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Article ; Online: Viral E protein neutralizes BET protein-mediated post-entry antagonism of SARS-CoV-2.

2022 Volume 40, Issue 3, Page(s) 111088

Abstract: Inhibitors of bromodomain and extraterminal domain (BET) proteins are possible anti-severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here we show that BET proteins ... ...

Abstract	Inhibitors of bromodomain and extraterminal domain (BET) proteins are possible anti-severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here we show that BET proteins should not be inactivated therapeutically because they are critical antiviral factors at the post-entry level. Depletion of BRD3 or BRD4 in cells overexpressing ACE2 exacerbates SARS-CoV-2 infection; the same is observed when cells with endogenous ACE2 expression are treated with BET inhibitors during infection and not before. Viral replication and mortality are also enhanced in BET inhibitor-treated mice overexpressing ACE2. BET inactivation suppresses interferon production induced by SARS-CoV-2, a process phenocopied by the envelope (E) protein previously identified as a possible "histone mimetic." E protein, in an acetylated form, directly binds the second bromodomain of BRD4. Our data support a model where SARS-CoV-2 E protein evolved to antagonize interferon responses via BET protein inhibition; this neutralization should not be further enhanced with BET inhibitor treatment.
MeSH term(s)	Angiotensin-Converting Enzyme 2 ; Animals ; Antiviral Agents/pharmacology ; COVID-19 ; Interferons ; Mice ; Nuclear Proteins ; SARS-CoV-2 ; Transcription Factors ; Viral Proteins
Chemical Substances	Antiviral Agents ; Nuclear Proteins ; Transcription Factors ; Viral Proteins ; Interferons (9008-11-1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2022-06-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2022.111088
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Viral E Protein Neutralizes BET Protein-Mediated Post-Entry Antagonism of SARS-CoV-2.

bioRxiv : the preprint server for biology

2021

Abstract: Inhibitors of Bromodomain and Extra-terminal domain (BET) proteins are possible anti-SARS-CoV-2 prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here, we show that BET proteins should not be inactivated therapeutically as they ... ...

Abstract	Inhibitors of Bromodomain and Extra-terminal domain (BET) proteins are possible anti-SARS-CoV-2 prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here, we show that BET proteins should not be inactivated therapeutically as they are critical antiviral factors at the post-entry level. Knockouts of BRD3 or BRD4 in cells overexpressing ACE2 exacerbate SARS-CoV-2 infection; the same is observed when cells with endogenous ACE2 expression are treated with BET inhibitors during infection, and not before. Viral replication and mortality are also enhanced in BET inhibitor-treated mice overexpressing ACE2. BET inactivation suppresses interferon production induced by SARS-CoV-2, a process phenocopied by the envelope (E) protein previously identified as a possible "histone mimetic." E protein, in an acetylated form, directly binds the second bromodomain of BRD4. Our data support a model where SARS-CoV-2 E protein evolved to antagonize interferon responses via BET protein inhibition; this neutralization should not be further enhanced with BET inhibitor treatment.
Language	English
Publishing date	2021-11-15
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.11.14.468537
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Article ; Online: Conserved Streptococcus pneumoniae spirosomes suggest a single type of transformation pilus in competence.

Laurenceau, Raphaël / Krasteva, Petya V / Diallo, Amy / Ouarti, Sahra / Duchateau, Magalie / Malosse, Christian / Chamot-Rooke, Julia / Fronzes, Rémi

PLoS pathogens

2015 Volume 11, Issue 4, Page(s) e1004835

Abstract: The success of S. pneumoniae as a major human pathogen is largely due to its remarkable genomic plasticity, allowing efficient escape from antimicrobials action and host immune response. Natural transformation, or the active uptake and chromosomal ... ...

