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Artikel ; Online: Sex differences in fear discrimination do not manifest as differences in conditioned inhibition.

Foilb, Allison R / Bals, Julia / Sarlitto, Mary C / Christianson, John P

Learning & memory (Cold Spring Harbor, N.Y.)

2017 Band 25, Heft 1, Seite(n) 49–53

Abstract: Distinguishing safety from danger is necessary for survival, but is aberrant in individuals with post-traumatic stress disorder (PTSD). While PTSD is more prevalent in women than men, research on sex differences in safety learning is limited. Here, ... ...

Abstract	Distinguishing safety from danger is necessary for survival, but is aberrant in individuals with post-traumatic stress disorder (PTSD). While PTSD is more prevalent in women than men, research on sex differences in safety learning is limited. Here, female rats demonstrated greater fear discrimination than males in a CS+/CS- paradigm. To determine if this sex difference transferred to fear inhibition, rats were tested for conditioned inhibition in a summation test with the CS+ and CS- presented in compound; no sex difference emerged. The results suggest sex differences in the neural mechanisms of discrimination learning but not recall of a fear inhibitor.
Mesh-Begriff(e)	Analysis of Variance ; Animals ; Conditioning (Psychology)/physiology ; Cues ; Discrimination (Psychology)/physiology ; Electroshock ; Fear/physiology ; Female ; Freezing Reaction, Cataleptic/physiology ; Generalization (Psychology)/physiology ; Inhibition (Psychology) ; Male ; Mental Recall/physiology ; Psychological Tests ; Rats, Sprague-Dawley ; Sex Characteristics
Sprache	Englisch
Erscheinungsdatum	2017-12-15
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1204777-6
ISSN	1549-5485 ; 1072-0502
ISSN (online)	1549-5485
ISSN	1072-0502
DOI	10.1101/lm.045500.117
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Mannose-binding lectin and complement mediate follicular localization and enhanced immunogenicity of diverse protein nanoparticle immunogens.

Read, Benjamin J / Won, Lori / Kraft, John C / Sappington, Isaac / Aung, Aereas / Wu, Shengwei / Bals, Julia / Chen, Chengbo / Lee, Kelly K / Lingwood, Daniel / King, Neil P / Irvine, Darrell J

Cell reports

2022 Band 38, Heft 2, Seite(n) 110217

Abstract: Nanoparticle (NP) vaccine formulations promote immune responses through multiple mechanisms. We recently reported that mannose-binding lectin (MBL) triggers trafficking of glycosylated HIV Env-immunogen NPs to lymph node follicles. Here, we investigate ... ...

Abstract	Nanoparticle (NP) vaccine formulations promote immune responses through multiple mechanisms. We recently reported that mannose-binding lectin (MBL) triggers trafficking of glycosylated HIV Env-immunogen NPs to lymph node follicles. Here, we investigate effects of MBL and complement on NP forms of HIV and other viral antigens. MBL recognition of oligomannose on gp120 nanoparticles significantly increases antigen accumulation in lymph nodes and antigen-specific germinal center (GC) responses. MBL and complement also mediate follicular trafficking and enhance GC responses to influenza, HBV, and HPV particulate antigens. Using model protein nanoparticles bearing titrated levels of glycosylation, we determine that mannose patches at a minimal density of 2.1 × 10
Mesh-Begriff(e)	Animals ; Antigens/metabolism ; Antigens, Viral/immunology ; Complement System Proteins/metabolism ; Drug Delivery Systems/methods ; Female ; Germinal Center/metabolism ; Glycosylation ; HIV-1/drug effects ; HIV-1/immunology ; Humans ; Immunity, Humoral/immunology ; Male ; Mannose ; Mannose-Binding Lectin/immunology ; Mice ; Mice, Inbred C57BL ; Nanoparticle Drug Delivery System/pharmacology ; Nanoparticles ; Polysaccharides/metabolism
Chemische Substanzen	Antigens ; Antigens, Viral ; Mannose-Binding Lectin ; Nanoparticle Drug Delivery System ; Polysaccharides ; Complement System Proteins (9007-36-7) ; Mannose (PHA4727WTP)
Sprache	Englisch
Erscheinungsdatum	2022-01-12
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2021.110217
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Eliciting a single amino acid change by vaccination generates antibody protection against group 1 and group 2 influenza A viruses.

