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Article: The DHH1/RCKp54 family of helicases: an ancient family of proteins that promote translational silencing.

Presnyak, Vlad / Coller, Jeff

2013 Volume 1829, Issue 8, Page(s) 817–823

Abstract: Translational control is a vital aspect of gene expression. Message specific translational repressors have been known for decades. Recent evidence, however, suggests that a general machinery exists that dampens the translational capacity of the majority ... ...

Abstract	Translational control is a vital aspect of gene expression. Message specific translational repressors have been known for decades. Recent evidence, however, suggests that a general machinery exists that dampens the translational capacity of the majority of mRNAs. This activity has been best ascribed to a conserved family of RNA helicases called the DHH1/RCKp54 family. The function of these helicases is to promote translational silencing. By transitioning mRNA into quiescence, DHH1/RCKp54 helicases promote either mRNA destruction or storage. In this review we describe the known roles of these helicases and propose a mechanistic model to explain their mode of action. This article is part of a Special Issue entitled: The Biology of RNA helicases - Modulation for life.
MeSH term(s)	Animals ; DEAD-box RNA Helicases/chemistry ; DEAD-box RNA Helicases/genetics ; DEAD-box RNA Helicases/metabolism ; Humans ; RNA Interference ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism
Chemical Substances	RNA, Messenger ; DEAD-box RNA Helicases (EC 3.6.4.13)
Language	English
Publishing date	2013-03-23
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	60-7
ISSN	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagrm.2013.03.006
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Article: The DHH1/RCKp54 family of helicases: An ancient family of proteins that promote translational silencing

Presnyak, Vlad / Coller, Jeff

BBA - Gene Regulatory Mechanisms. 2013 Aug., v. 1829, no. 8

2013

Abstract	Translational control is a vital aspect of gene expression. Message specific translational repressors have been known for decades. Recent evidence, however, suggests that a general machinery exists that dampens the translational capacity of the majority of mRNAs. This activity has been best ascribed to a conserved family of RNA helicases called the DHH1/RCKp54 family. The function of these helicases is to promote translational silencing. By transitioning mRNA into quiescence, DHH1/RCKp54 helicases promote either mRNA destruction or storage. In this review we describe the known roles of these helicases and propose a mechanistic model to explain their mode of action. This article is part of a Special Issue entitled: The Biology of RNA helicases — Modulation for life.
Keywords	RNA helicases ; equipment ; gene expression ; mechanism of action ; messenger RNA ; models ; proteins ; translation (genetics)
Language	English
Dates of publication	2013-08
Size	p. 817-823.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	2918786-2
ISSN	1876-4320 ; 1874-9399
ISSN (online)	1876-4320
ISSN	1874-9399
DOI	10.1016/j.bbagrm.2013.03.006
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Human 5' UTR design and variant effect prediction from a massively parallel translation assay.

Sample, Paul J / Wang, Ban / Reid, David W / Presnyak, Vlad / McFadyen, Iain J / Morris, David R / Seelig, Georg

Nature biotechnology

2019 Volume 37, Issue 7, Page(s) 803–809

Abstract: The ability to predict the impact of cis-regulatory sequences on gene expression would facilitate discovery in fundamental and applied biology. Here we combine polysome profiling of a library of 280,000 randomized 5' untranslated regions (UTRs) with deep ...

Abstract	The ability to predict the impact of cis-regulatory sequences on gene expression would facilitate discovery in fundamental and applied biology. Here we combine polysome profiling of a library of 280,000 randomized 5' untranslated regions (UTRs) with deep learning to build a predictive model that relates human 5' UTR sequence to translation. Together with a genetic algorithm, we use the model to engineer new 5' UTRs that accurately direct specified levels of ribosome loading, providing the ability to tune sequences for optimal protein expression. We show that the same approach can be extended to chemically modified RNA, an important feature for applications in mRNA therapeutics and synthetic biology. We test 35,212 truncated human 5' UTRs and 3,577 naturally occurring variants and show that the model predicts ribosome loading of these sequences. Finally, we provide evidence of 45 single-nucleotide variants (SNVs) associated with human diseases that substantially change ribosome loading and thus may represent a molecular basis for disease.
MeSH term(s)	5' Untranslated Regions ; Base Sequence ; Gene Expression Regulation ; Humans ; Models, Genetic ; Protein Biosynthesis ; Pseudouridine/analogs & derivatives ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Reproducibility of Results ; Ribosomes
Chemical Substances	5' Untranslated Regions ; RNA, Messenger ; 1-methylpseudouridine (13860-38-3) ; Pseudouridine (1445-07-4)
Language	English
Publishing date	2019-07-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/s41587-019-0164-5
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Article ; Online: The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G

Presnyak Vlad / Miller James H / Smith Harold C

Retrovirology, Vol 4, Iss 1, p

2007 Volume 81

Abstract: Abstract Background The HIV-1 accessory protein known as viral infectivity factor or Vif binds to the host defence factor human APOBEC3G (hA3G) and prevents its assembly with viral particles and mediates its elimination through ubiquitination and ... ...

