LIVIVO - Search results -

Search results

Result 1 - 10 of total 19

Search options

Article ; Online: Broad sarbecovirus neutralization by a human monoclonal antibody.

Tortorici, M Alejandra / Czudnochowski, Nadine / Starr, Tyler N / Marzi, Roberta / Walls, Alexandra C / Zatta, Fabrizia / Bowen, John E / Jaconi, Stefano / Di Iulio, Julia / Wang, Zhaoqian / De Marco, Anna / Zepeda, Samantha K / Pinto, Dora / Liu, Zhuoming / Beltramello, Martina / Bartha, Istvan / Housley, Michael P / Lempp, Florian A / Rosen, Laura E /

Dellota, Exequiel / Kaiser, Hannah / Montiel-Ruiz, Martin / Zhou, Jiayi / Addetia, Amin / Guarino, Barbara / Culap, Katja / Sprugasci, Nicole / Saliba, Christian / Vetti, Eneida / Giacchetto-Sasselli, Isabella / Fregni, Chiara Silacci / Abdelnabi, Rana / Foo, Shi-Yan Caroline / Havenar-Daughton, Colin / Schmid, Michael A / Benigni, Fabio / Cameroni, Elisabetta / Neyts, Johan / Telenti, Amalio / Virgin, Herbert W / Whelan, Sean P J / Snell, Gyorgy / Bloom, Jesse D / Corti, Davide / Veesler, David / Pizzuto, Matteo Samuele

Nature

2021 Volume 597, Issue 7874, Page(s) 103–108

Abstract: The recent emergence of SARS-CoV-2 variants of ... ...

Abstract	The recent emergence of SARS-CoV-2 variants of concern
MeSH term(s)	Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Antibodies, Viral/therapeutic use ; Broadly Neutralizing Antibodies/chemistry ; Broadly Neutralizing Antibodies/immunology ; Broadly Neutralizing Antibodies/therapeutic use ; COVID-19/immunology ; COVID-19/prevention & control ; COVID-19/virology ; Cross Reactions/immunology ; Disease Models, Animal ; Female ; Humans ; Immune Evasion/genetics ; Immune Evasion/immunology ; Mesocricetus/immunology ; Mesocricetus/virology ; Mutation ; Neutralization Tests ; SARS-CoV-2/chemistry ; SARS-CoV-2/classification ; SARS-CoV-2/genetics ; SARS-CoV-2/immunology ; Viral Zoonoses/immunology ; Viral Zoonoses/prevention & control ; Viral Zoonoses/virology
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Viral ; Broadly Neutralizing Antibodies
Language	English
Publishing date	2021-07-19
Publishing country	England
Document type	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	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-021-03817-4
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 9: Show issues
Zs.MO 244: Show issues

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article: Structural basis for broad sarbecovirus neutralization by a human monoclonal antibody.

Tortorici, M Alejandra / Czudnochowski, Nadine / Starr, Tyler N / Marzi, Roberta / Walls, Alexandra C / Zatta, Fabrizia / Bowen, John E / Jaconi, Stefano / di Iulio, Julia / Wang, Zhaoqian / De Marco, Anna / Zepeda, Samantha K / Pinto, Dora / Liu, Zhuoming / Beltramello, Martina / Bartha, Istvan / Housley, Michael P / Lempp, Florian A / Rosen, Laura E /

Dellota, Exequiel / Kaiser, Hannah / Montiel-Ruiz, Martin / Zhou, Jiayi / Addetia, Amin / Guarino, Barbara / Culap, Katja / Sprugasci, Nicole / Saliba, Christian / Vetti, Eneida / Giacchetto-Sasselli, Isabella / Silacci Fregni, Chiara / Abdelnabi, Rana / Caroline Foo, Shi-Yan / Havenar-Daughton, Colin / Schmid, Michael A / Benigni, Fabio / Cameroni, Elisabetta / Neyts, Johan / Telenti, Amalio / Snell, Gyorgy / Virgin, Herbert W / Whelan, Sean P J / Bloom, Jesse D / Corti, Davide / Veesler, David / Pizzuto, Matteo Samuele

bioRxiv : the preprint server for biology

2021

Abstract: ... we describe a human monoclonal antibody (mAb), designated S2X259, recognizing a highly conserved cryptic ... of coronaviruses in the human population highlight the need for broadly neutralizing antibodies that are not ... 429 VOC, as well as a wide spectrum of human and zoonotic sarbecoviruses through inhibition of ACE2 ...

