Gen. Virol, 96, 1702–1711.
  18. ↑ Emily V. Wong, Wenxiang Cao, Judit Vörös, Monique Merchant, Yorgo Modis, David D. Hackney, Ben Montpetit & Enrique M. De La Cruz (2016). Pi release limits the intrinsic and RNA-stimulated ATPase cycles of DEAD-box protein 5 (Dbp5). J. Mol. Biol., 428, 492-508.
  19. ↑ Chang-Min Lee, Chuan Hua He, Adel M Nour, Yang Zhou, Bing Ma, Jin Wook Park, Kyung Hee Kim, Charles Dela Cruz, Lokesh Kumar Sharma, Mahmoud L Nasr, Yorgo Modis, Chun Geun Lee & Jack A Elias (2016). IL-13Rα2 uses TMEM219 in chitinase 3-like-1-induced signaling and effector responses. Nat. Commun., 7, 12752.
  20. ↑ Shmuel Willensky, Hagit Bar-Rogovsky, Eduardo A. Bignon, Nicole D. Tischler, Yorgo Modis & Moshe Dessau (2016). Crystal structure of glycoprotein C from a hantavirus in the post-fusion conformation. PLoS Pathog., 12, e1005948.
  21. ↑ Iva A. Tchasovnikarova, Richard T. Timms, Christopher H. Douse, Rhys C. Roberts, Gordon Dougan, Robert E. Kingston, Yorgo Modis & Paul J. Lehner (2017). Hyper-activation of HUSH complex function by Charcot-Marie-Tooth disease mutation in MORC2. Nat. Genet., 9, 1035.
  22. ↑ Michael K. Fenwick, Yue Li, Stephen Almo, Peter Cresswell, Yorgo Modis & Steven E. Ealick (2017). Structural studies of viperin, an antiviral radical SAM enzyme (2017). Proc. Natl. Acad. Sci. U.S.A., 114, 6806.
  23. ↑ Christopher Sng, Sorcha O’Byrne, Daniil M. Prigozhin, Matthias R Bauer, Jenny C. Harvey, Michelle Ruhle, Ben G. Challis, Sara Lear, Lee Roberts, Sarita Workman, Tobias Janowitz, L. Magiera, Rainer Doffinger, Matthew S. Buckland, Duncan J. Jodrell, Robert K. Semple, Timothy J. Wilson, Yorgo Modis & James E. D. Thaventhiran (2018). A Type III Complement Factor D Deficiency: Structural insights for inhibition of the alternative pathway. J. Allergy Clin. Immun., 142, 311.
  24. ↑ Ming-Shih Hwang, Jérôme Boulanger, Jonathan Howe, Anna Albecka, Mathias Pasche, Leila Mureşan & Yorgo Modis (2019). Endogenous MAVS oligomers smaller than 80 nm induce mitochondrial membrane remodeling and interferon signaling. FEBS J., 286, 1543-1560. PMC6513760.
  25. ↑ "Български: Портрет на Теодорос Модис, гръцки търговец от Битоля, организатор на гръцката пропаганда в Македония, убит от дейци на ВМОРОEnglish: Theodoros Modis (Θεοδώρος Μόδης) a Greek Macedonian merchant and scholar of Monastir (Μοναστήρι Π. Γ. Δ. Μ) (Modern Bitola, Битола) Macedonia. Died: 1904".
  26. ↑ "The funeral of the Theodoros Modi in the Monastir(FYROM) IN 1904 - YouTube". YouTube .


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