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Article ; Online: Understanding Rhinovirus Circulation and Impact on Illness.

Esneau, Camille / Duff, Alexandra Cate / Bartlett, Nathan W

2022 Volume 14, Issue 1

Abstract: Rhinoviruses (RVs) have been reported as one of the main viral causes for severe respiratory illnesses that may require hospitalization, competing with the burden of other respiratory viruses such as influenza and RSV in terms of severity, economic cost, ...

Abstract	Rhinoviruses (RVs) have been reported as one of the main viral causes for severe respiratory illnesses that may require hospitalization, competing with the burden of other respiratory viruses such as influenza and RSV in terms of severity, economic cost, and resource utilization. With three species and 169 subtypes, RV presents the greatest diversity within the Enterovirus genus, and despite the efforts of the research community to identify clinically relevant subtypes to target therapeutic strategies, the role of species and subtype in the clinical outcomes of RV infection remains unclear. This review aims to collect and organize data relevant to RV illness in order to find patterns and links with species and/or subtype, with a specific focus on species and subtype diversity in clinical studies typing of respiratory samples.
MeSH term(s)	Asthma/etiology ; Coinfection/virology ; Enterovirus ; Enterovirus Infections/virology ; Genotyping Techniques ; Hospitalization ; Humans ; Picornaviridae Infections/virology ; Respiratory Tract Infections/virology ; Rhinovirus/classification ; Rhinovirus/genetics ; Serotyping
Language	English
Publishing date	2022-01-13
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14010141
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Understanding Rhinovirus Circulation and Impact on Illness

Esneau, Camille / Duff, Alexandra Cate / Bartlett, Nathan W.

Viruses. 2022 Jan. 13, v. 14, no. 1

2022

Abstract	Rhinoviruses (RVs) have been reported as one of the main viral causes for severe respiratory illnesses that may require hospitalization, competing with the burden of other respiratory viruses such as influenza and RSV in terms of severity, economic cost, and resource utilization. With three species and 169 subtypes, RV presents the greatest diversity within the Enterovirus genus, and despite the efforts of the research community to identify clinically relevant subtypes to target therapeutic strategies, the role of species and subtype in the clinical outcomes of RV infection remains unclear. This review aims to collect and organize data relevant to RV illness in order to find patterns and links with species and/or subtype, with a specific focus on species and subtype diversity in clinical studies typing of respiratory samples.
Keywords	Enterovirus ; economic costs ; influenza ; therapeutics
Language	English
Dates of publication	2022-0113
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v14010141
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Human coronaviruses 229E and OC43 replicate and induce distinct antiviral responses in differentiated primary human bronchial epithelial cells.

Loo, Su-Ling / Wark, Peter A B / Esneau, Camille / Nichol, Kristy S / Hsu, Alan C-Y / Bartlett, Nathan W

American journal of physiology. Lung cellular and molecular physiology

2020 Volume 319, Issue 6, Page(s) L926–L931

Abstract: The recurrent emergence of novel, pathogenic coronaviruses (CoVs) severe acute respiratory syndrome coronavirus 1 (SARS-CoV-1; 2002), Middle East respiratory syndrome (MERS)-CoV (2012), and most recently SARS-CoV-2 (2019) has highlighted the need for ... ...

Abstract	The recurrent emergence of novel, pathogenic coronaviruses (CoVs) severe acute respiratory syndrome coronavirus 1 (SARS-CoV-1; 2002), Middle East respiratory syndrome (MERS)-CoV (2012), and most recently SARS-CoV-2 (2019) has highlighted the need for physiologically informative airway epithelial cell infection models for studying immunity to CoVs and development of antiviral therapies. To address this, we developed an in vitro infection model for two human coronaviruses; alphacoronavirus 229E-CoV (229E) and betacoronavirus OC43-CoV (OC43) in differentiated primary human bronchial epithelial cells (pBECs). Primary BECs from healthy subjects were grown at air-liquid interface (ALI) and infected with 229E or OC43, and replication kinetics and time-course expression of innate immune mediators were assessed. OC43 and 229E-CoVs replicated in differentiated pBECs but displayed distinct replication kinetics: 229E replicated rapidly with viral load peaking at 24 h postinfection, while OC43 replication was slower peaking at 96 h after infection. This was associated with diverse antiviral response profiles defined by increased expression of type I/III interferons and interferon-stimulated genes (ISGs) by 229E compared with no innate immune activation with OC43 infection. Understanding the host-virus interaction for previously established coronaviruses will give insight into pathogenic mechanisms underpinning SARS-CoV-2-induced respiratory disease and other future coronaviruses that may arise from zoonotic sources.
MeSH term(s)	Antiviral Agents/pharmacology ; Bronchi/drug effects ; Bronchi/immunology ; Bronchi/virology ; Cells, Cultured ; Coronavirus 229E, Human/drug effects ; Coronavirus 229E, Human/immunology ; Coronavirus Infections/drug therapy ; Coronavirus Infections/immunology ; Coronavirus Infections/virology ; Epithelial Cells/drug effects ; Epithelial Cells/immunology ; Epithelial Cells/virology ; Humans ; Interferons/metabolism ; Virus Replication/drug effects
Chemical Substances	Antiviral Agents ; interferon type III ; Interferons (9008-11-1)
Keywords	covid19
Language	English
Publishing date	2020-09-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	1013184-x
ISSN	1522-1504 ; 1040-0605
ISSN (online)	1522-1504
ISSN	1040-0605
DOI	10.1152/ajplung.00374.2020
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Article ; Online: IL-25 blockade augments antiviral immunity during respiratory virus infection.