Abstract	The recent emergence of SARS-CoV-2 variants of concern (VOC) and the recurrent spillovers of coronaviruses in the human population highlight the need for broadly neutralizing antibodies that are not affected by the ongoing antigenic drift and that can prevent or treat future zoonotic infections. Here, we describe a human monoclonal antibody (mAb), designated S2X259, recognizing a highly conserved cryptic receptor-binding domain (RBD) epitope and cross-reacting with spikes from all sarbecovirus clades. S2X259 broadly neutralizes spike-mediated entry of SARS-CoV-2 including the B.1.1.7, B.1.351, P.1 and B.1.427/B.1.429 VOC, as well as a wide spectrum of human and zoonotic sarbecoviruses through inhibition of ACE2 binding to the RBD. Furthermore, deep-mutational scanning and
Language	English
Publishing date	2021-04-08
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.04.07.438818
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Structural basis for broad sarbecovirus neutralization by a human monoclonal antibody

Tortorici, M. Alejandra / Czudnochowski, Nadine / Starr, Tyler N / Marzi, Roberta / Walls, Alexandra C. / Zatta, Fabrizia / Bowen, John E. / Jaconi, Stefano / di Iulio, Julia / Wang, Zhaoqian / De Marco, Anna / Zepeda, Samantha / Pinto, Dora / Liu, Zhuoming / Beltramello, Martina / Bartha, Istvan / Housley, Michael P. / Lempp, Florian A / Rosen, Laura E. /

Dellota, Exequiel / Kaiser, Hanna / Montiel-Ruiz, Martin / Zhou, Jiayi / Addetia, Amin / Guarino, Barbara / Culap, Katja / Sprugasci, Nicole / Saliba, Christian / Vetti, Eneida / Giacchetto-Sasselli, Isabella / Silacci Fregni, Chiara / Abdelnabi, Rana / Foo, Caroline Shi-Yan / Havenar-Daughton, Colin / Schmid, Michael A / Benigni, Fabio / Cameroni, Elisabetta / Neyts, Johan / Telenti, Amalio / Snell, Gyorgy / Virgin, Herbert W / Whelan, Sean P. J. / Bloom, Jesse D / Corti, Davide / Veesler, David / Pizzuto, Matteo Samuele

bioRxiv

Abstract	The recent emergence of SARS-CoV-2 variants of concern (VOC) and the recurrent spillovers of coronaviruses in the human population highlight the need for broadly neutralizing antibodies that are not affected by the ongoing antigenic drift and that can prevent or treat future zoonotic infections. Here, we describe a human monoclonal antibody (mAb), designated S2X259, recognizing a highly conserved cryptic receptor-binding domain (RBD) epitope and cross-reacting with spikes from all sarbecovirus clades. S2X259 broadly neutralizes spike-mediated entry of SARS-CoV-2 including the B.1.1.7, B.1.351, P.1 and B.1.427/B.1.429 VOC, as well as a wide spectrum of human and zoonotic sarbecoviruses through inhibition of ACE2 binding to the RBD. Furthermore, deep-mutational scanning and in vitro escape selection experiments demonstrate that S2X259 possesses a remarkably high barrier to the emergence of resistance mutants. We show that prophylactic administration of S2X259 protects Syrian hamsters against challenges with the prototypic SARS-CoV-2 and the B.1.351 variant, suggesting this mAb is a promising candidate for the prevention and treatment of emergent VOC and zoonotic infections. Our data unveil a key antigenic site targeted by broadly-neutralizing antibodies and will guide the design of pan-sarbecovirus vaccines.
Keywords	covid19
Language	English
Publishing date	2021-04-08
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.04.07.438818
Database	COVID19

Full text online

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Broad receptor tropism and immunogenicity of a clade 3 sarbecovirus.

Lee, Jimin / Zepeda, Samantha K / Park, Young-Jun / Taylor, Ashley L / Quispe, Joel / Stewart, Cameron / Leaf, Elizabeth M / Treichel, Catherine / Corti, Davide / King, Neil P / Starr, Tyler N / Veesler, David

Cell host & microbe

2023 Volume 31, Issue 12, Page(s) 1961–1973.e11

Abstract: ... we show that the African Rhinolophus bat clade 3 sarbecovirus PRD-0038 S has a broad angiotensin ... CoV-2. Characterization of PRD-0038 S using cryo-EM and monoclonal antibody reactivity reveals ... promiscuity and enable human ACE2 utilization. We determine a cryo-EM structure of the PRD-0038 RBD bound ...