Abstract	Abstract Background The HIV-1 accessory protein known as viral infectivity factor or Vif binds to the host defence factor human APOBEC3G (hA3G) and prevents its assembly with viral particles and mediates its elimination through ubiquitination and degradation by the proteosomal pathway. In the absence of Vif, hA3G becomes incorporated within viral particles. During the post entry phase of infection, hA3G attenuates viral replication by binding to the viral RNA genome and deaminating deoxycytidines to form deoxyuridines within single stranded DNA regions of the replicated viral genome. Vif dimerization has been reported to be essential for viral infectivity but the mechanistic requirement for Vif multimerization is unknown. Results We demonstrate that a peptide antagonist of Vif dimerization fused to the cell transduction domain of HIV TAT suppresses live HIV-1 infectivity. We show rapid cellular uptake of the peptide and cytoplasmic distribution. Robust suppression of viral infectivity was dependent on the expression of Vif and hA3G. Disruption of Vif multimerization resulted in the production of virions with markedly increased hA3G content and reduced infectivity. Conclusion The role of Vif multimerization in viral infectivity of nonpermissive cells has been validated with an antagonist of Vif dimerization. An important part of the mechanism for this antiretroviral effect is that blocking Vif dimerization enables hA3G incorporation within virions. We propose that Vif multimers are required to interact with hA3G to exclude it from viral particles during their assembly. Blocking Vif dimerization is an effective means of sustaining hA3G antiretroviral activity in HIV-1 infected cells. Vif dimerization is therefore a validated target for therapeutic HIV-1/AIDS drug development.
Keywords	Medicine (General) ; R5-920 ; Medicine ; R ; DOAJ:Medicine (General) ; DOAJ:Health Sciences ; Immunologic diseases. Allergy ; RC581-607
Subject code	570
Language	English
Publishing date	2007-11-01T00:00:00Z
Publisher	BioMed Central
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G.

Miller, James H / Presnyak, Vlad / Smith, Harold C

Retrovirology

2007 Volume 4, Page(s) 81

Abstract: Background: The HIV-1 accessory protein known as viral infectivity factor or Vif binds to the host defence factor human APOBEC3G (hA3G) and prevents its assembly with viral particles and mediates its elimination through ubiquitination and degradation by ...

Abstract	Background: The HIV-1 accessory protein known as viral infectivity factor or Vif binds to the host defence factor human APOBEC3G (hA3G) and prevents its assembly with viral particles and mediates its elimination through ubiquitination and degradation by the proteosomal pathway. In the absence of Vif, hA3G becomes incorporated within viral particles. During the post entry phase of infection, hA3G attenuates viral replication by binding to the viral RNA genome and deaminating deoxycytidines to form deoxyuridines within single stranded DNA regions of the replicated viral genome. Vif dimerization has been reported to be essential for viral infectivity but the mechanistic requirement for Vif multimerization is unknown. Results: We demonstrate that a peptide antagonist of Vif dimerization fused to the cell transduction domain of HIV TAT suppresses live HIV-1 infectivity. We show rapid cellular uptake of the peptide and cytoplasmic distribution. Robust suppression of viral infectivity was dependent on the expression of Vif and hA3G. Disruption of Vif multimerization resulted in the production of virions with markedly increased hA3G content and reduced infectivity. Conclusion: The role of Vif multimerization in viral infectivity of nonpermissive cells has been validated with an antagonist of Vif dimerization. An important part of the mechanism for this antiretroviral effect is that blocking Vif dimerization enables hA3G incorporation within virions. We propose that Vif multimers are required to interact with hA3G to exclude it from viral particles during their assembly. Blocking Vif dimerization is an effective means of sustaining hA3G antiretroviral activity in HIV-1 infected cells. Vif dimerization is therefore a validated target for therapeutic HIV-1/AIDS drug development.
MeSH term(s)	APOBEC-3G Deaminase ; Cytidine Deaminase/metabolism ; Dimerization ; HIV Infections/virology ; HIV-1/pathogenicity ; HIV-1/physiology ; Humans ; Virulence ; Virus Replication ; vif Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	vif Gene Products, Human Immunodeficiency Virus ; APOBEC-3G Deaminase (EC 3.5.4.5) ; APOBEC3G protein, human (EC 3.5.4.5) ; Cytidine Deaminase (EC 3.5.4.5)
Language	English
Publishing date	2007-11-24
Publishing country	England
Document type	Journal Article
ISSN	1742-4690
ISSN (online)	1742-4690
DOI	10.1186/1742-4690-4-81
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Article ; Online: Dual mRNA therapy restores metabolic function in long-term studies in mice with propionic acidemia.

