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Artikel ; Online: Enveloped RNA virus utilization of phosphatidylserine receptors: Advantages of exploiting a conserved, widely available mechanism of entry.

Bohan, Dana / Maury, Wendy

2021 Band 17, Heft 9, Seite(n) e1009899

Mesh-Begriff(e)	Animals ; Humans ; RNA Viruses/physiology ; Receptors, Cell Surface/metabolism ; Receptors, Virus/metabolism ; Virion/physiology ; Virus Attachment ; Virus Internalization
Chemische Substanzen	Receptors, Cell Surface ; Receptors, Virus ; phosphatidylserine receptor
Sprache	Englisch
Erscheinungsdatum	2021-09-23
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7374
ISSN (online)	1553-7374
ISSN	1553-7374
DOI	10.1371/journal.ppat.1009899
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Epitranscriptomic

Phillips, Stacia / Mishra, Tarun / Khadka, Shaubhagya / Bohan, Dana / Espada, Constanza E / Maury, Wendy / Wu, Li

Microbiology spectrum

2023 Band 11, Heft 1, Seite(n) e0394322

Abstract: ... ...

Abstract	N
Mesh-Begriff(e)	Humans ; SARS-CoV-2/genetics ; COVID-19/pathology ; Lung/pathology ; Epithelial Cells ; RNA/metabolism ; Interferons
Chemische Substanzen	N-methyladenosine (CLE6G00625) ; RNA (63231-63-0) ; Interferons (9008-11-1)
Sprache	Englisch
Erscheinungsdatum	2023-01-10
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.03943-22
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Epitranscriptomic N6-methyladenosine profile of SARS-CoV-2-infected human lung epithelial cells

Phillips, Stacia / Khadka, Shaubhagya / Bohan, Dana / Espada, Constanza E. / Maury, Wendy / Wu, Li

bioRxiv

Abstract: N6-methyladenosine (m6A) is a dynamic post-transcriptional RNA modification that plays an important role in determining transcript fate. Severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) has caused the global pandemic of coronavirus ... ...

Abstract	N6-methyladenosine (m6A) is a dynamic post-transcriptional RNA modification that plays an important role in determining transcript fate. Severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) has caused the global pandemic of coronavirus disease 2019 (COVID-19) and the virus has been extensively studied. However, how m6A modification of host cell RNAs change during SARS-CoV-2 infection has not been reported. Here we define the epitranscriptomic m6A profile of SARS-CoV-2-infected human lung epithelial cells compared to uninfected controls. Biological pathway analyses revealed that differentially methylated transcripts were significantly associated with cancer-related pathways, protein processing in the endoplasmic reticulum, cell death and proliferation. Upstream regulators predicted to be associated with the proteins encoded by differentially methylated mRNAs include proteins involved in the type I interferon response, inflammation, and cytokine signaling. These data suggest that m6A modification of cellular RNA is an important mechanism of regulating host gene expression during SARS-CoV-2 infection of lung epithelial cells.
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2022-08-01
Verlag	Cold Spring Harbor Laboratory
Dokumenttyp	Artikel ; Online
DOI	10.1101/2022.08.01.502311
Datenquelle	COVID19

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Artikel ; Online: IL-4/IL-13 polarization of macrophages enhances Ebola virus glycoprotein-dependent infection.

Rogers, Kai J / Brunton, Bethany / Mallinger, Laura / Bohan, Dana / Sevcik, Kristina M / Chen, Jing / Ruggio, Natalie / Maury, Wendy

PLoS neglected tropical diseases

2019 Band 13, Heft 12, Seite(n) e0007819

Abstract: Background: Ebolavirus (EBOV) outbreaks, while sporadic, cause tremendous morbidity and mortality. No therapeutics or vaccines are currently licensed; however, a vaccine has shown promise in clinical trials. A critical step towards development of ... ...