Ray, Rashmi / Nait Mohamed, Faez Amokrane / Maurer, Daniel P / Huang, Jiachen / Alpay, Berk A / Ronsard, Larance / Xie, Zhenfei / Han, Julianna / Fernandez-Quintero, Monica / Phan, Quynh Anh / Ursin, Rebecca L / Vu, Mya / Kirsch, Kathrin H / Prum, Thavaleak / Rosado, Victoria C / Bracamonte-Moreno, Thalia / Okonkwo, Vintus / Bals, Julia / McCarthy, Caitlin /

Nair, Usha / Kanekiyo, Masaru / Ward, Andrew B / Schmidt, Aaron G / Batista, Facundo D / Lingwood, Daniel

Immunity

2024 Band 57, Heft 5, Seite(n) 1141–1159.e11

Abstract: Broadly neutralizing antibodies (bnAbs) targeting the hemagglutinin (HA) stem of influenza A viruses (IAVs) tend to be effective against either group 1 or group 2 viral diversity. In rarer cases, intergroup protective bnAbs can be generated by human ... ...

Abstract	Broadly neutralizing antibodies (bnAbs) targeting the hemagglutinin (HA) stem of influenza A viruses (IAVs) tend to be effective against either group 1 or group 2 viral diversity. In rarer cases, intergroup protective bnAbs can be generated by human antibody paratopes that accommodate the conserved glycan differences between the group 1 and group 2 stems. We applied germline-engaging nanoparticle immunogens to elicit a class of cross-group bnAbs from physiological precursor frequency within a humanized mouse model. Cross-group protection depended on the presence of the human bnAb precursors within the B cell repertoire, and the vaccine-expanded antibodies enriched for an N55T substitution in the CDRH2 loop, a hallmark of the bnAb class. Structurally, this single mutation introduced a flexible fulcrum to accommodate glycosylation differences and could alone enable cross-group protection. Thus, broad IAV immunity can be expanded from the germline repertoire via minimal antigenic input and an exceptionally simple antibody development pathway.
Mesh-Begriff(e)	Animals ; Mice ; Humans ; Antibodies, Viral/immunology ; Influenza Vaccines/immunology ; Influenza A virus/immunology ; Antibodies, Neutralizing/immunology ; Vaccination ; Orthomyxoviridae Infections/immunology ; Orthomyxoviridae Infections/prevention & control ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Amino Acid Substitution ; B-Lymphocytes/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Broadly Neutralizing Antibodies/immunology
Sprache	Englisch
Erscheinungsdatum	2024-04-25
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2024.03.022
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Naive human B cells engage the receptor binding domain of SARS-CoV-2, variants of concern, and related sarbecoviruses.

Feldman, Jared / Bals, Julia / Altomare, Clara G / St Denis, Kerri / Lam, Evan C / Hauser, Blake M / Ronsard, Larance / Sangesland, Maya / Moreno, Thalia Bracamonte / Okonkwo, Vintus / Hartojo, Nathania / Balazs, Alejandro B / Bajic, Goran / Lingwood, Daniel / Schmidt, Aaron G

bioRxiv : the preprint server for biology

2021

Abstract: Exposure to a pathogen elicits an adaptive immune response aimed to control and eradicate. Interrogating the abundance and specificity of the naive B cell repertoire contributes to understanding how to potentially elicit protective responses. Here, we ... ...

