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Artikel ; Online: Structural insights into coronavirus entry.

Tortorici, M Alejandra / Veesler, David

2019 Band 105, Seite(n) 93–116

Abstract: Coronaviruses (CoVs) have caused outbreaks of deadly pneumonia in humans since the beginning of the 21st century. The severe acute respiratory syndrome coronavirus (SARS-CoV) emerged in 2002 and was responsible for an epidemic that spread to five ... ...

Abstract	Coronaviruses (CoVs) have caused outbreaks of deadly pneumonia in humans since the beginning of the 21st century. The severe acute respiratory syndrome coronavirus (SARS-CoV) emerged in 2002 and was responsible for an epidemic that spread to five continents with a fatality rate of 10% before being contained in 2003 (with additional cases reported in 2004). The Middle-East respiratory syndrome coronavirus (MERS-CoV) emerged in the Arabian Peninsula in 2012 and has caused recurrent outbreaks in humans with a fatality rate of 35%. SARS-CoV and MERS-CoV are zoonotic viruses that crossed the species barrier using bats/palm civets and dromedary camels, respectively. No specific treatments or vaccines have been approved against any of the six human coronaviruses, highlighting the need to investigate the principles governing viral entry and cross-species transmission as well as to prepare for zoonotic outbreaks which are likely to occur due to the large reservoir of CoVs found in mammals and birds. Here, we review our understanding of the infection mechanism used by coronaviruses derived from recent structural and biochemical studies.
Mesh-Begriff(e)	Animals ; Coronavirus/physiology ; Coronavirus/ultrastructure ; Host-Pathogen Interactions ; Humans ; Virion/ultrastructure ; Virus Internalization
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2019-08-22
Erscheinungsland	United States
Dokumenttyp	Journal Article
ZDB-ID	195-8
ISSN	1557-8399 ; 0065-3527
ISSN (online)	1557-8399
ISSN	0065-3527
DOI	10.1016/bs.aivir.2019.08.002
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Human coronavirus HKU1 recognition of the TMPRSS2 host receptor.

McCallum, Matthew / Park, Young-Jun / Stewart, Cameron / Sprouse, Kaitlin R / Brown, Jack / Tortorici, M Alejandra / Gibson, Cecily / Wong, Emily / Ieven, Margareta / Telenti, Amalio / Veesler, David

bioRxiv : the preprint server for biology

2024

Abstract: The human coronavirus HKU1 spike (S) glycoprotein engages host cell surface sialoglycans and transmembrane protease serine 2 (TMPRSS2) to initiate infection. The molecular basis of HKU1 binding to TMPRSS2 and determinants of host receptor tropism remain ... ...

Abstract	The human coronavirus HKU1 spike (S) glycoprotein engages host cell surface sialoglycans and transmembrane protease serine 2 (TMPRSS2) to initiate infection. The molecular basis of HKU1 binding to TMPRSS2 and determinants of host receptor tropism remain elusive. Here, we designed an active human TMPRSS2 construct enabling high-yield recombinant production in human cells of this key therapeutic target. We determined a cryo-electron microscopy structure of the HKU1 RBD bound to human TMPRSS2 providing a blueprint of the interactions supporting viral entry and explaining the specificity for TMPRSS2 among human type 2 transmembrane serine proteases. We found that human, rat, hamster and camel TMPRSS2 promote HKU1 S-mediated entry into cells and identified key residues governing host receptor usage. Our data show that serum antibodies targeting the HKU1 RBD TMPRSS2 binding-site are key for neutralization and that HKU1 uses conformational masking and glycan shielding to balance immune evasion and receptor engagement.
Sprache	Englisch
Erscheinungsdatum	2024-01-09
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2024.01.09.574565
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Persistent immune imprinting occurs after vaccination with the COVID-19 XBB.1.5 mRNA booster in humans.

Tortorici, M Alejandra / Addetia, Amin / Seo, Albert J / Brown, Jack / Sprouse, Kaiti / Logue, Jenni / Clark, Erica / Franko, Nicholas / Chu, Helen / Veesler, David

Immunity

2024 Band 57, Heft 4, Seite(n) 904–911.e4

Abstract: Immune imprinting describes how the first exposure to a virus shapes immunological outcomes of subsequent exposures to antigenically related strains. Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) Omicron breakthrough infections and ... ...