Abstract	Background: Ebolavirus (EBOV) outbreaks, while sporadic, cause tremendous morbidity and mortality. No therapeutics or vaccines are currently licensed; however, a vaccine has shown promise in clinical trials. A critical step towards development of effective therapeutics is a better understanding of factors that govern host susceptibility to this pathogen. As macrophages are an important cell population targeted during virus replication, we explore the effect of cytokine polarization on macrophage infection. Methods/main findings: We utilized a BSL2 EBOV model virus, infectious, recombinant vesicular stomatitis virus encoding EBOV glycoprotein (GP) (rVSV/EBOV GP) in place of its native glycoprotein. Macrophages polarized towards a M2-like anti-inflammatory state by combined IL-4 and IL-13 treatment were more susceptible to rVSV/EBOV GP, but not to wild-type VSV (rVSV/G), suggesting that EBOV GP-dependent entry events were enhanced by these cytokines. Examination of RNA expression of known surface receptors that bind and internalize filoviruses demonstrated that IL-4/IL-13 stimulated expression of the C-type lectin receptor DC-SIGN in human macrophages and addition of the competitive inhibitor mannan abrogated IL-4/IL-13 enhanced infection. Two murine DC-SIGN-like family members, SIGNR3 and SIGNR5, were upregulated by IL-4/IL-13 in murine macrophages, but only SIGNR3 enhanced virus infection in a mannan-inhibited manner, suggesting that murine SIGNR3 plays a similar role to human DC-SIGN. In vivo IL-4/IL-13 administration significantly increased virus-mediated mortality in a mouse model and transfer of ex vivo IL-4/IL-13-treated murine peritoneal macrophages into the peritoneal cavity of mice enhanced pathogenesis. Significance: These studies highlight the ability of macrophage polarization to influence EBOV GP-dependent virus replication in vivo and ex vivo, with M2a polarization upregulating cell surface receptor expression and thereby enhancing virus replication. Our findings provide an increased understanding of the host factors in macrophages governing susceptibility to filoviruses and identify novel murine receptors mediating EBOV entry.
Mesh-Begriff(e)	Animals ; Disease Models, Animal ; Ebolavirus/physiology ; Female ; Hemorrhagic Fever, Ebola/pathology ; Hemorrhagic Fever, Ebola/virology ; Host-Pathogen Interactions ; Interleukin-13/metabolism ; Interleukin-4/metabolism ; Macrophages/immunology ; Macrophages/virology ; Male ; Mice, Inbred C57BL ; Virus Internalization
Chemische Substanzen	Il4 protein, mouse ; Interleukin-13 ; Interleukin-4 (207137-56-2)
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2019-12-11
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2429704-5
ISSN	1935-2735 ; 1935-2727
ISSN (online)	1935-2735
ISSN	1935-2727
DOI	10.1371/journal.pntd.0007819
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Frontline Science: CD40 signaling restricts RNA virus replication in Mϕs, leading to rapid innate immune control of acute virus infection.

Rogers, Kai J / Shtanko, Olena / Stunz, Laura L / Mallinger, Laura N / Arkee, Tina / Schmidt, Megan E / Bohan, Dana / Brunton, Bethany / White, Judith M / Varga, Steve M / Butler, Noah S / Bishop, Gail A / Maury, Wendy

Journal of leukocyte biology

2020 Band 109, Heft 2, Seite(n) 309–325

Abstract: Many acute viral infections target tissue Mϕs, yet the mechanisms of Mϕ-mediated control of viruses are poorly understood. Here, we report that CD40 expressed by peritoneal Mϕs restricts early infection of a broad range of RNA viruses. Loss of CD40 ... ...