Abstract	Exposure to a pathogen elicits an adaptive immune response aimed to control and eradicate. Interrogating the abundance and specificity of the naive B cell repertoire contributes to understanding how to potentially elicit protective responses. Here, we isolated naive B cells from 8 seronegative human donors targeting the SARS-CoV-2 receptor-binding domain (RBD). Single B cell analysis showed diverse gene usage with no restricted complementarity determining region lengths. We show that recombinant antibodies engage SARS-CoV-2 RBD, circulating variants, and pre-emergent coronaviruses. Representative antibodies signal in a B cell activation assay and can be affinity matured through directed evolution. Structural analysis of a naive antibody in complex with spike shows a conserved mode of recognition shared with infection-induced antibodies. Lastly, both naive and affinity-matured antibodies can neutralize SARS-CoV-2. Understanding the naive repertoire may inform potential responses recognizing variants or emerging coronaviruses enabling the development of pan-coronavirus vaccines aimed at engaging germline responses.
Sprache	Englisch
Erscheinungsdatum	2021-07-09
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2021.02.02.429458
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Naive human B cells engage the receptor binding domain of SARS-CoV-2, variants of concern, and related sarbecoviruses.

Science immunology

2021 Band 6, Heft 66, Seite(n) eabl5842

Abstract: Initial exposure to a pathogen elicits an adaptive immune response to control and eradicate the threat. Interrogating the abundance and specificity of the naive B cell repertoire drives understanding of how to mount protective responses. Here, we ... ...

Abstract	Initial exposure to a pathogen elicits an adaptive immune response to control and eradicate the threat. Interrogating the abundance and specificity of the naive B cell repertoire drives understanding of how to mount protective responses. Here, we isolated naive B cells from eight seronegative human donors targeting the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) receptor binding domain (RBD). Single-cell B cell receptor (BCR) sequencing identified diverse gene usage and no restriction on complementarity determining region length. A subset of recombinant antibodies produced by naive B cell precursors bound to SARS-CoV-2 RBD and engaged circulating variants including B.1.1.7, B.1.351, and B.1.617.2, as well as preemergent bat-derived coronaviruses RaTG13, SHC104, and WIV1. By structural characterization of a naive antibody in complex with SARS-CoV-2 spike, we identified a conserved mode of recognition shared with infection-induced antibodies. We found that representative naive antibodies could signal in a B cell activation assay, and by using directed evolution, we could select for a higher-affinity RBD interaction, conferred by a single amino acid change. The minimally mutated, affinity-matured antibodies also potently neutralized SARS-CoV-2. Understanding the SARS-CoV-2 RBD–specific naive repertoire may inform potential responses capable of recognizing future SARS-CoV-2 variants or emerging coronaviruses, enabling the development of pan-coronavirus vaccines aimed at engaging protective germline responses.
Mesh-Begriff(e)	Antibodies, Neutralizing/immunology ; Antigens, Viral/immunology ; B-Lymphocytes/cytology ; B-Lymphocytes/immunology ; B-Lymphocytes/metabolism ; COVID-19/immunology ; COVID-19 Vaccines/immunology ; Coronavirus/immunology ; Epitopes ; Humans ; Lymphocyte Activation ; SARS-CoV-2/classification ; SARS-CoV-2/immunology ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/metabolism
Chemische Substanzen	Antibodies, Neutralizing ; Antigens, Viral ; COVID-19 Vaccines ; Epitopes ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Sprache	Englisch
Erscheinungsdatum	2021-12-10
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2470-9468
ISSN (online)	2470-9468
DOI	10.1126/sciimmunol.abl5842
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Naive human B cells can neutralize SARS-CoV-2 through recognition of its receptor binding domain

Feldman, Jared / Bals, Julia / Denis, Kerri St. / Lam, Evan C. / Hauser, Blake M. / Ronsard, Larance / Sangesland, Maya / Moreno, Thalia Bracamonte / Okonkwo, Vintus / Hartojo, Nathania / Balazs, Alejandro B. / Lingwood, Daniel / Schmidt, Aaron G.

bioRxiv

Abstract: Exposure to a pathogen elicits an adaptive immune response aimed to control and eradicate. This initial exposure is imprinted on the immune system, so that a subsequent encounter to the same pathogen or a variant will result in a memory recall response ... ...