Abstract	Although Rhinolophus bats harbor diverse clade 3 sarbecoviruses, the structural determinants of receptor tropism along with the antigenicity of their spike (S) glycoproteins remain uncharacterized. Here, we show that the African Rhinolophus bat clade 3 sarbecovirus PRD-0038 S has a broad angiotensin-converting enzyme 2 (ACE2) usage and that receptor-binding domain (RBD) mutations further expand receptor promiscuity and enable human ACE2 utilization. We determine a cryo-EM structure of the PRD-0038 RBD bound to Rhinolophus alcyone ACE2, explaining receptor tropism and highlighting differences with SARS-CoV-1 and SARS-CoV-2. Characterization of PRD-0038 S using cryo-EM and monoclonal antibody reactivity reveals its distinct antigenicity relative to SARS-CoV-2 and identifies PRD-0038 cross-neutralizing antibodies for pandemic preparedness. PRD-0038 S vaccination elicits greater titers of antibodies cross-reacting with vaccine-mismatched clade 2 and clade 1a sarbecoviruses compared with SARS-CoV-2 S due to broader antigenic targeting, motivating the inclusion of clade 3 antigens in next-generation vaccines for enhanced resilience to viral evolution.
MeSH term(s)	Animals ; Humans ; Angiotensin-Converting Enzyme 2 ; Severe acute respiratory syndrome-related coronavirus ; Chiroptera ; SARS-CoV-2/genetics ; Tropism ; Spike Glycoprotein, Coronavirus ; Antibodies, Viral
Chemical Substances	Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; Spike Glycoprotein, Coronavirus ; Antibodies, Viral
Language	English
Publishing date	2023-11-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2278004-X
ISSN	1934-6069 ; 1931-3128
ISSN (online)	1934-6069
ISSN	1931-3128
DOI	10.1016/j.chom.2023.10.018
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 6578: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry.

Park, Young-Jun / De Marco, Anna / Starr, Tyler N / Liu, Zhuoming / Pinto, Dora / Walls, Alexandra C / Zatta, Fabrizia / Zepeda, Samantha K / Bowen, John E / Sprouse, Kaitlin R / Joshi, Anshu / Giurdanella, Martina / Guarino, Barbara / Noack, Julia / Abdelnabi, Rana / Foo, Shi-Yan Caroline / Rosen, Laura E / Lempp, Florian A / Benigni, Fabio /

Snell, Gyorgy / Neyts, Johan / Whelan, Sean P J / Virgin, Herbert W / Bloom, Jesse D / Corti, Davide / Pizzuto, Matteo Samuele / Veesler, David

Science (New York, N.Y.)

2022 Volume 375, Issue 6579, Page(s) 449–454

Abstract: ... characterization of a human monoclonal antibody, designated S2K146, that broadly neutralizes viruses belonging ... Understanding broadly neutralizing sarbecovirus antibody responses is key to developing ... vaccines eliciting broad sarbecovirus immunity. ...

Abstract	Understanding broadly neutralizing sarbecovirus antibody responses is key to developing countermeasures against SARS-CoV-2 variants and future zoonotic sarbecoviruses. We describe the isolation and characterization of a human monoclonal antibody, designated S2K146, that broadly neutralizes viruses belonging to SARS-CoV- and SARS-CoV-2-related sarbecovirus clades which use ACE2 as an entry receptor. Structural and functional studies show that most of the virus residues that directly bind S2K146 are also involved in binding to ACE2. This allows the antibody to potently inhibit receptor attachment. S2K146 protects against SARS-CoV-2 Beta challenge in hamsters and viral passaging experiments reveal a high barrier for emergence of escape mutants, making it a good candidate for clinical development. The conserved ACE2-binding residues present a site of vulnerability that might be leveraged for developing vaccines eliciting broad sarbecovirus immunity.
MeSH term(s)	Angiotensin-Converting Enzyme 2/chemistry ; Angiotensin-Converting Enzyme 2/metabolism ; Animals ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/metabolism ; Antibodies, Monoclonal/therapeutic use ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Antibody Affinity ; Betacoronavirus/immunology ; Broadly Neutralizing Antibodies/chemistry ; Broadly Neutralizing Antibodies/immunology ; Broadly Neutralizing Antibodies/metabolism ; Broadly Neutralizing Antibodies/therapeutic use ; COVID-19/immunology ; COVID-19/therapy ; Cross Reactions ; Cryoelectron Microscopy ; Epitopes ; Humans ; Immune Evasion ; Mesocricetus ; Models, Molecular ; Molecular Mimicry ; Mutation ; Protein Conformation ; Protein Domains ; Receptors, Coronavirus/chemistry ; Receptors, Coronavirus/metabolism ; SARS-CoV-2/immunology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Viral ; Broadly Neutralizing Antibodies ; Epitopes ; Receptors, Coronavirus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Language	English
Publishing date	2022-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abm8143
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 77: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Broad receptor tropism and immunogenicity of a clade 3 sarbecovirus