Abstract	Immune imprinting describes how the first exposure to a virus shapes immunological outcomes of subsequent exposures to antigenically related strains. Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) Omicron breakthrough infections and bivalent COVID-19 vaccination primarily recall cross-reactive memory B cells induced by prior Wuhan-Hu-1 spike mRNA vaccination rather than priming Omicron-specific naive B cells. These findings indicate that immune imprinting occurs after repeated Wuhan-Hu-1 spike exposures, but whether it can be overcome remains unclear. To understand the persistence of immune imprinting, we investigated memory and plasma antibody responses after administration of the updated XBB.1.5 COVID-19 mRNA vaccine booster. We showed that the XBB.1.5 booster elicited neutralizing antibody responses against current variants that were dominated by recall of pre-existing memory B cells previously induced by the Wuhan-Hu-1 spike. Therefore, immune imprinting persists after multiple exposures to Omicron spikes through vaccination and infection, including post XBB.1.5 booster vaccination, which will need to be considered to guide future vaccination.
Mesh-Begriff(e)	Humans ; COVID-19 Vaccines ; COVID-19/prevention & control ; SARS-CoV-2 ; Antibodies, Neutralizing ; RNA, Messenger/genetics ; Vaccination ; Antibodies, Viral
Chemische Substanzen	COVID-19 Vaccines ; Antibodies, Neutralizing ; RNA, Messenger ; Antibodies, Viral
Sprache	Englisch
Erscheinungsdatum	2024-03-14
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.2024.02.016
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Persistent immune imprinting after XBB.1.5 COVID vaccination in humans.

Tortorici, M Alejandra / Addetia, Amin / Seo, Albert J / Brown, Jack / Sprouse, Kaitlin R / Logue, Jenni / Clark, Erica / Franko, Nicholas / Chu, Helen / Veesler, David

bioRxiv : the preprint server for biology

2023

Abstract: Immune imprinting - also known as 'original antigenic sin' - describes how the first exposure to a virus shapes the immunological outcome of subsequent exposures to antigenically related strains. SARS-CoV-2 Omicron breakthrough infections and bivalent ... ...

Abstract	Immune imprinting - also known as 'original antigenic sin' - describes how the first exposure to a virus shapes the immunological outcome of subsequent exposures to antigenically related strains. SARS-CoV-2 Omicron breakthrough infections and bivalent COVID-19 vaccination were shown to primarily recall cross-reactive memory B cells and antibodies induced by prior mRNA vaccination with the Wuhan-Hu-1 spike rather than priming naive B cells that recognize Omicron-specific epitopes. These findings underscored a strong immune imprinting resulting from repeated Wuhan-Hu-1 spike exposures. To understand if immune imprinting can be overcome, we investigated memory and plasma antibody responses after administration of the updated XBB.1.5 COVID mRNA vaccine booster. Our data show that the XBB.1.5 booster elicits neutralizing antibody responses against current variants that are dominated by recall of pre-existing memory B cells previously induced by the Wuhan-Hu-1 spike. These results indicate that immune imprinting persists even after multiple exposures to Omicron spikes through vaccination and infection, including post XBB.1.5 spike booster mRNA vaccination, which will need to be considered to guide the design of future vaccine boosters.
Sprache	Englisch
Erscheinungsdatum	2023-11-30
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2023.11.28.569129
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.

Walls, Alexandra C / Park, Young-Jun / Tortorici, M Alejandra / Wall, Abigail / McGuire, Andrew T / Veesler, David

Cell

2020 Band 183, Heft 6, Seite(n) 1735

Sprache	Englisch
Erscheinungsdatum	2020-12-14
Erscheinungsland	United States
Dokumenttyp	Published Erratum
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2020.11.032
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel: Broadly neutralizing antibodies against emerging delta-coronaviruses.

bioRxiv : the preprint server for biology

2024

Abstract: Porcine deltacoronavirus (PDCoV) spillovers were recently detected in children with acute undifferentiated febrile illness, underscoring recurrent zoonoses of divergent coronaviruses. To date, no vaccines or specific therapeutics are approved for use in ... ...