Abstract	Exposure to a pathogen elicits an adaptive immune response aimed to control and eradicate. This initial exposure is imprinted on the immune system, so that a subsequent encounter to the same pathogen or a variant will result in a memory recall response that is often protective. Interrogating the naive B cell repertoire in terms of both abundance and specificity to said pathogen may contribute to an understanding of how to potentially elicit protective responses. Here, we isolated naive B cells across 8 human donors, targeting the SARS-CoV-2 receptor-binding domain (RBD). Single B cell sorting, and subsequent sequence analysis, showed diverse gene usage and pairing with no apparent restriction on complementarity determining region length in either the heavy or light chains. We show that recombinantly expressed IgGs and Fabs of these germline precursors bind SARS-CoV-2 RBD. Importantly, a subset of these naive antibodies also bind SARS-CoV, an emergent variant (501Y.V2) and a potential pandemic (WIV-1) coronavirus. Furthermore, naive antibodies can also neutralize SARS-CoV-2 pseudoviruses in the absence of any somatic hypermutation, suggesting that protective immunity to coronaviruses, more broadly, may be genetically encoded. Future studies aimed at understanding the naive repertoire to other coronaviruses may ultimately reveal shared specificities that could be leveraged to develop pan-coronavirus vaccines aimed at priming encoded germline responses.
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2021-02-10
Verlag	Cold Spring Harbor Laboratory
Dokumenttyp	Artikel ; Online
DOI	10.1101/2021.02.02.429458
Datenquelle	COVID19

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Artikel ; Online: Spontaneous Glycan Reattachment Following N-Glycanase Treatment of Influenza and HIV Vaccine Antigens.

Keating, Celina L / Kuhn, Eric / Bals, Julia / Cocco, Alexandra R / Yousif, Ashraf S / Matysiak, Colette / Sangesland, Maya / Ronsard, Larance / Smoot, Matthew / Moreno, Thalia Bracamonte / Okonkwo, Vintus / Setliff, Ian / Georgiev, Ivelin / Balazs, Alejandro B / Carr, Steven A / Lingwood, Daniel

Journal of proteome research

2020 Band 19, Heft 2, Seite(n) 733–743

Abstract: In cells, asparagine/N-linked glycans are added to glycoproteins cotranslationally, in an attachment process that supports proper folding of the nascent polypeptide. We found that following pruning ... ...

Abstract	In cells, asparagine/N-linked glycans are added to glycoproteins cotranslationally, in an attachment process that supports proper folding of the nascent polypeptide. We found that following pruning of
Mesh-Begriff(e)	AIDS Vaccines ; HIV Antigens ; Humans ; Influenza Vaccines ; Influenza, Human ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase ; Polysaccharides
Chemische Substanzen	AIDS Vaccines ; HIV Antigens ; Influenza Vaccines ; Polysaccharides ; Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase (EC 3.5.1.52)
Sprache	Englisch
Erscheinungsdatum	2020-01-24
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2078618-9
ISSN	1535-3907 ; 1535-3893
ISSN (online)	1535-3907
ISSN	1535-3893
DOI	10.1021/acs.jproteome.9b00620
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Germline-Encoded Affinity for Cognate Antigen Enables Vaccine Amplification of a Human Broadly Neutralizing Response against Influenza Virus.

Sangesland, Maya / Ronsard, Larance / Kazer, Samuel W / Bals, Julia / Boyoglu-Barnum, Seyhan / Yousif, Ashraf S / Barnes, Ralston / Feldman, Jared / Quirindongo-Crespo, Maricel / McTamney, Patrick M / Rohrer, Daniel / Lonberg, Nils / Chackerian, Bryce / Graham, Barney S / Kanekiyo, Masaru / Shalek, Alex K / Lingwood, Daniel

Immunity

2019 Band 51, Heft 4, Seite(n) 735–749.e8

Abstract: Antibody paratopes are formed by hypervariable complementarity-determining regions (CDRH3s) and variable gene-encoded CDRs. The latter show biased usage in human broadly neutralizing antibodies (bnAbs) against both HIV and influenza virus, suggesting the ...