Lee, Jimin / Zepeda, Samantha / Park, Young-Jun / Taylor, Ashley L / Quispe, Joel / Stewart, Cameron / Leaf, Elizabeth M / Treichel, Catherine / Corti, Davide / King, Neil P / Starr, Tyler N / Veesler, David

bioRxiv

Abstract: ... we show that the African Rinolophus bat clade 3 sarbecovirus PRD-0038 S has a broad ACE2 usage and ... monoclonal antibody reactivity revealed its distinct antigenicity relative to SARS-CoV-2 and identified PRD-0038 cross ... that RBD mutations further expand receptor promiscuity and enable human ACE2 utilization. We determined ...

Abstract	Although Rhinolophus bats harbor diverse clade 3 sarbecoviruses, the structural determinants of receptor tropism along with the antigenicity of their spike (S) glycoproteins remain uncharacterized. Here, we show that the African Rinolophus bat clade 3 sarbecovirus PRD-0038 S has a broad ACE2 usage and that RBD mutations further expand receptor promiscuity and enable human ACE2 utilization. We determined a cryoEM structure of the PRD-0038 RBD bound to R. alcyone ACE2, explaining receptor tropism and highlighting differences with SARS-CoV-1 and SARS-CoV-2. Characterization of PRD-0038 S using cryoEM and monoclonal antibody reactivity revealed its distinct antigenicity relative to SARS-CoV-2 and identified PRD-0038 cross-neutralizing antibodies for pandemic preparedness. PRD-0038 S vaccination elicited greater titers of antibodies cross-reacting with vaccine-mismatched clade 2 and clade 1a sarbecoviruses compared to SARS-CoV-2 S due to broader antigenic targeting, motivating the inclusion of clade 3 antigens in next-generation vaccines for enhanced resilience to viral evolution.
Keywords	covid19
Language	English
Publishing date	2023-09-13
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2023.09.12.557371
Database	COVID19

Full text online

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry.

Park, Young-Jun / De Marco, Anna / Starr, Tyler N / Liu, Zhuoming / Pinto, Dora / Walls, Alexandra C / Zatta, Fabrizia / Zepeda, Samantha K / Bowen, John / Sprouse, Kaitlin S / Joshi, Anshu / Giurdanella, Martina / Guarino, Barbara / Noack, Julia / Abdelnabi, Rana / Foo, Shi-Yan Caroline / Lempp, Florian A / Benigni, Fabio / Snell, Gyorgy /

Neyts, Johan / Whelan, Sean Pj / Virgin, Herbert W / Bloom, Jesse D / Corti, Davide / Pizzuto, Matteo Samuele / Veesler, David

bioRxiv : the preprint server for biology

2021

Abstract: Understanding broadly neutralizing sarbecovirus antibody responses is key to developing ... we describe the isolation and characterization of a human monoclonal antibody, designated S2K146, broadly ... neutralizing viruses belonging to all three sarbecovirus clades known to utilize ACE2 as entry receptor and ...