Abstract	Porcine deltacoronavirus (PDCoV) spillovers were recently detected in children with acute undifferentiated febrile illness, underscoring recurrent zoonoses of divergent coronaviruses. To date, no vaccines or specific therapeutics are approved for use in humans against PDCoV. To prepare for possible future PDCoV epidemics, we isolated human spike (S)-directed monoclonal antibodies from transgenic mice and found that two of them, designated PD33 and PD41, broadly neutralized a panel of PDCoV variants. Cryo-electron microscopy structures of PD33 and PD41 in complex with the PDCoV receptor-binding domain and S ectodomain trimer provide a blueprint of the epitopes recognized by these mAbs, rationalizing their broad inhibitory activity. We show that both mAbs inhibit PDCoV by competitively interfering with host APN binding to the PDCoV receptor-binding loops, explaining the mechanism of viral neutralization. PD33 and PD41 are candidates for clinical advancement, which could be stockpiled to prepare for possible future PDCoV outbreaks.
Sprache	Englisch
Erscheinungsdatum	2024-04-01
Erscheinungsland	United States
Dokumenttyp	Preprint
DOI	10.1101/2024.03.27.586411
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Persistent immune imprinting after XBB.1.5 COVID vaccination in humans

Tortorici, M. Alejandra / Addetia, Amin / Seo, Albert J / Brown, Jack / Sprouse, Kaitlin / Logue, Jenni / Clarke, Erica / Franko, Nicholas / Chu, Helen / Veesler, David

bioRxiv

Abstract: Immune imprinting - also known as original antigenic sin describes how the first exposure a virus shapes the immunological outcome of subsequent exposures to antigenically related strains. SARS-CoV-2 Omicron breakthrough infections and bivalent COVID-19 ... ...

Abstract	Immune imprinting - also known as original antigenic sin describes how the first exposure a virus shapes the immunological outcome of subsequent exposures to antigenically related strains. SARS-CoV-2 Omicron breakthrough infections and bivalent COVID-19 vaccination were shown to primarily recall cross-reactive memory B cells and antibodies induced by prior mRNA vaccination with the Wuhan-Hu-1 spike rather than priming naive B cells that recognize Omicron-specific epitopes. These findings underscored a strong immune imprinting resulting from repeated Wuhan-Hu-1 spike exposures. To understand if immune imprinting can be overcome, we investigated memory and plasma antibody responses after administration of the updated XBB.1.5 COVID mRNA vaccine booster. Our data show that the XBB.1.5 booster elicits neutralizing antibody responses against current variants that are dominated by recall of pre-existing memory B cells previously induced by the Wuhan-Hu-1 spike. These results indicate that immune imprinting persists even after multiple exposures to Omicron spikes through vaccination and infection, including post XBB.1.5 spike booster mRNA vaccination, which will need to be considered to guide the design of future vaccine boosters.
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2023-11-30
Verlag	Cold Spring Harbor Laboratory
Dokumenttyp	Artikel ; Online
DOI	10.1101/2023.11.28.569129
Datenquelle	COVID19

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Artikel ; Online: Persistent immune imprinting after XBB.1.5 COVID vaccination in humans

Tortorici, M. Alejandra / Addetia, Amin / Seo, Albert J. / Brown, Jack / Sprouse, Kaitlin R. / Logue, Jenni / Clark, Erica / Franko, Nicholas / Chu, Helen / Veesler, David

bioRxiv

Abstract	Immune imprinting - also known as original antigenic sin describes how the first exposure a virus shapes the immunological outcome of subsequent exposures to antigenically related strains. SARS-CoV-2 Omicron breakthrough infections and bivalent COVID-19 vaccination were shown to primarily recall cross-reactive memory B cells and antibodies induced by prior mRNA vaccination with the Wuhan-Hu-1 spike rather than priming naive B cells that recognize Omicron-specific epitopes. These findings underscored a strong immune imprinting resulting from repeated Wuhan-Hu-1 spike exposures. To understand if immune imprinting can be overcome, we investigated memory and plasma antibody responses after administration of the updated XBB.1.5 COVID mRNA vaccine booster. Our data show that the XBB.1.5 booster elicits neutralizing antibody responses against current variants that are dominated by recall of pre-existing memory B cells previously induced by the Wuhan-Hu-1 spike. These results indicate that immune imprinting persists even after multiple exposures to Omicron spikes through vaccination and infection, including post XBB.1.5 spike booster mRNA vaccination, which will need to be considered to guide the design of future vaccine boosters.
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2023-11-30
Verlag	Cold Spring Harbor Laboratory
Dokumenttyp	Artikel ; Online
DOI	10.1101/2023.11.28.569129
Datenquelle	COVID19

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Artikel ; Online: A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease/cofactor complex to switch between RNA replication and virion morphogenesis.