Nature communications

2020 Volume 11, Issue 1, Page(s) 5339

Abstract: Propionic acidemia/aciduria (PA) is an ultra-rare, life-threatening, inherited metabolic disorder caused by deficiency of the mitochondrial enzyme, propionyl-CoA carboxylase (PCC) composed of six alpha (PCCA) and six beta (PCCB) subunits. We herein ... ...

Abstract	Propionic acidemia/aciduria (PA) is an ultra-rare, life-threatening, inherited metabolic disorder caused by deficiency of the mitochondrial enzyme, propionyl-CoA carboxylase (PCC) composed of six alpha (PCCA) and six beta (PCCB) subunits. We herein report an enzyme replacement approach to treat PA using a combination of two messenger RNAs (mRNAs) (dual mRNAs) encoding both human PCCA (hPCCA) and PCCB (hPCCB) encapsulated in biodegradable lipid nanoparticles (LNPs) to produce functional PCC enzyme in liver. In patient fibroblasts, dual mRNAs encoded proteins localize in mitochondria and produce higher PCC enzyme activity vs. single (PCCA or PCCB) mRNA alone. In a hypomorphic murine model of PA, dual mRNAs normalize ammonia similarly to carglumic acid, a drug approved in Europe for the treatment of hyperammonemia due to PA. Dual mRNAs additionally restore functional PCC enzyme in liver and thus reduce primary disease-associated toxins in a dose-dependent manner in long-term 3- and 6-month repeat-dose studies in PA mice. Dual mRNAs are well-tolerated in these studies with no adverse findings. These studies demonstrate the potential of mRNA technology to chronically administer multiple mRNAs to produce large complex enzymes, with applicability to other genetic disorders.
MeSH term(s)	Animals ; Disease Models, Animal ; Enzyme Replacement Therapy/methods ; Glutamates/therapeutic use ; Humans ; Kinetics ; Lipids/chemistry ; Liver/enzymology ; Methylmalonyl-CoA Decarboxylase/chemistry ; Methylmalonyl-CoA Decarboxylase/genetics ; Methylmalonyl-CoA Decarboxylase/metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Mitochondria/enzymology ; Nanoparticles/administration & dosage ; Nanoparticles/chemistry ; Propionic Acidemia/genetics ; Propionic Acidemia/metabolism ; Propionic Acidemia/therapy ; Protein Subunits/chemistry ; Protein Subunits/genetics ; RNA, Messenger/administration & dosage ; RNA, Messenger/genetics ; RNA, Messenger/therapeutic use
Chemical Substances	Glutamates ; Lipids ; Protein Subunits ; RNA, Messenger ; carglumic acid (5L0HB4V1EW) ; Methylmalonyl-CoA Decarboxylase (EC 7.2.4.3)
Language	English
Publishing date	2020-10-21
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-19156-3
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Article: SARS-CoV-2 mRNA Vaccine Development Enabled by Prototype Pathogen Preparedness.

Corbett, Kizzmekia S / Edwards, Darin / Leist, Sarah R / Abiona, Olubukola M / Boyoglu-Barnum, Seyhan / Gillespie, Rebecca A / Himansu, Sunny / Schäfer, Alexandra / Ziwawo, Cynthia T / DiPiazza, Anthony T / Dinnon, Kenneth H / Elbashir, Sayda M / Shaw, Christine A / Woods, Angela / Fritch, Ethan J / Martinez, David R / Bock, Kevin W / Minai, Mahnaz / Nagata, Bianca M /

