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Article ; Online: Comparing the incubation period, serial interval, and infectiousness profile between SARS-CoV-2 Omicron and Delta variants.

Guo, Zihao / Zhao, Shi / Mok, Chris Ka Pun / So, Ray T Y / Yam, Carrie Ho Kwan / Chow, Tsz Yu / Chan, Tony Chin Pok / Wei, Yuchen / Jia, Katherine Min / Wang, Maggie Haitian / Chong, Ka Chun / Yeoh, Eng Kiong

Journal of medical virology

2023 Volume 95, Issue 3, Page(s) e28648

Abstract: In January 2022, the SARS-CoV-2 Omicron variants initiated major outbreaks and dominated the transmissions in Hong Kong, displacing an earlier outbreak seeded by the Delta variants. To provide insight into the transmission potential of the emerging ... ...

Abstract	In January 2022, the SARS-CoV-2 Omicron variants initiated major outbreaks and dominated the transmissions in Hong Kong, displacing an earlier outbreak seeded by the Delta variants. To provide insight into the transmission potential of the emerging variants, we aimed to compare the epidemiological characteristics of the Omicron and Delta variants. We analyzed the line-list clinical and contact tracing data of the SARS-CoV-2 confirmed cases in Hong Kong. Transmission pairs were constructed based on the individual contact history. We fitted bias-controlled models to the data to estimate the serial interval, incubation period and infectiousness profile of the two variants. Viral load data were extracted and fitted to the random effect models to investigate the potential risk modifiers for the clinical viral shedding course. Totally 14 401 confirmed cases were reported between January 1 and February 15, 2022. The estimated mean serial interval (4.4 days vs. 5.8 days) and incubation period (3.4 days vs. 3.8 days) were shorter for the Omicron than the Delta variants. A larger proportion of presymptomatic transmission was observed for the Omicron (62%) compared to the Delta variants (48%). The Omicron cases had higher mean viral load over an infection course than the Delta cases, with the elder cases appearing more infectious than the younger cases for both variants. The epidemiological features of Omicron variants were likely an obstacle to contact tracing measures, imposed as a major intervention in settings like Hong Kong. Continuously monitoring the epidemiological feature for any emerging SARS-CoV-2 variants in the future is needed to assist officials in planning measures for COVID-19 control.
MeSH term(s)	Humans ; SARS-CoV-2/genetics ; COVID-19/epidemiology ; Infectious Disease Incubation Period ; Disease Outbreaks ; Seizures
Language	English
Publishing date	2023-03-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	752392-0
ISSN	1096-9071 ; 0146-6615
ISSN (online)	1096-9071
ISSN	0146-6615
DOI	10.1002/jmv.28648
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Article ; Online: Neutralizing Antibody Response to

Lv, Huibin / So, Ray T Y / Teo, Qi Wen / Yuan, Meng / Liu, Hejun / Lee, Chang-Chun D / Yip, Garrick K / Ng, Wilson W / Wilson, Ian A / Peiris, Malik / Wu, Nicholas C / Mok, Chris Ka Pun

Viruses

2022 Volume 14, Issue 7

Abstract: Antigenic imprinting, which describes the bias of the antibody response due to previous immune history, can influence vaccine effectiveness. While this phenomenon has been reported for viruses such as influenza, there is little understanding of how prior ...

Abstract	Antigenic imprinting, which describes the bias of the antibody response due to previous immune history, can influence vaccine effectiveness. While this phenomenon has been reported for viruses such as influenza, there is little understanding of how prior immune history affects the antibody response to SARS-CoV-2. This study provides evidence for antigenic imprinting through immunization with two
MeSH term(s)	Animals ; Antibodies, Neutralizing ; Antibodies, Viral ; Antibody Formation ; COVID-19/prevention & control ; Immunization ; Mice ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2022-06-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14071382
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Article ; Online: Amino acid substitution L232F in non-structural protein 6 identified as a possible human-adaptive mutation in clade B MERS coronaviruses.

So, Ray T Y / Chu, Daniel K W / Hui, Kenrie P Y / Mok, Chris K P / Shum, Marcus H H / Sanyal, Sumana / Nicholls, John M / Ho, John C W / Cheung, Man-Chun / Ng, Ka-Chun / Yeung, Hin-Wo / Chan, Michael C W / Poon, Leo L M / Zhao, Jincun / Lam, Tommy T Y / Peiris, Malik

Journal of virology

2023 Volume 97, Issue 12, Page(s) e0136923

Abstract: Importance: Viral host adaptation plays an important role in inter-species transmission of coronaviruses and influenza viruses. Multiple human-adaptive mutations have been identified in influenza viruses but not so far in MERS-CoV that circulates widely ...