Dubrau, Danilo / Tortorici, M Alejandra / Rey, Félix A / Tautz, Norbert

PLoS pathogens

2017 Band 13, Heft 2, Seite(n) e1006134

Abstract: The viruses of the family Flaviviridae possess a positive-strand RNA genome and express a single polyprotein which is processed into functional proteins. Initially, the nonstructural (NS) proteins, which are not part of the virions, form complexes ... ...

Abstract	The viruses of the family Flaviviridae possess a positive-strand RNA genome and express a single polyprotein which is processed into functional proteins. Initially, the nonstructural (NS) proteins, which are not part of the virions, form complexes capable of genome replication. Later on, the NS proteins also play a critical role in virion formation. The molecular basis to understand how the same proteins form different complexes required in both processes is so far unknown. For pestiviruses, uncleaved NS2-3 is essential for virion morphogenesis while NS3 is required for RNA replication but is not functional in viral assembly. Recently, we identified two gain of function mutations, located in the C-terminal region of NS2 and in the serine protease domain of NS3 (NS3 residue 132), which allow NS2 and NS3 to substitute for uncleaved NS2-3 in particle assembly. We report here the crystal structure of pestivirus NS3-4A showing that the NS3 residue 132 maps to a surface patch interacting with the C-terminal region of NS4A (NS4A-kink region) suggesting a critical role of this contact in virion morphogenesis. We show that destabilization of this interaction, either by alanine exchanges at this NS3/4A-kink interface, led to a gain of function of the NS3/4A complex in particle formation. In contrast, RNA replication and thus replicase assembly requires a stable association between NS3 and the NS4A-kink region. Thus, we propose that two variants of NS3/4A complexes exist in pestivirus infected cells each representing a basic building block required for either RNA replication or virion morphogenesis. This could be further corroborated by trans-complementation studies with a replication-defective NS3/4A double mutant that was still functional in viral assembly. Our observations illustrate the presence of alternative overlapping surfaces providing different contacts between the same proteins, allowing the switch from RNA replication to virion formation.
Mesh-Begriff(e)	Animals ; Blotting, Western ; Cell Line ; Crystallography, X-Ray ; Dogs ; Fluorescent Antibody Technique ; Morphogenesis ; Mutagenesis, Site-Directed ; Pestivirus/chemistry ; Pestivirus/physiology ; RNA Helicases/chemistry ; RNA Helicases/metabolism ; RNA, Viral ; Serine Endopeptidases/chemistry ; Serine Endopeptidases/metabolism ; Viral Nonstructural Proteins/chemistry ; Viral Nonstructural Proteins/metabolism ; Virion/physiology ; Virus Assembly ; Virus Replication/physiology
Chemische Substanzen	NS3 protein, flavivirus ; NS4A protein, flavivirus ; RNA, Viral ; Viral Nonstructural Proteins ; Serine Endopeptidases (EC 3.4.21.-) ; RNA Helicases (EC 3.6.4.13)
Sprache	Englisch
Erscheinungsdatum	2017-02-02
Erscheinungsland	United States
Dokumenttyp	Journal Article ; 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.1006134
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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Artikel ; Online: Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.

Walls, Alexandra C / Park, Young-Jun / Tortorici, M Alejandra / Wall, Abigail / McGuire, Andrew T / Veesler, David

Cell

2020 Band 181, Heft 2, Seite(n) 281–292.e6

Abstract: The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor- ...

Abstract	The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S
Mesh-Begriff(e)	Amino Acid Sequence ; Angiotensin-Converting Enzyme 2 ; Antibodies, Neutralizing/metabolism ; Antibodies, Neutralizing/pharmacology ; Antigens, Viral/chemistry ; Antigens, Viral/immunology ; Antigens, Viral/metabolism ; Betacoronavirus/chemistry ; Betacoronavirus/metabolism ; Cell Line ; Cryoelectron Microscopy ; Humans ; Models, Molecular ; Peptidyl-Dipeptidase A/metabolism ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; SARS Virus/metabolism ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/immunology ; Spike Glycoprotein, Coronavirus/metabolism ; Spike Glycoprotein, Coronavirus/ultrastructure ; Virus Internalization/drug effects
Chemische Substanzen	Antibodies, Neutralizing ; Antigens, Viral ; 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)
Schlagwörter	covid19
Sprache	Englisch
Erscheinungsdatum	2020-03-09
Erscheinungsland	United States
Dokumenttyp	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2020.02.058
Datenquelle	MEDical Literature Analysis and Retrieval System OnLINE

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