Abstract	The success of S. pneumoniae as a major human pathogen is largely due to its remarkable genomic plasticity, allowing efficient escape from antimicrobials action and host immune response. Natural transformation, or the active uptake and chromosomal integration of exogenous DNA during the transitory differentiated state competence, is the main mechanism for horizontal gene transfer and genomic makeover in pneumococci. Although transforming DNA has been proposed to be captured by Type 4 pili (T4P) in Gram-negative bacteria, and a competence-inducible comG operon encoding proteins homologous to T4P-biogenesis components is present in transformable Gram-positive bacteria, a prevailing hypothesis has been that S. pneumoniae assembles only short pseudopili to destabilize the cell wall for DNA entry. We recently identified a micrometer-sized T4P-like pilus on competent pneumococci, which likely serves as initial DNA receptor. A subsequent study, however, visualized a different structure--short, 'plaited' polymers--released in the medium of competent S. pneumoniae. Biochemical observation of concurrent pilin secretion led the authors to propose that the 'plaited' structures correspond to transformation pili acting as peptidoglycan drills that leave DNA entry pores upon secretion. Here we show that the 'plaited' filaments are not related to natural transformation as they are released by non-competent pneumococci, as well as by cells with disrupted pilus biogenesis components. Combining electron microscopy visualization with structural, biochemical and proteomic analyses, we further identify the 'plaited' polymers as spirosomes: macromolecular assemblies of the fermentative acetaldehyde-alcohol dehydrogenase enzyme AdhE that is well conserved in a broad range of Gram-positive and Gram-negative bacteria.
MeSH term(s)	Fimbriae, Bacterial/ultrastructure ; Gene Transfer, Horizontal ; Macromolecular Substances/ultrastructure ; Microscopy, Electron, Transmission ; Polymerase Chain Reaction ; Proteomics ; Streptococcus pneumoniae/genetics ; Streptococcus pneumoniae/ultrastructure ; Transformation, Bacterial/genetics
Chemical Substances	Macromolecular Substances
Language	English
Publishing date	2015-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1004835
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Article ; Online: Bacterial transformation: ComFA is a DNA-dependent ATPase that forms complexes with ComFC and DprA.

Diallo, Amy / Foster, Hannah R / Gromek, Katarzyna A / Perry, Thomas N / Dujeancourt, Annick / Krasteva, Petya V / Gubellini, Francesca / Falbel, Tanya G / Burton, Briana M / Fronzes, Rémi

Molecular microbiology

2017 Volume 105, Issue 5, Page(s) 741–754

Abstract: Pneumococcal natural transformation contributes to genomic plasticity, antibiotic resistance development and vaccine escape. Streptococcus pneumoniae, like many other naturally transformable species, has evolved sophisticated protein machinery for the ... ...

Abstract	Pneumococcal natural transformation contributes to genomic plasticity, antibiotic resistance development and vaccine escape. Streptococcus pneumoniae, like many other naturally transformable species, has evolved sophisticated protein machinery for the binding and uptake of DNA. Two proteins encoded by the comF operon, ComFA and ComFC, are involved in transformation but their exact molecular roles remain unknown. In this study, we provide experimental evidence that ComFA binds to single stranded DNA (ssDNA) and has ssDNA-dependent ATPase activity. We show that both ComFA and ComFC are essential for the transformation process in pneumococci. Moreover, we show that these proteins interact with each other and with other proteins involved in homologous recombination, such as DprA, thus placing the ComFA-ComFC duo at the interface between DNA uptake and DNA recombination during transformation.
Language	English
Publishing date	2017-09
Publishing country	England
Document type	Journal Article
ZDB-ID	619315-8
ISSN	1365-2958 ; 0950-382X
ISSN (online)	1365-2958
ISSN	0950-382X
DOI	10.1111/mmi.13732
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Article ; Online: Viral E Protein Neutralizes BET Protein-Mediated Post-Entry Antagonism of SARS-CoV-2

bioRxiv

Abstract	Inhibitors of Bromodomain and Extra-terminal domain (BET) proteins are possible anti-SARS-CoV-2 prophylactics as they downregulate angiotensin-converting enzyme 2 (ACE2). Here, we show that BET proteins should not be inactivated therapeutically as they are critical antiviral factors at the post-entry level. Knockouts of BRD3 or BRD4 in cells overexpressing ACE2 exacerbate SARS-CoV-2 infection; the same is observed when cells with endogenous ACE2 expression are treated with BET inhibitors during infection, and not before. Viral replication and mortality are also enhanced in BET inhibitor-treated mice overexpressing ACE2. BET inactivation suppresses interferon production induced by SARS-CoV-2, a process phenocopied by the envelope (E) protein previously identified as a possible "histone mimetic." E protein, in an acetylated form, directly binds the second bromodomain of BRD4. Our data support a model where SARS-CoV-2 E protein evolved to antagonize interferon responses via BET protein inhibition; this neutralization should not be further enhanced with BET inhibitor treatment.
Keywords	covid19
Language	English
Publishing date	2021-11-15
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.11.14.468537
Database	COVID19

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Article ; Online: Workshop-based learning and networking: a scalable model for research capacity strengthening in low- and middle-income countries.