Abstract	Many acute viral infections target tissue Mϕs, yet the mechanisms of Mϕ-mediated control of viruses are poorly understood. Here, we report that CD40 expressed by peritoneal Mϕs restricts early infection of a broad range of RNA viruses. Loss of CD40 expression enhanced virus replication as early as 12-24 h of infection and, conversely, stimulation of CD40 signaling with an agonistic Ab blocked infection. With peritoneal cell populations infected with the filovirus, wild-type (WT) Ebola virus (EBOV), or a BSL2 model virus, recombinant vesicular stomatitis virus encoding Ebola virus glycoprotein (rVSV/EBOV GP), we examined the mechanism conferring protection. Here, we demonstrate that restricted virus replication in Mϕs required CD154/CD40 interactions that stimulated IL-12 production through TRAF6-dependent signaling. In turn, IL-12 production resulted in IFN-γ production, which induced proinflammatory polarization of Mϕs, protecting the cells from infection. These CD40-dependent events protected mice against virus challenge. CD40
Mesh-Begriff(e)	Acute Disease ; Animals ; CD40 Antigens/metabolism ; CD40 Ligand/metabolism ; Ebolavirus/physiology ; Glycoproteins/immunology ; Humans ; Immunity, Innate ; Interferon-gamma/metabolism ; Interleukin-12/biosynthesis ; Macrophages/immunology ; Macrophages/virology ; Mice, Inbred C57BL ; Models, Biological ; Peritoneum/pathology ; Peritoneum/virology ; RNA Viruses/physiology ; Signal Transduction ; TNF Receptor-Associated Factor 6/metabolism ; Virus Diseases/immunology ; Virus Diseases/virology ; Virus Replication/physiology ; Mice
Chemische Substanzen	CD40 Antigens ; Glycoproteins ; TNF Receptor-Associated Factor 6 ; CD40 Ligand (147205-72-9) ; Interleukin-12 (187348-17-0) ; Interferon-gamma (82115-62-6)
Sprache	Englisch
Erscheinungsdatum	2020-05-22
Erscheinungsland	England
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	605722-6
ISSN	1938-3673 ; 0741-5400
ISSN (online)	1938-3673
ISSN	0741-5400
DOI	10.1002/JLB.4HI0420-285RR
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Phosphatidylserine Receptors Enhance SARS-CoV-2 Infection: AXL as a Therapeutic Target for COVID-19.

Bohan, Dana / Ert, Hanora Van / Ruggio, Natalie / Rogers, Kai J / Badreddine, Mohammad / Aguilar Briseño, José A / Rojas Chavez, Roberth Anthony / Gao, Boning / Stokowy, Tomasz / Christakou, Eleni / Micklem, David / Gausdal, Gro / Haim, Hillel / Minna, John / Lorens, James B / Maury, Wendy

bioRxiv : the preprint server for biology

2021

Abstract: Phosphatidylserine (PS) receptors are PS binding proteins that mediate uptake of apoptotic bodies. Many enveloped viruses utilize this PS/PS receptor mechanism to adhere to and internalize into the endosomal compartment of cells and this is termed ... ...

Abstract	Phosphatidylserine (PS) receptors are PS binding proteins that mediate uptake of apoptotic bodies. Many enveloped viruses utilize this PS/PS receptor mechanism to adhere to and internalize into the endosomal compartment of cells and this is termed apoptotic mimicry. For viruses that have a mechanism(s) of endosomal escape, apoptotic mimicry is a productive route of virus entry. We evaluated if PS receptors serve as cell surface receptors for SARS-CoV-2 and found that the PS receptors, AXL, TIM-1 and TIM-4, facilitated virus infection when low concentrations of the SARS-CoV-2 cognate receptor, ACE2, was present. Consistent with the established mechanism of PS receptor utilization by other viruses, PS liposomes competed with SARS-CoV-2 for binding and entry. We demonstrated that this PS receptor enhances SARS-CoV-2 binding to and infection of an array of human lung cell lines and is an under-appreciated but potentially important host factor facilitating SARS-CoV-2 entry.
Sprache	Englisch
Erscheinungsdatum	2021-06-24
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2021.06.15.448419
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Phosphatidylserine receptors enhance SARS-CoV-2 infection.

Bohan, Dana / Van Ert, Hanora / Ruggio, Natalie / Rogers, Kai J / Badreddine, Mohammad / Aguilar Briseño, José A / Elliff, Jonah M / Rojas Chavez, Roberth Anthony / Gao, Boning / Stokowy, Tomasz / Christakou, Eleni / Kursula, Petri / Micklem, David / Gausdal, Gro / Haim, Hillel / Minna, John / Lorens, James B / Maury, Wendy

PLoS pathogens

2021 Band 17, Heft 11, Seite(n) e1009743

Abstract: Phosphatidylserine (PS) receptors enhance infection of many enveloped viruses through virion-associated PS binding that is termed apoptotic mimicry. Here we show that this broadly shared uptake mechanism is utilized by SARS-CoV-2 in cells that express ... ...