Abstract	Understanding broadly neutralizing sarbecovirus antibody responses is key to developing countermeasures effective against SARS-CoV-2 variants and future spillovers of other sarbecoviruses. Here we describe the isolation and characterization of a human monoclonal antibody, designated S2K146, broadly neutralizing viruses belonging to all three sarbecovirus clades known to utilize ACE2 as entry receptor and protecting therapeutically against SARS-CoV-2 beta challenge in hamsters. Structural and functional studies show that most of the S2K146 epitope residues are shared with the ACE2 binding site and that the antibody inhibits receptor attachment competitively. Viral passaging experiments underscore an unusually high barrier for emergence of escape mutants making it an ideal candidate for clinical development. These findings unveil a key site of vulnerability for the development of a next generation of vaccines eliciting broad sarbecovirus immunity.
Language	English
Publishing date	2021-10-14
Publishing country	United States
Document type	Preprint
DOI	10.1101/2021.10.13.464254
Database	MEDical Literature Analysis and Retrieval System OnLINE

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾

Article ; Online: Modular adjuvant-free pan-HLA-DR-immunotargeting subunit vaccine against SARS-CoV-2 elicits broad sarbecovirus-neutralizing antibody responses.

Kassardjian, Audrey / Sun, Eric / Sookhoo, Jamie / Muthuraman, Krithika / Boligan, Kayluz Frias / Kucharska, Iga / Rujas, Edurne / Jetha, Arif / Branch, Donald R / Babiuk, Shawn / Barber, Brian / Julien, Jean-Philippe

Cell reports

2023 Volume 42, Issue 4, Page(s) 112391

Abstract: ... broad sarbecovirus neutralization. Our findings support anti-HLA-DR immunotargeting as an effective ... ITV) that leverages the pan-HLA-DR monoclonal antibody 44H10 to deliver the viral spike protein ... immunization in rabbits and ferrets induces robust anti-RBD antibody responses that neutralize SARS-CoV-2 ...

Abstract	Subunit vaccines typically require co-administration with an adjuvant to elicit protective immunity, adding development hurdles that can impede rapid pandemic responses. To circumvent the need for adjuvant in a severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) subunit vaccine, we engineer a thermostable immunotargeting vaccine (ITV) that leverages the pan-HLA-DR monoclonal antibody 44H10 to deliver the viral spike protein receptor-binding domain (RBD) to antigen-presenting cells. X-ray crystallography shows that 44H10 binds to a conserved epitope on HLA-DR, providing the basis for its broad HLA-DR reactivity. Adjuvant-free ITV immunization in rabbits and ferrets induces robust anti-RBD antibody responses that neutralize SARS-CoV-2 variants of concern and protect recipients from SARS-CoV-2 challenge. We demonstrate that the modular nature of the ITV scaffold with respect to helper T cell epitopes and diverse RBD antigens facilitates broad sarbecovirus neutralization. Our findings support anti-HLA-DR immunotargeting as an effective means to induce strong antibody responses to subunit antigens without requiring an adjuvant.
MeSH term(s)	Animals ; Humans ; Rabbits ; SARS-CoV-2 ; COVID-19 Vaccines ; Antibodies, Viral ; Broadly Neutralizing Antibodies ; Severe acute respiratory syndrome-related coronavirus ; COVID-19/prevention & control ; Ferrets ; Adjuvants, Immunologic ; Receptors, Virus/metabolism ; HLA-DR Antigens ; Vaccines, Subunit ; Antibodies, Neutralizing
Chemical Substances	COVID-19 Vaccines ; Antibodies, Viral ; Broadly Neutralizing Antibodies ; Adjuvants, Immunologic ; Receptors, Virus ; HLA-DR Antigens ; Vaccines, Subunit ; Antibodies, Neutralizing
Language	English
Publishing date	2023-04-03
Publishing country	United States
Document type	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	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.112391
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Broad neutralization of SARS-related viruses by human monoclonal antibodies.

Wec, Anna Z / Wrapp, Daniel / Herbert, Andrew S / Maurer, Daniel P / Haslwanter, Denise / Sakharkar, Mrunal / Jangra, Rohit K / Dieterle, M Eugenia / Lilov, Asparouh / Huang, Deli / Tse, Longping V / Johnson, Nicole V / Hsieh, Ching-Lin / Wang, Nianshuang / Nett, Juergen H / Champney, Elizabeth / Burnina, Irina / Brown, Michael / Lin, Shu /

Sinclair, Melanie / Johnson, Carl / Pudi, Sarat / Bortz, Robert / Wirchnianski, Ariel S / Laudermilch, Ethan / Florez, Catalina / Fels, J Maximilian / O'Brien, Cecilia M / Graham, Barney S / Nemazee, David / Burton, Dennis R / Baric, Ralph S / Voss, James E / Chandran, Kartik / Dye, John M / McLellan, Jason S / Walker, Laura M

Science (New York, N.Y.)