Williams, Teresa C / Loo, Su-Ling / Nichol, Kristy S / Reid, Andrew T / Veerati, Punnam C / Esneau, Camille / Wark, Peter A B / Grainge, Christopher L / Knight, Darryl A / Vincent, Thomas / Jackson, Crystal L / Alton, Kirby / Shimkets, Richard A / Girkin, Jason L / Bartlett, Nathan W

Communications biology

2022 Volume 5, Issue 1, Page(s) 415

Abstract: IL-25 is implicated in the pathogenesis of viral asthma exacerbations. However, the effect of IL-25 on antiviral immunity has yet to be elucidated. We observed abundant expression and colocalization of IL-25 and IL-25 receptor at the apical surface of ... ...

Abstract	IL-25 is implicated in the pathogenesis of viral asthma exacerbations. However, the effect of IL-25 on antiviral immunity has yet to be elucidated. We observed abundant expression and colocalization of IL-25 and IL-25 receptor at the apical surface of uninfected airway epithelial cells and rhinovirus infection increased IL-25 expression. Analysis of immune transcriptome of rhinovirus-infected differentiated asthmatic bronchial epithelial cells (BECs) treated with an anti-IL-25 monoclonal antibody (LNR125) revealed a re-calibrated response defined by increased type I/III IFN and reduced expression of type-2 immune genes CCL26, IL1RL1 and IL-25 receptor. LNR125 treatment also increased type I/III IFN expression by coronavirus infected BECs. Exogenous IL-25 treatment increased viral load with suppressed innate immunity. In vivo LNR125 treatment reduced IL-25/type 2 cytokine expression and increased IFN-β expression and reduced lung viral load. We define a new immune-regulatory role for IL-25 that directly inhibits virus induced airway epithelial cell innate anti-viral immunity.
MeSH term(s)	Antiviral Agents/pharmacology ; Asthma/metabolism ; Humans ; Immunity, Innate ; Interleukin-17/immunology ; Rhinovirus ; Virus Diseases
Chemical Substances	Antiviral Agents ; IL25 protein, human ; Interleukin-17
Language	English
Publishing date	2022-05-04
Publishing country	England
Document type	Journal Article
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-022-03367-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: TLR2-mediated innate immune priming boosts lung anti-viral immunity.

Girkin, Jason / Loo, Su-Ling / Esneau, Camille / Maltby, Steven / Mercuri, Francesca / Chua, Brendon / Reid, Andrew T / Veerati, Punnam Chander / Grainge, Chris L / Wark, Peter A B / Knight, Darryl / Jackson, David / Demaison, Christophe / Bartlett, Nathan W

The European respiratory journal

2021 Volume 58, Issue 1

Abstract: Background: We assessed whether Toll-like receptor (TLR)2 activation boosts the innate immune response to rhinovirus infection, as a treatment strategy for virus-induced respiratory diseases.: Methods: We employed treatment with a novel TLR2 agonist ( ...

Abstract	Background: We assessed whether Toll-like receptor (TLR)2 activation boosts the innate immune response to rhinovirus infection, as a treatment strategy for virus-induced respiratory diseases. Methods: We employed treatment with a novel TLR2 agonist (INNA-X) prior to rhinovirus infection in mice, and INNA-X treatment in differentiated human bronchial epithelial cells derived from asthmatic-donors. We assessed viral load, immune cell recruitment, cytokines, type I and III interferon (IFN) production, as well as the lung tissue and epithelial cell immune transcriptome. Results: We show, Conclusion: Airway epithelial cell TLR2 activation induces prolonged innate immune priming, defined by early NF-κB activation, IFN-λ expression and lymphocyte recruitment. This response enhanced anti-viral innate immunity and reduced virus-induced airway inflammation.
MeSH term(s)	Animals ; Antiviral Agents ; Epithelial Cells ; Humans ; Immunity, Innate ; Lung ; Mice ; Toll-Like Receptor 2
Chemical Substances	Antiviral Agents ; TLR2 protein, human ; Tlr2 protein, mouse ; Toll-Like Receptor 2
Language	English
Publishing date	2021-07-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639359-7
ISSN	1399-3003 ; 0903-1936
ISSN (online)	1399-3003
ISSN	0903-1936
DOI	10.1183/13993003.01584-2020
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Article ; Online: Biochemical characterization of the respiratory syncytial virus N