Abstract	Phosphatidylserine (PS) receptors enhance infection of many enveloped viruses through virion-associated PS binding that is termed apoptotic mimicry. Here we show that this broadly shared uptake mechanism is utilized by SARS-CoV-2 in cells that express low surface levels of ACE2. Expression of members of the TIM (TIM-1 and TIM-4) and TAM (AXL) families of PS receptors enhance SARS-CoV-2 binding to cells, facilitate internalization of fluorescently-labeled virions and increase ACE2-dependent infection of SARS-CoV-2; however, PS receptors alone did not mediate infection. We were unable to detect direct interactions of the PS receptor AXL with purified SARS-CoV-2 spike, contrary to a previous report. Instead, our studies indicate that the PS receptors interact with PS on the surface of SARS-CoV-2 virions. In support of this, we demonstrate that: 1) significant quantities of PS are located on the outer leaflet of SARS-CoV-2 virions, 2) PS liposomes, but not phosphatidylcholine liposomes, reduced entry of VSV/Spike pseudovirions and 3) an established mutant of TIM-1 which does not bind to PS is unable to facilitate entry of SARS-CoV-2. As AXL is an abundant PS receptor on a number of airway lines, we evaluated small molecule inhibitors of AXL signaling such as bemcentinib for their ability to inhibit SARS-CoV-2 infection. Bemcentinib robustly inhibited virus infection of Vero E6 cells as well as multiple human lung cell lines that expressed AXL. This inhibition correlated well with inhibitors that block endosomal acidification and cathepsin activity, consistent with AXL-mediated uptake of SARS-CoV-2 into the endosomal compartment. We extended our observations to the related betacoronavirus mouse hepatitis virus (MHV), showing that inhibition or ablation of AXL reduces MHV infection of murine cells. In total, our findings provide evidence that PS receptors facilitate infection of the pandemic coronavirus SARS-CoV-2 and suggest that inhibition of the PS receptor AXL has therapeutic potential against SARS-CoV-2.
Mesh-Begriff(e)	Angiotensin-Converting Enzyme 2/physiology ; Animals ; COVID-19/drug therapy ; COVID-19/etiology ; Female ; HEK293 Cells ; Humans ; Mice ; Mice, Inbred C57BL ; Proto-Oncogene Proteins/physiology ; Receptor Protein-Tyrosine Kinases/physiology ; Receptors, Cell Surface/antagonists & inhibitors ; Receptors, Cell Surface/physiology ; SARS-CoV-2 ; Virus Internalization
Chemische Substanzen	Proto-Oncogene Proteins ; Receptors, Cell Surface ; phosphatidylserine receptor ; Receptor Protein-Tyrosine Kinases (EC 2.7.10.1) ; axl receptor tyrosine kinase (EC 2.7.10.1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Sprache	Englisch
Erscheinungsdatum	2021-11-19
Erscheinungsland	United States
Dokumenttyp	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.1009743
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Human Organotypic Airway and Lung Organoid Cells of Bronchiolar and Alveolar Differentiation Are Permissive to Infection by Influenza and SARS-CoV-2 Respiratory Virus.

Frontiers in cellular and infection microbiology

2022 Band 12, Seite(n) 841447

Abstract: The ongoing coronavirus disease 2019 (COVID-19) pandemic has led to the initiation of unprecedented research efforts to understand the pathogenesis mediated by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2). More knowledge is needed ... ...

Abstract	The ongoing coronavirus disease 2019 (COVID-19) pandemic has led to the initiation of unprecedented research efforts to understand the pathogenesis mediated by Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2). More knowledge is needed regarding the cell type-specific cytopathology and its impact on cellular tropism. Furthermore, the impact of novel SARS-CoV-2 mutations on cellular tropism, alternative routes of entry, the impact of co-infections, and virus replication kinetics along the respiratory tract remains to be explored in improved models. Most applied virology models are not well suited to address the remaining questions, as they do not recapitulate the histoarchitecture and cellular composition of human respiratory tissues. The overall aim of this work was to establish from single biopsy specimens, a human adult stem cell-derived organoid model representing the upper respiratory airways and lungs and explore the applicability of this model to study respiratory virus infection. First, we characterized the organoid model with respect to growth pattern and histoarchitecture, cellular composition, and functional characteristics. Next,
Mesh-Begriff(e)	Adult ; COVID-19 ; Humans ; Influenza A Virus, H5N1 Subtype ; Influenza A Virus, H7N1 Subtype ; Influenza, Human ; Lung ; Organoids ; SARS-CoV-2
Sprache	Englisch
Erscheinungsdatum	2022-03-14
Erscheinungsland	Switzerland
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2619676-1
ISSN	2235-2988 ; 2235-2988
ISSN (online)	2235-2988
ISSN	2235-2988
DOI	10.3389/fcimb.2022.841447
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Limited Variation between SARS-CoV-2-Infected Individuals in Domain Specificity and Relative Potency of the Antibody Response against the Spike Glycoprotein.