2020 Volume 369, Issue 6504, Page(s) 731–736

Abstract: Broadly protective vaccines against known and preemergent human coronaviruses (HCoVs) are urgently ... needed. To gain a deeper understanding of cross-neutralizing antibody responses, we mined the memory B ... of pan-sarbecovirus vaccines. ...

Abstract	Broadly protective vaccines against known and preemergent human coronaviruses (HCoVs) are urgently needed. To gain a deeper understanding of cross-neutralizing antibody responses, we mined the memory B cell repertoire of a convalescent severe acute respiratory syndrome (SARS) donor and identified 200 SARS coronavirus 2 (SARS-CoV-2) binding antibodies that target multiple conserved sites on the spike (S) protein. A large proportion of the non-neutralizing antibodies display high levels of somatic hypermutation and cross-react with circulating HCoVs, suggesting recall of preexisting memory B cells elicited by prior HCoV infections. Several antibodies potently cross-neutralize SARS-CoV, SARS-CoV-2, and the bat SARS-like virus WIV1 by blocking receptor attachment and inducing S1 shedding. These antibodies represent promising candidates for therapeutic intervention and reveal a target for the rational design of pan-sarbecovirus vaccines.
MeSH term(s)	Adult ; Aged ; Angiotensin-Converting Enzyme 2 ; Antibodies, Monoclonal/immunology ; Antibodies, Viral/immunology ; Antibody Affinity ; B-Lymphocyte Subsets/immunology ; Betacoronavirus/immunology ; Binding Sites ; Broadly Neutralizing Antibodies/immunology ; Cross Reactions ; Epitopes ; Female ; Humans ; Immunologic Memory ; Male ; Middle Aged ; Neutralization Tests ; Peptidyl-Dipeptidase A/chemistry ; Peptidyl-Dipeptidase A/metabolism ; Protein Domains ; Receptors, Coronavirus ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; Severe acute respiratory syndrome-related coronavirus/immunology ; SARS-CoV-2 ; Severe Acute Respiratory Syndrome/immunology ; Somatic Hypermutation, Immunoglobulin ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism ; Young Adult
Chemical Substances	Antibodies, Monoclonal ; Antibodies, Viral ; Broadly Neutralizing Antibodies ; Epitopes ; Receptors, Coronavirus ; Receptors, Virus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Keywords	covid19
Language	English
Publishing date	2020-06-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abc7424
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 27: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 77: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Antibody-mediated broad sarbecovirus neutralization through ACE2 molecular mimicry

Park, Young-Jun / De Marco, Anna / Starr, Tyler N / Liu, Zhuoming / Pinto, Dora / Walls, Alexandra C / Zatta, Fabrizia / Zepeda, Samantha K / Bowen, John E / Sprouse, Kaitlin S / Joshi, Anshu / Giurdanella, Martina / Guarino, Barbara / Noack, Julia / Abdelnabi, Rana / Foo, Shi-Yan Caroline / Lempp, Florian A / Benigni, Fabio / Snell, Gyorgy /

Neyts, Johan / Whelan, Sean PJ / Virgin, Herbert W / Bloom, Jesse D / Corti, Davide / Pizzuto, Matteo Samuele / Veesler, David

bioRxiv

Abstract	Understanding broadly neutralizing sarbecovirus antibody responses is key to developing countermeasures effective against SARS-CoV-2 variants and future spillovers of other sarbecoviruses. Here we describe the isolation and characterization of a human monoclonal antibody, designated S2K146, broadly neutralizing viruses belonging to all three sarbecovirus clades known to utilize ACE2 as entry receptor and protecting therapeutically against SARS-CoV-2 beta challenge in hamsters. Structural and functional studies show that most of the S2K146 epitope residues are shared with the ACE2 binding site and that the antibody inhibits receptor attachment competitively. Viral passaging experiments underscore an unusually high barrier for emergence of escape mutants making it an ideal candidate for clinical development. These findings unveil a key site of vulnerability for the development of a next generation of vaccines eliciting broad sarbecovirus immunity.
Keywords	covid19
Language	English
Publishing date	2021-10-14
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2021.10.13.464254
Database	COVID19

Full text online

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Inter-library loan at ZB MED

Full text online

Kategorien

Inter-library loan at ZB MED

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

Kategorien

Inter-library loan at ZB MED