Esneau, Camille / Raynal, Bertrand / Roblin, Pierre / Brûlé, Sébastien / Richard, Charles-Adrien / Fix, Jenna / Eléouët, Jean-François / Galloux, Marie

The Journal of biological chemistry

2019 Volume 294, Issue 10, Page(s) 3647–3660

Abstract: As all the viruses belonging to ... ...

Abstract	As all the viruses belonging to the
MeSH term(s)	Binding Sites ; DNA-Directed RNA Polymerases/genetics ; DNA-Directed RNA Polymerases/metabolism ; Models, Molecular ; Mutation ; Nucleoproteins/chemistry ; Nucleoproteins/genetics ; Nucleoproteins/metabolism ; Protein Conformation ; Respiratory Syncytial Virus, Human ; Solutions ; Surface Properties ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism
Chemical Substances	Nucleoproteins ; Solutions ; Viral Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6)
Language	English
Publishing date	2019-01-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.RA118.006453
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Article: Human coronaviruses 229E and OC43 replicate and induce distinct anti-viral responses in differentiated primary human bronchial epithelial cells

Loo, Su-Ling / Wark, Peter A B / Esneau, Camille / Nichol, Kristy S / Hsu, Alan C-Y / Bartlett, Nathan W

Abstract: The recurrent emergence of novel, pathogenic coronaviruses (CoVs) SARS-CoV-1 (2002), MERS-CoV (2012) and most recently SARS-CoV-2 (2019) has highlighted the need for physiologically informative airway epithelial cell infection models for studying ... ...

Abstract	The recurrent emergence of novel, pathogenic coronaviruses (CoVs) SARS-CoV-1 (2002), MERS-CoV (2012) and most recently SARS-CoV-2 (2019) has highlighted the need for physiologically informative airway epithelial cell infection models for studying immunity to CoVs and development of anti-viral therapies. To address this, we developed an in-vitro infection model for two human coronaviruses; alphacoronavirus 229E-CoV (229E) and betacoronavirus OC43-CoV (OC43) in differentiated primary human bronchial epithelial cells (pBECs). Primary BECs from healthy subjects were grown at air liquid interface (ALI) and infected with 229E or OC43, and replication kinetics and time-course expression of innate immune mediators were assessed. OC43 and 229E-CoVs replicated in differentiated pBECs but displayed distinct replication kinetics: 229E replicated rapidly with viral load peaking at 24 hours post-infection, whilst OC43 replication was slower peaking at 7 days after infection. This was associated with diverse anti-viral response profiles defined by increased expression of type I/III interferons and interferon-stimulated genes (ISGs) by 229E compared to OC43. Understanding the host-virus interaction for previously established coronaviruses will give insight into pathogenic mechanisms underpinning SARS-CoV-2-induced respiratory disease and other future coronaviruses that may arise from zoonotic sources.
Keywords	covid19
Publisher	WHO
Document type	Article
Note	WHO #Covidence: #751458
Database	COVID19

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Article ; Online: TMPRSS2 activation of Omicron lineage Spike glycoproteins is regulated by TMPRSS2 cleavage of ACE2

bioRxiv

Abstract: Continued high levels spread of SARS-CoV-2 globally enabled accumulation of changes within the Spike glycoprotein, leading to resistance to neutralising antibodies and concomitant changes to entry requirements that increased viral transmission fitness. ... ...

Abstract	Continued high levels spread of SARS-CoV-2 globally enabled accumulation of changes within the Spike glycoprotein, leading to resistance to neutralising antibodies and concomitant changes to entry requirements that increased viral transmission fitness. Herein, we demonstrate a significant change in ACE2 and TMPRSS2 use by primary SARS-CoV-2 isolates that occurred upon arrival of Omicron lineages. Mechanistically we show this shift to be a function of two distinct ACE2 pools based on cleavage or non-cleavage of ACE2 by TMPRSS2 activity. In engineered cells overexpressing ACE2 and TMPRSS2, ACE2 was cleaved by TMPRSS2 and this led to either augmentation or progressive attenuation of pre-Omicron and Omicron lineages, respectfully. In contrast, TMPRSS2 resistant ACE2 restored infectivity across all Omicron lineages through enabling ACE2 binding that facilitated TMPRSS2 spike activation. Therefore, our data support the tropism shift of Omicron lineages to be a function of evolution towards the use of uncleaved pools of ACE2 with the latter consistent with its role as a chaperone for many tissue specific amino acid transport proteins.
Keywords	covid19
Language	English
Publishing date	2023-09-22
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.09.22.558930
Database	COVID19