Perier, Celine / Nasinghe, Emmanuel / Charles, Isabelle / Ssetaba, Leoson Junior / Ahyong, Vida / Bangs, Derek / Beatty, P Robert / Czudnochowski, Nadine / Diallo, Amy / Dugan, Eli / Fabius, Jacqueline M / Fong Baker, Hildy / Gardner, Jackson / Isaacs, Stephen / Joanah, Birungi / Kalantar, Katrina / Kateete, David / Knight, Matt / Krasilnikov, Maria /

Krogan, Nevan J / Langelier, Chaz / Lee, Eric / Li, Lucy M / Licht, Daniel / Lien, Katie / Lyons, Zilose / Mboowa, Gerald / Mwebaza, Ivan / Mwesigwa, Savannah / Nalwadda, Geraldine / Nichols, Robert / Penaranda, Maria Elena / Petnic, Sarah / Phelps, Maira / Popper, Stephen J / Rape, Michael / Reingold, Arthur / Robbins, Richard / Rosenberg, Oren S / Savage, David F / Schildhauer, Samuel / Settles, Matthew L / Sserwadda, Ivan / Stanley, Sarah / Tato, Cristina M / Tsitsiklis, Alexandra / Van Dis, Erik / Vanaerschot, Manu / Vinden, Joanna / Cox, Jeffery S / Joloba, Moses L / Schaletzky, Julia

Global health action

2022 Volume 15, Issue 1, Page(s) 2062175

Abstract: Science education and research have the potential to drive profound change in low- and middle-income countries (LMICs) through encouraging innovation, attracting industry, and creating job opportunities. However, in LMICs, research capacity is often ... ...

Abstract	Science education and research have the potential to drive profound change in low- and middle-income countries (LMICs) through encouraging innovation, attracting industry, and creating job opportunities. However, in LMICs, research capacity is often limited, and acquisition of funding and access to state-of-the-art technologies is challenging. The Alliance for Global Health and Science (the Alliance) was founded as a partnership between the University of California, Berkeley (USA) and Makerere University (Uganda), with the goal of strengthening Makerere University's capacity for bioscience research. The flagship program of the Alliance partnership is the MU/UCB Biosciences Training Program, an in-country, hands-on workshop model that trains a large number of students from Makerere University in infectious disease and molecular biology research. This approach nucleates training of larger and more diverse groups of students, development of mentoring and bi-directional research partnerships, and support of the local economy. Here, we describe the project, its conception, implementation, challenges, and outcomes of bioscience research workshops. We aim to provide a blueprint for workshop implementation, and create a valuable resource for bioscience research capacity strengthening in LMICs.
MeSH term(s)	Capacity Building ; Developing Countries ; Global Health ; Humans ; Poverty ; Students ; Universities
Language	English
Publishing date	2022-06-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2540569-X
ISSN	1654-9880 ; 1654-9880
ISSN (online)	1654-9880
ISSN	1654-9880
DOI	10.1080/16549716.2022.2062175
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Article: CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

Gupta, Meghna / Azumaya, Caleigh M / Moritz, Michelle / Pourmal, Sergei / Diallo, Amy / Merz, Gregory E / Jang, Gwendolyn / Bouhaddou, Mehdi / Fossati, Andrea / Brilot, Axel F / Diwanji, Devan / Hernandez, Evelyn / Herrera, Nadia / Kratochvil, Huong T / Lam, Victor L / Li, Fei / Li, Yang / Nguyen, Henry C / Nowotny, Carlos /

Owens, Tristan W / Peters, Jessica K / Rizo, Alexandrea N / Schulze-Gahmen, Ursula / Smith, Amber M / Young, Iris D / Yu, Zanlin / Asarnow, Daniel / Billesbølle, Christian / Campbell, Melody G / Chen, Jen / Chen, Kuei-Ho / Chio, Un Seng / Dickinson, Miles Sasha / Doan, Loan / Jin, Mingliang / Kim, Kate / Li, Junrui / Li, Yen-Li / Linossi, Edmond / Liu, Yanxin / Lo, Megan / Lopez, Jocelyne / Lopez, Kyle E / Mancino, Adamo / Moss, Frank R / Paul, Michael D / Pawar, Komal Ishwar / Pelin, Adrian / Pospiech, Thomas H / Puchades, Cristina / Remesh, Soumya Govinda / Safari, Maliheh / Schaefer, Kaitlin / Sun, Ming / Tabios, Mariano C / Thwin, Aye C / Titus, Erron W / Trenker, Raphael / Tse, Eric / Tsui, Tsz Kin Martin / Wang, Feng / Zhang, Kaihua / Zhang, Yang / Zhao, Jianhua / Zhou, Fengbo / Zhou, Yuan / Zuliani-Alvarez, Lorena / Agard, David A / Cheng, Yifan / Fraser, James S / Jura, Natalia / Kortemme, Tanja / Manglik, Aashish / Southworth, Daniel R / Stroud, Robert M / Swaney, Danielle L / Krogan, Nevan J / Frost, Adam / Rosenberg, Oren S / Verba, Kliment A

Research square

2021

Abstract: The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo- ... ...