Abstract	Antibody paratopes are formed by hypervariable complementarity-determining regions (CDRH3s) and variable gene-encoded CDRs. The latter show biased usage in human broadly neutralizing antibodies (bnAbs) against both HIV and influenza virus, suggesting the existence of gene-endowed targeting solutions that may be amenable to pathway amplification. To test this, we generated transgenic mice with human CDRH3 diversity but simultaneously constrained to individual user-defined human immunoglobulin variable heavy-chain (V
Mesh-Begriff(e)	Animals ; Antibodies, Viral/genetics ; Antibodies, Viral/metabolism ; Antibody Affinity ; B-Lymphocytes/immunology ; Broadly Neutralizing Antibodies/genetics ; Broadly Neutralizing Antibodies/metabolism ; Complementarity Determining Regions/genetics ; Germ-Line Mutation/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Humans ; Immunity, Humoral ; Immunization, Secondary ; Immunoglobulin Heavy Chains/genetics ; Influenza A virus/physiology ; Influenza Vaccines/immunology ; Influenza, Human/immunology ; Mice ; Mice, Transgenic ; Nanoparticles ; Protein Engineering ; Receptors, Antigen, B-Cell/genetics
Chemische Substanzen	Antibodies, Viral ; Broadly Neutralizing Antibodies ; Complementarity Determining Regions ; Hemagglutinin Glycoproteins, Influenza Virus ; Immunoglobulin Heavy Chains ; Influenza Vaccines ; Receptors, Antigen, B-Cell ; hemagglutinin, human influenza A virus
Sprache	Englisch
Erscheinungsdatum	2019-09-25
Erscheinungsland	United States
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	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2019.09.001
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: A particulate saponin/TLR agonist vaccine adjuvant alters lymph flow and modulates adaptive immunity.

Silva, Murillo / Kato, Yu / Melo, Mariane B / Phung, Ivy / Freeman, Brian L / Li, Zhongming / Roh, Kangsan / Van Wijnbergen, Jan W / Watkins, Hannah / Enemuo, Chiamaka A / Hartwell, Brittany L / Chang, Jason Y H / Xiao, Shuhao / Rodrigues, Kristen A / Cirelli, Kimberly M / Li, Na / Haupt, Sonya / Aung, Aereas / Cossette, Benjamin /

Science immunology

2021 Band 6, Heft 66, Seite(n) eabf1152

Abstract: Saponins are potent and safe vaccine adjuvants, but their mechanisms of action remain incompletely understood. Here, we explored the properties of several saponin formulations, including immune-stimulatory complexes (ISCOMs) formed by the self-assembly ... ...

Abstract	Saponins are potent and safe vaccine adjuvants, but their mechanisms of action remain incompletely understood. Here, we explored the properties of several saponin formulations, including immune-stimulatory complexes (ISCOMs) formed by the self-assembly of saponin and phospholipids in the absence or presence of the Toll-like receptor 4 agonist monophosphoryl lipid A (MPLA). We found that MPLA self-assembles with saponins to form particles physically resembling ISCOMs, which we termed saponin/MPLA nanoparticles (SMNP). Saponin-containing adjuvants exhibited distinctive mechanisms of action, altering lymph flow in a mast cell–dependent manner and promoting antigen entry into draining lymph nodes. SMNP was particularly effective, exhibiting even greater potency than the compositionally related adjuvant AS01
Mesh-Begriff(e)	Adaptive Immunity/drug effects ; Adjuvants, Immunologic/pharmacology ; Animals ; B-Lymphocytes/immunology ; CD4-Positive T-Lymphocytes/immunology ; Female ; Lymph/drug effects ; Lymph/physiology ; Macaca mulatta ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Nanoparticles ; Rats ; Rats, Wistar ; Saponins/pharmacology ; Toll-Like Receptors/agonists
Chemische Substanzen	Adjuvants, Immunologic ; Saponins ; Toll-Like Receptors
Sprache	Englisch
Erscheinungsdatum	2021-12-03
Erscheinungsland	United States
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.
ISSN	2470-9468
ISSN (online)	2470-9468
DOI	10.1126/sciimmunol.abf1152
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: SARS-CoV-2 Receptor ACE2 Is an Interferon-Stimulated Gene in Human Airway Epithelial Cells and Is Detected in Specific Cell Subsets across Tissues