Microbiology spectrum

2022 Band 10, Heft 1, Seite(n) e0267621

Abstract: The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is arranged as a trimer on the virus surface, composed of three S1 and three S2 subunits. Infected and vaccinated individuals generate antibodies against spike, which can ... ...

Abstract	The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is arranged as a trimer on the virus surface, composed of three S1 and three S2 subunits. Infected and vaccinated individuals generate antibodies against spike, which can neutralize the virus. Most antibodies target the receptor-binding domain (RBD) and N-terminal domain (NTD) of S1; however, antibodies against other regions of spike have also been isolated. The interhost variability in domain specificity and relative neutralization efficacy of the antibodies is still poorly characterized. To this end, we tested serum and plasma samples collected from 85 coronavirus disease 2019 (COVID-19) convalescent subjects. Samples were analyzed using seven immunoassays that employ different domains, subunits, and oligomeric forms of spike to capture the antibodies. Samples were also tested for their neutralization of pseudovirus containing SARS-CoV-2 spike and of replication-competent SARS-CoV-2. While the total amount of anti-spike antibodies produced varied among convalescent subjects, we observed an unexpectedly fixed ratio of RBD- to NTD-targeting antibodies. The relative potency of the response (defined as the measured neutralization efficacy relative to the total level of spike-targeting antibodies) also exhibited limited variation between subjects and was not associated with the overall amount of antispike antibodies produced. These studies suggest that host-to-host variation in the polyclonal response elicited against SARS-CoV-2 spike in early pandemic subjects is primarily limited to the quantity of antibodies generated rather than their domain specificity or relative neutralization potency.
Mesh-Begriff(e)	Antibodies, Neutralizing/blood ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/blood ; Antibodies, Viral/immunology ; Antibody Formation ; COVID-19/blood ; COVID-19/immunology ; COVID-19/virology ; Enzyme-Linked Immunosorbent Assay ; Humans ; Neutralization Tests ; Protein Domains ; SARS-CoV-2/chemistry ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology
Chemische Substanzen	Antibodies, Neutralizing ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus
Sprache	Englisch
Erscheinungsdatum	2022-01-26
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2807133-5
ISSN	2165-0497 ; 2165-0497
ISSN (online)	2165-0497
ISSN	2165-0497
DOI	10.1128/spectrum.02676-21
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Phosphatidylserine Receptors Enhance SARS-CoV-2 Infection: AXL as a Therapeutic Target for COVID-19

Bohan, Dana / Van Ert, Hanora / Ruggio, Natalie / Rogers, Kai J. / Baddredine, Mohammad / Briseño, José A. A. / Rojas Chavez, Roberth Anthony / Gao, Boning / Stokowy, Tomasz / Christakou, Eleni / Micklem, David / Gausdal, Gro / Haim, Hillel / Minna, John / Lorens, James B. / Maury, Wendy

bioRxiv

Abstract	Phosphatidylserine (PS) receptors are PS binding proteins that mediate uptake of apoptotic bodies. Many enveloped viruses utilize this PS/PS receptor mechanism to adhere to and internalize into the endosomal compartment of cells and this is termed apoptotic mimicry. For viruses that have a mechanism(s) of endosomal escape, apoptotic mimicry is a productive route of virus entry. We evaluated if PS receptors serve as cell surface receptors for SARS-CoV-2 and found that the PS receptors, AXL, TIM-1 and TIM-4, facilitated virus infection when low concentrations of the SARS-CoV-2 cognate receptor, ACE2, was present. Consistent with the established mechanism of PS receptor utilization by other viruses, PS liposomes competed with SARS-CoV-2 for binding and entry. We demonstrated that this PS receptor enhances SARS-CoV-2 binding to and infection of an array of human lung cell lines and is an under-appreciated but potentially important host factor facilitating SARS-CoV-2 entry.
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2021-06-15
Verlag	Cold Spring Harbor Laboratory
Dokumenttyp	Artikel ; Online
DOI	10.1101/2021.06.15.448419
Datenquelle	COVID19

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