Abstract	The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIGYF2, an inhibitor of translation initiation and modulator of ribosome-associated quality control. Our work suggests a potential role of Nsp2 in linking viral transcription within the viral replication-transcription complexes (RTC) to the translation initiation of the viral message. Collectively, the structure reported here, combined with mutant interaction mapping, provides a foundation for functional studies of this evolutionary conserved coronavirus protein and may assist future drug design.
Language	English
Publishing date	2021-05-19
Publishing country	United States
Document type	Preprint
DOI	10.21203/rs.3.rs-515215/v1
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Article: CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

bioRxiv : the preprint server for biology

2021

Abstract	The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIGYF2, an inhibitor of translation initiation and modulator of ribosome-associated quality control. Our work suggests a potential role of Nsp2 in linking viral transcription within the viral replication-transcription complexes (RTC) to the translation initiation of the viral message. Collectively, the structure reported here, combined with mutant interaction mapping, provides a foundation for functional studies of this evolutionary conserved coronavirus protein and may assist future drug design.
Language	English
Publishing date	2021-05-11
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.05.10.443524
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Article ; Online: CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes

Gupta, Meghna / Azumaya, Caleigh M. / Moritz, Michelle / Pourmal, Sergei / Diallo, Amy / Merz, Gregory E. / Jang, Gwendolyn / Bouhaddou, Mehdi / Fossati, Andrea / Brilot, Axel F. / Diwanji, Devan / Hernandez, Evelyn / Herrera, Nadia / Kratochvil, Huong T. / Lam, Victor L. / Li, Fei / Li, Yang / Nguyen, Henry C. / Nowotny, Carlos /

Owens, Tristan W. / Peters, Jessica K. / Rizo, Alexandrea N. / Schulze-Gahmen, Ursula / Smith, Amber M. / Young, Iris D. / Yu, Zanlin / Asarnow, Daniel / Billesbølle, Christian / Campbell, Melody G. / Chen, Jen / Chen, Kuei-Ho / Chio, Un Seng / Dickinson, Miles Sasha / Doan, Loan / Jin, Mingliang / Kim, Kate / Li, Junrui / Li, Yen-Li / Linossi, Edmond / Liu, Yanxin / Lo, Megan / Lopez, Jocelyne / Lopez, Kyle E. / Mancino, Adamo / Moss, Frank R. / Paul, Michael D. / Pawar, Komal Ishwar / Pelin, Adrian / Pospiech, Thomas H. / Puchades, Cristina / Remesh, Soumya Govinda / Safari, Maliheh / Schaefer, Kaitlin / Sun, Ming / Tabios, Mariano C / Thwin, Aye C. / Titus, Erron W. / Trenker, Raphael / Tse, Eric / Tsui, Tsz Kin Martin / Wang, Feng / Zhang, Kaihua / Zhang, Yang / Zhao, Jianhua / Zhou, Fengbo / Zhou, Yuan / Zuliani-Alvarez, Lorena / QCRG Structural Biology Consortium / Agard, David A / Cheng, Yifan / Fraser, James S / Jura, Natalia / Kortemme, Tanja / Manglik, Aashish / Southworth, Daniel R. / Stroud, Robert M / Swaney, Danielle L / Krogan, Nevan J / Frost, Adam / Rosenberg, Oren S / Verba, Kliment A

bioRxiv

Abstract	The SARS-CoV-2 protein Nsp2 has been implicated in a wide range of viral processes, but its exact functions, and the structural basis of those functions, remain unknown. Here, we report an atomic model for full-length Nsp2 obtained by combining cryo-electron microscopy with deep learning-based structure prediction from AlphaFold2. The resulting structure reveals a highly-conserved zinc ion-binding site, suggesting a role for Nsp2 in RNA binding. Mapping emerging mutations from variants of SARS-CoV-2 on the resulting structure shows potential host-Nsp2 interaction regions. Using structural analysis together with affinity tagged purification mass spectrometry experiments, we identify Nsp2 mutants that are unable to interact with the actin-nucleation-promoting WASH protein complex or with GIGYF2, an inhibitor of translation initiation and modulator of ribosome-associated quality control. Our work suggests a potential role of Nsp2 in linking viral transcription within the viral replication-transcription complexes (RTC) to the translation initiation of the viral message. Collectively, the structure reported here, combined with mutant interaction mapping, provides a foundation for functional studies of this evolutionary conserved coronavirus protein and may assist future drug design.
Keywords	covid19
Language	English
Publishing date	2021-05-12
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.05.10.443524
Database	COVID19

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Article ; Online: Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.