Hutchinson, Geoffrey B / Bahl, Kapil / Garcia-Dominguez, Dario / Ma, LingZhi / Renzi, Isabella / Kong, Wing-Pui / Schmidt, Stephen D / Wang, Lingshu / Zhang, Yi / Stevens, Laura J / Phung, Emily / Chang, Lauren A / Loomis, Rebecca J / Altaras, Nedim Emil / Narayanan, Elisabeth / Metkar, Mihir / Presnyak, Vlad / Liu, Catherine / Louder, Mark K / Shi, Wei / Leung, Kwanyee / Yang, Eun Sung / West, Ande / Gully, Kendra L / Wang, Nianshuang / Wrapp, Daniel / Doria-Rose, Nicole A / Stewart-Jones, Guillaume / Bennett, Hamilton / Nason, Martha C / Ruckwardt, Tracy J / McLellan, Jason S / Denison, Mark R / Chappell, James D / Moore, Ian N / Morabito, Kaitlyn M / Mascola, John R / Baric, Ralph S / Carfi, Andrea / Graham, Barney S

bioRxiv : the preprint server for biology

2020

Abstract: A SARS-CoV-2 vaccine is needed to control the global COVID-19 public health crisis. Atomic-level structures directed the application of prefusion-stabilizing mutations that improved expression and immunogenicity of betacoronavirus spike proteins. Using ... ...

Abstract	A SARS-CoV-2 vaccine is needed to control the global COVID-19 public health crisis. Atomic-level structures directed the application of prefusion-stabilizing mutations that improved expression and immunogenicity of betacoronavirus spike proteins. Using this established immunogen design, the release of SARS-CoV-2 sequences triggered immediate rapid manufacturing of an mRNA vaccine expressing the prefusion-stabilized SARS-CoV-2 spike trimer (mRNA-1273). Here, we show that mRNA-1273 induces both potent neutralizing antibody and CD8 T cell responses and protects against SARS-CoV-2 infection in lungs and noses of mice without evidence of immunopathology. mRNA-1273 is currently in a Phase 2 clinical trial with a trajectory towards Phase 3 efficacy evaluation.
Keywords	covid19
Language	English
Publishing date	2020-06-11
Publishing country	United States
Document type	Preprint
DOI	10.1101/2020.06.11.145920
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Article ; Online: SARS-CoV-2 mRNA vaccine design enabled by prototype pathogen preparedness.

Corbett, Kizzmekia S / Edwards, Darin K / Leist, Sarah R / Abiona, Olubukola M / Boyoglu-Barnum, Seyhan / Gillespie, Rebecca A / Himansu, Sunny / Schäfer, Alexandra / Ziwawo, Cynthia T / DiPiazza, Anthony T / Dinnon, Kenneth H / Elbashir, Sayda M / Shaw, Christine A / Woods, Angela / Fritch, Ethan J / Martinez, David R / Bock, Kevin W / Minai, Mahnaz / Nagata, Bianca M /

Hutchinson, Geoffrey B / Wu, Kai / Henry, Carole / Bahl, Kapil / Garcia-Dominguez, Dario / Ma, LingZhi / Renzi, Isabella / Kong, Wing-Pui / Schmidt, Stephen D / Wang, Lingshu / Zhang, Yi / Phung, Emily / Chang, Lauren A / Loomis, Rebecca J / Altaras, Nedim Emil / Narayanan, Elisabeth / Metkar, Mihir / Presnyak, Vlad / Liu, Cuiping / Louder, Mark K / Shi, Wei / Leung, Kwanyee / Yang, Eun Sung / West, Ande / Gully, Kendra L / Stevens, Laura J / Wang, Nianshuang / Wrapp, Daniel / Doria-Rose, Nicole A / Stewart-Jones, Guillaume / Bennett, Hamilton / Alvarado, Gabriela S / Nason, Martha C / Ruckwardt, Tracy J / McLellan, Jason S / Denison, Mark R / Chappell, James D / Moore, Ian N / Morabito, Kaitlyn M / Mascola, John R / Baric, Ralph S / Carfi, Andrea / Graham, Barney S

Nature

2020 Volume 586, Issue 7830, Page(s) 567–571

Abstract: A vaccine for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is needed to control the coronavirus disease 2019 (COVID-19) global pandemic. Structural studies have led to the development of mutations that stabilize Betacoronavirus spike ... ...