Abstract	Importance: Viral host adaptation plays an important role in inter-species transmission of coronaviruses and influenza viruses. Multiple human-adaptive mutations have been identified in influenza viruses but not so far in MERS-CoV that circulates widely in dromedary camels in the Arabian Peninsula leading to zoonotic transmission. Here, we analyzed clade B MERS-CoV sequences and identified an amino acid substitution L232F in nsp6 that repeatedly occurs in human MERS-CoV. Using a loss-of-function reverse genetics approach, we found the nsp6 L232F conferred increased viral replication competence
MeSH term(s)	Animals ; Humans ; Mice ; Amino Acid Substitution ; Camelus ; Coronavirus Infections/virology ; Middle East Respiratory Syndrome Coronavirus/genetics ; Mutation ; Viral Nonstructural Proteins/genetics
Chemical Substances	Viral Nonstructural Proteins
Language	English
Publishing date	2023-12-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/jvi.01369-23
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Article ; Online: Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domain.

Wang, Yanqun / Zhang, Zhaoyong / Yang, Minnan / Xiong, Xinyi / Yan, Qihong / Cao, Lei / Wei, Peilan / Zhang, Yuting / Zhang, Lu / Lv, Kexin / Chen, Jiantao / Liu, Xuesong / Zhao, Xiaochu / Xiao, Juxue / Zhang, Shengnan / Zhu, Airu / Gan, Mian / Zhang, Jingjun / Cai, Ruoxi /

Zhuo, Jianfen / Zhang, Yanjun / Rao, Haiyue / Qu, Bin / Zhang, Yuanyuan / Chen, Lei / Dai, Jun / Cheng, Linling / Hu, Qingtao / Chen, Yaoqing / Lv, Huibin / So, Ray T Y / Peiris, Malik / Zhao, Jingxian / Liu, Xiaoqing / Mok, Chris Ka Pun / Wang, Xiangxi / Zhao, Jincun

Cell reports

2024 Volume 43, Issue 1, Page(s) 113653

Abstract: Omicron, as the emerging variant with enhanced vaccine tolerance, has sharply disrupted most therapeutic antibodies. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) belongs to the subgenus Sarbecovirus, members of which share high sequence ... ...

Abstract	Omicron, as the emerging variant with enhanced vaccine tolerance, has sharply disrupted most therapeutic antibodies. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) belongs to the subgenus Sarbecovirus, members of which share high sequence similarity. Herein, we report one sarbecovirus antibody, 5817, which has broad-spectrum neutralization capacity against SARS-CoV-2 variants of concern (VOCs) and SARS-CoV, as well as related bat and pangolin viruses. 5817 can hardly compete with six classes of receptor-binding-domain-targeted antibodies grouped by structural classifications. No obvious impairment in the potency is detected against SARS-CoV-2 Omicron and subvariants. The cryoelectron microscopy (cryo-EM) structure of neutralizing antibody 5817 in complex with Omicron spike reveals a highly conserved epitope, only existing at the receptor-binding domain (RBD) open state. Prophylactic and therapeutic administration of 5817 potently protects mice from SARS-CoV-2 Beta, Delta, Omicron, and SARS-CoV infection. This study reveals a highly conserved cryptic epitope targeted by a broad sarbecovirus neutralizing antibody, which would be beneficial to meet the potential threat of pre-emergent SARS-CoV-2 VOCs.
MeSH term(s)	Animals ; Mice ; Severe acute respiratory syndrome-related coronavirus ; Broadly Neutralizing Antibodies ; Cryoelectron Microscopy ; Antibodies, Neutralizing ; Epitopes ; Antibodies, Viral
Chemical Substances	Broadly Neutralizing Antibodies ; Antibodies, Neutralizing ; Epitopes ; Antibodies, Viral
Language	English
Publishing date	2024-01-03
Publishing country	United States
Document type	Journal Article ; 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.2023.113653
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Article ; Online: A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV.

Yuan, Meng / Wu, Nicholas C / Zhu, Xueyong / Lee, Chang-Chun D / So, Ray T Y / Lv, Huibin / Mok, Chris K P / Wilson, Ian A

Science (New York, N.Y.)

2020 Volume 368, Issue 6491, Page(s) 630–633

Abstract: The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore ... ...