Ziegler, Carly G.K. / Allon, Samuel J. / Nyquist, Sarah K. / Mbano, Ian M. / Miao, Vincent N. / Tzouanas, Constantine N. / Cao, Yuming / Yousif, Ashraf S. / Bals, Julia / Hauser, Blake M. / Feldman, Jared / Muus, Christoph / Wadsworth, Marc H. / Kazer, Samuel W. / Hughes, Travis K. / Doran, Benjamin / Gatter, G. James / Vukovic, Marko / Taliaferro, Faith /

Mead, Benjamin E. / Guo, Zhiru / Wang, Jennifer P. / Gras, Delphine / Plaisant, Magali / Ansari, Meshal / Angelidis, Ilias / Adler, Heiko / Sucre, Jennifer M.S. / Taylor, Chase J. / Lin, Brian / Waghray, Avinash

2020

Abstract: There is pressing urgency to understand the pathogenesis of the severe acute respiratory syndrome coronavirus clade 2 (SARS-CoV-2), which causes the disease COVID-19. SARS-CoV-2 spike (S) protein binds angiotensin-converting enzyme 2 (ACE2), and in ... ...

Abstract	There is pressing urgency to understand the pathogenesis of the severe acute respiratory syndrome coronavirus clade 2 (SARS-CoV-2), which causes the disease COVID-19. SARS-CoV-2 spike (S) protein binds angiotensin-converting enzyme 2 (ACE2), and in concert with host proteases, principally transmembrane serine protease 2 (TMPRSS2), promotes cellular entry. The cell subsets targeted by SARS-CoV-2 in host tissues and the factors that regulate ACE2 expression remain unknown. Here, we leverage human, non-human primate, and mouse single-cell RNA-sequencing (scRNA-seq) datasets across health and disease to uncover putative targets of SARS-CoV-2 among tissue-resident cell subsets. We identify ACE2 and TMPRSS2 co-expressing cells within lung type II pneumocytes, ileal absorptive enterocytes, and nasal goblet secretory cells. Strikingly, we discovered that ACE2 is a human interferon-stimulated gene (ISG) in vitro using airway epithelial cells and extend our findings to in vivo viral infections. Our data suggest that SARS-CoV-2 could exploit species-specific interferon-driven upregulation of ACE2, a tissue-protective mediator during lung injury, to enhance infection.Analysis of single-cell RNA-seq datasets from human, non-human primate, and mouse barrier tissues identifies putative cellular targets of SARS-CoV-2 on the basis of ACE2 and TMPRSS2 expression. ACE2 represents a previously unappreciated interferon-stimulated gene in human, but not mouse, epithelial tissues, identifying anti-viral induction of a host tissue-protective mechanism, but also a potential means for viral exploitation of the host response.
Schlagwörter	ACE2 ; COVID-19 ; human ; influenza ; interferon ; ISG ; mouse ; non-human primate ; SARS-CoV-2 ; scRNA-seq ; 1300 Biochemistry ; Genetics and Molecular Biology ; covid19
Sprache	Englisch
Erscheinungsdatum	2020-01-01
Verlag	Cell Press
Erscheinungsland	au
Dokumenttyp	Artikel ; Online
Datenquelle	BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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