Abstract	A vaccine for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is needed to control the coronavirus disease 2019 (COVID-19) global pandemic. Structural studies have led to the development of mutations that stabilize Betacoronavirus spike proteins in the prefusion state, improving their expression and increasing immunogenicity
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Betacoronavirus/genetics ; Betacoronavirus/immunology ; CD8-Positive T-Lymphocytes/immunology ; COVID-19 ; COVID-19 Vaccines ; Clinical Trials, Phase III as Topic ; Coronavirus Infections/genetics ; Coronavirus Infections/immunology ; Coronavirus Infections/prevention & control ; Coronavirus Infections/virology ; Female ; Lung/immunology ; Lung/virology ; Mice ; Mutation ; Nose/immunology ; Nose/virology ; Pandemics/prevention & control ; Pneumonia, Viral/immunology ; Pneumonia, Viral/prevention & control ; Pneumonia, Viral/virology ; RNA, Messenger/genetics ; RNA, Viral/genetics ; SARS-CoV-2 ; Th1 Cells/immunology ; Toll-Like Receptor 4/agonists ; Toll-Like Receptor 4/immunology ; Viral Vaccines/chemistry ; Viral Vaccines/genetics ; Viral Vaccines/immunology
Chemical Substances	Antibodies, Neutralizing ; COVID-19 Vaccines ; RNA, Messenger ; RNA, Viral ; Tlr4 protein, mouse ; Toll-Like Receptor 4 ; Viral Vaccines ; mRNA-1273 vaccine (EPK39PL4R4)
Keywords	covid19
Language	English
Publishing date	2020-08-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-020-2622-0
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Article: SARS-CoV-2 mRNA vaccine design enabled by prototype pathogen preparedness

Nature

Abstract	A vaccine for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is needed to control the coronavirus disease 2019 (COVID-19) global pandemic. Structural studies have led to the development of mutations that stabilize Betacoronavirus spike proteins in the prefusion state, improving their expression and increasing immunogenicity1. This principle has been applied to design mRNA-1273, an mRNA vaccine that encodes a SARS-CoV-2 spike protein that is stabilized in the prefusion conformation. Here we show that mRNA-1273 induces potent neutralizing antibody responses to both wild-type (D614) and D614G mutant2 SARS-CoV-2 as well as CD8+ T cell responses, and protects against SARS-CoV-2 infection in the lungs and noses of mice without evidence of immunopathology. mRNA-1273 is currently in a phase III trial to evaluate its efficacy.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #807033
Database	COVID19

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Article ; Online: SARS-CoV-2 mRNA Vaccine Development Enabled by Prototype Pathogen Preparedness

Corbett, Kizzmekia S. / Edwards, Darin / Leist, Sarah R. / Abiona, Olubukola M. / Boyoglu-Barnum, Seyhan / Gillespie, Rebecca A. / Himansu, Sunny / Schafer, Alexandra / Ziwawo, Cynthia T. / DiPiazza, Anthony T. / Dinnon, Kenneth H. / Elbashir, Sayda M. / Shaw, Christine A. / Woods, Angela / Fritch, Ethan J. / Martinez, David R. / Bock, Kevin W. / Minai, Mahnaz / Nagata, Bianca M. /

Hutchinson, Geoffrey B. / Bahl, Kapil / Garcia-Dominguez, Dario / Ma, LingZhi / Renzi, Isabella / Kong, Wing-Pui / Schmidt, Stephen D. / Wang, Lingshu / Zhang, Yi / Stevens, Laura J. / Phung, Emily / Chang, Lauren A. / Loomis, Rebecca J. / Altaras, Nedim Emil / Narayanan, Elisabeth / Metkar, Mihir / Presnyak, Vlad / Liu, Catherine / Louder, Mark K. / Shi, Wei / Leung, Kwanyee / Yang, Eun Sung / West, Ande / Gully, Kendra L. / Wang, Nianshuang / Wrapp, Daniel / Doria-Rose, Nicole A. / Stewart-Jones, Guillaume / Bennett, Hamilton / Nason, Martha C. / Ruckwardt, Tracy J. / McLellan, Jason S. / Denison, Mark R. / Chappell, James D. / Moore, Ian N. / Morabito, Kaitlyn M. / Mascola, John R. / Baric, Ralph S. / Carfi, Andrea / Graham, Barney S

bioRxiv

Abstract	A SARS-CoV-2 vaccine is needed to control the global COVID-19 public health crisis. Atomic-level structures directed the application of prefusion-stabilizing mutations that improved expression and immunogenicity of betacoronavirus spike proteins. Using this established immunogen design, the release of SARS-CoV-2 sequences triggered immediate rapid manufacturing of an mRNA vaccine expressing the prefusion-stabilized SARS-CoV-2 spike trimer (mRNA-1273). Here, we show that mRNA-1273 induces both potent neutralizing antibody and CD8 T cell responses and protects against SARS-CoV-2 infection in lungs and noses of mice without evidence of immunopathology. mRNA-1273 is currently in a Phase 2 clinical trial with a trajectory towards Phase 3 efficacy evaluation.
Keywords	covid19
Language	English
Publishing date	2020-06-11
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.06.11.145920
Database	COVID19

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