Gordon, David E / Hiatt, Joseph / Bouhaddou, Mehdi / Rezelj, Veronica V / Ulferts, Svenja / Braberg, Hannes / Jureka, Alexander S / Obernier, Kirsten / Guo, Jeffrey Z / Batra, Jyoti / Kaake, Robyn M / Weckstein, Andrew R / Owens, Tristan W / Gupta, Meghna / Pourmal, Sergei / Titus, Erron W / Cakir, Merve / Soucheray, Margaret / McGregor, Michael /

Cakir, Zeynep / Jang, Gwendolyn / O'Meara, Matthew J / Tummino, Tia A / Zhang, Ziyang / Foussard, Helene / Rojc, Ajda / Zhou, Yuan / Kuchenov, Dmitry / Hüttenhain, Ruth / Xu, Jiewei / Eckhardt, Manon / Swaney, Danielle L / Fabius, Jacqueline M / Ummadi, Manisha / Tutuncuoglu, Beril / Rathore, Ujjwal / Modak, Maya / Haas, Paige / Haas, Kelsey M / Naing, Zun Zar Chi / Pulido, Ernst H / Shi, Ying / Barrio-Hernandez, Inigo / Memon, Danish / Petsalaki, Eirini / Dunham, Alistair / Marrero, Miguel Correa / Burke, David / Koh, Cassandra / Vallet, Thomas / Silvas, Jesus A / Azumaya, Caleigh M / Billesbølle, Christian / Brilot, Axel F / Campbell, Melody G / Diallo, Amy / Dickinson, Miles Sasha / Diwanji, Devan / Herrera, Nadia / Hoppe, Nick / Kratochvil, Huong T / Liu, Yanxin / Merz, Gregory E / Moritz, Michelle / Nguyen, Henry C / Nowotny, Carlos / Puchades, Cristina / Rizo, Alexandrea N / Schulze-Gahmen, Ursula / Smith, Amber M / Sun, Ming / Young, Iris D / Zhao, Jianhua / Asarnow, Daniel / Biel, Justin / Bowen, Alisa / Braxton, Julian R / Chen, Jen / Chio, Cynthia M / Chio, Un Seng / Deshpande, Ishan / Doan, Loan / Faust, Bryan / Flores, Sebastian / Jin, Mingliang / Kim, Kate / Lam, Victor L / Li, Fei / Li, Junrui / Li, Yen-Li / Li, Yang / Liu, Xi / Lo, Megan / Lopez, Kyle E / Melo, Arthur A / Moss, Frank R / Nguyen, Phuong / Paulino, Joana / Pawar, Komal Ishwar / Peters, Jessica K

2020

Abstract: The COVID-19 (Coronavirus disease-2019) pandemic, caused by the SARS-CoV-2 coronavirus, is a significant threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and ... ...

Abstract	The COVID-19 (Coronavirus disease-2019) pandemic, caused by the SARS-CoV-2 coronavirus, is a significant threat to public health and the global economy. SARS-CoV-2 is closely related to the more lethal but less transmissible coronaviruses SARS-CoV-1 and MERS-CoV. Here, we have carried out comparative viral-human protein-protein interaction and viral protein localization analysis for all three viruses. Subsequent functional genetic screening identified host factors that functionally impinge on coronavirus proliferation, including Tom70, a mitochondrial chaperone protein that interacts with both SARS-CoV-1 and SARS-CoV-2 Orf9b, an interaction we structurally characterized using cryo-EM. Combining genetically-validated host factors with both COVID-19 patient genetic data and medical billing records identified important molecular mechanisms and potential drug treatments that merit further molecular and clinical study.
Keywords	QCRG Structural Biology Consortium ; Zoonomia Consortium ; General Science & Technology ; covid19
Subject code	572
Publishing date	2020-10-15
Publisher	eScholarship, University of California
Publishing country	us
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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