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Article ; Online: TMPRSS2 activation of Omicron lineage Spike glycoproteins is regulated by TMPRSS2 cleavage of ACE2

bioRxiv

Abstract	Continued high levels spread of SARS-CoV-2 globally enabled accumulation of changes within the Spike glycoprotein, leading to resistance to neutralising antibodies and concomitant changes to entry requirements that increased viral transmission fitness. Herein, we demonstrate a significant change in ACE2 and TMPRSS2 use by primary SARS-CoV-2 isolates that occurred upon arrival of Omicron lineages. Mechanistically we show this shift to be a function of two distinct ACE2 pools based on cleavage or non-cleavage of ACE2 by TMPRSS2 activity. In engineered cells overexpressing ACE2 and TMPRSS2, ACE2 was cleaved by TMPRSS2 and this led to either augmentation or progressive attenuation of pre-Omicron and Omicron lineages, respectfully. In contrast, TMPRSS2 resistant ACE2 restored infectivity across all Omicron lineages through enabling ACE2 binding that facilitated TMPRSS2 spike activation. Therefore, our data support the tropism shift of Omicron lineages to be a function of evolution towards the use of uncleaved pools of ACE2 with the latter consistent with its role as a chaperone for many tissue specific amino acid transport proteins.
Keywords	covid19
Language	English
Publishing date	2023-09-22
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.09.22.558930
Database	COVID19

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Article ; Online: RSV hijacks cellular protein phosphatase 1 to regulate M2-1 phosphorylation and viral transcription.

Richard, Charles-Adrien / Rincheval, Vincent / Lassoued, Safa / Fix, Jenna / Cardone, Christophe / Esneau, Camille / Nekhai, Sergei / Galloux, Marie / Rameix-Welti, Marie-Anne / Sizun, Christina / Eléouët, Jean-François

PLoS pathogens

2018 Volume 14, Issue 3, Page(s) e1006920

Abstract: Respiratory syncytial virus (RSV) RNA synthesis occurs in cytoplasmic inclusion bodies (IBs) in which all the components of the viral RNA polymerase are concentrated. In this work, we show that RSV P protein recruits the essential RSV transcription ... ...

Abstract	Respiratory syncytial virus (RSV) RNA synthesis occurs in cytoplasmic inclusion bodies (IBs) in which all the components of the viral RNA polymerase are concentrated. In this work, we show that RSV P protein recruits the essential RSV transcription factor M2-1 to IBs independently of the phosphorylation state of M2-1. We also show that M2-1 dephosphorylation is achieved by a complex formed between P and the cellular phosphatase PP1. We identified the PP1 binding site of P, which is an RVxF-like motif located nearby and upstream of the M2-1 binding region. NMR confirmed both P-M2-1 and P-PP1 interaction regions in P. When the P-PP1 interaction was disrupted, M2-1 remained phosphorylated and viral transcription was impaired, showing that M2-1 dephosphorylation is required, in a cyclic manner, for efficient viral transcription. IBs contain substructures called inclusion bodies associated granules (IBAGs), where M2-1 and neo-synthesized viral mRNAs concentrate. Disruption of the P-PP1 interaction was correlated with M2-1 exclusion from IBAGs, indicating that only dephosphorylated M2-1 is competent for viral mRNA binding and hence for a previously proposed post-transcriptional function.
MeSH term(s)	Amino Acid Sequence ; Binding Sites ; Cytoplasmic Granules/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Humans ; Inclusion Bodies/metabolism ; Phosphorylation ; Protein Phosphatase 1/metabolism ; Proteolysis ; RNA, Viral ; Respiratory Syncytial Virus Infections/metabolism ; Respiratory Syncytial Virus Infections/virology ; Respiratory Syncytial Virus, Human/genetics ; Respiratory Syncytial Virus, Human/pathogenicity ; Sequence Homology ; Transcription, Genetic ; Viral Proteins/metabolism
Chemical Substances	RNA, Viral ; Viral Proteins ; DNA-Directed RNA Polymerases (EC 2.7.7.6) ; Protein Phosphatase 1 (EC 3.1.3.16)
Language	English
Publishing date	2018-02-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; 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.1006920
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