Abstract	The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2.
MeSH term(s)	Amino Acid Sequence ; Angiotensin-Converting Enzyme 2 ; Antibodies, Neutralizing/chemistry ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/chemistry ; Antibodies, Viral/immunology ; Antibody Affinity ; Antigens, Viral/chemistry ; Antigens, Viral/immunology ; Betacoronavirus/chemistry ; Betacoronavirus/immunology ; Binding Sites ; Cross Reactions ; Crystallography, X-Ray ; Epitopes/chemistry ; Epitopes/immunology ; Models, Molecular ; Peptidyl-Dipeptidase A/chemistry ; Peptidyl-Dipeptidase A/metabolism ; Protein Conformation ; Protein Domains ; Protein Interaction Domains and Motifs/immunology ; Receptors, Coronavirus ; Receptors, Virus/chemistry ; Receptors, Virus/metabolism ; Severe acute respiratory syndrome-related coronavirus/chemistry ; Severe acute respiratory syndrome-related coronavirus/immunology ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/immunology
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral ; Antigens, Viral ; Epitopes ; Receptors, Coronavirus ; Receptors, Virus ; Spike Glycoprotein, Coronavirus ; spike glycoprotein, SARS-CoV ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
Keywords	covid19
Language	English
Publishing date	2020-04-03
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	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.abb7269
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Article ; Online: Identification of a broad sarbecovirus neutralizing antibody targeting a conserved epitope on the receptor-binding domain

Yanqun Wang / Zhaoyong Zhang / Minnan Yang / Xinyi Xiong / Qihong Yan / Lei Cao / Peilan Wei / Yuting Zhang / Lu Zhang / Kexin Lv / Jiantao Chen / Xuesong Liu / Xiaochu Zhao / Juxue Xiao / Shengnan Zhang / Airu Zhu / Mian Gan / Jingjun Zhang / Ruoxi Cai /

Jianfen Zhuo / Yanjun Zhang / Haiyue Rao / Bin Qu / Yuanyuan Zhang / Lei Chen / Jun Dai / Linling Cheng / Qingtao Hu / Yaoqing Chen / Huibin Lv / Ray T.Y. So / Malik Peiris / Jingxian Zhao / Xiaoqing Liu / Chris Ka Pun Mok / Xiangxi Wang / Jincun Zhao

Cell Reports, Vol 43, Iss 1, Pp 113653- (2024)

2024

Abstract: Summary: Omicron, as the emerging variant with enhanced vaccine tolerance, has sharply disrupted most therapeutic antibodies. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) belongs to the subgenus Sarbecovirus, members of which share high ... ...

Abstract	Summary: Omicron, as the emerging variant with enhanced vaccine tolerance, has sharply disrupted most therapeutic antibodies. Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) belongs to the subgenus Sarbecovirus, members of which share high sequence similarity. Herein, we report one sarbecovirus antibody, 5817, which has broad-spectrum neutralization capacity against SARS-CoV-2 variants of concern (VOCs) and SARS-CoV, as well as related bat and pangolin viruses. 5817 can hardly compete with six classes of receptor-binding-domain-targeted antibodies grouped by structural classifications. No obvious impairment in the potency is detected against SARS-CoV-2 Omicron and subvariants. The cryoelectron microscopy (cryo-EM) structure of neutralizing antibody 5817 in complex with Omicron spike reveals a highly conserved epitope, only existing at the receptor-binding domain (RBD) open state. Prophylactic and therapeutic administration of 5817 potently protects mice from SARS-CoV-2 Beta, Delta, Omicron, and SARS-CoV infection. This study reveals a highly conserved cryptic epitope targeted by a broad sarbecovirus neutralizing antibody, which would be beneficial to meet the potential threat of pre-emergent SARS-CoV-2 VOCs.
Keywords	CP: Immunology ; Biology (General) ; QH301-705.5
Subject code	570
Language	English
Publishing date	2024-01-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: Neutralizing Antibody Response to Sarbecovirus Is Delayed in Sequential Heterologous Immunization

Lv, Huibin / So, Ray T. Y. / Teo, Qi Wen / Yuan, Meng / Liu, Hejun / Lee, Chang-Chun D. / Yip, Garrick K. / Ng, Wilson W. / Wilson, Ian A. / Peiris, Malik / Wu, Nicholas C. / Mok, Chris Ka Pun

Viruses. 2022 June 24, v. 14, no. 7

2022

Abstract	Antigenic imprinting, which describes the bias of the antibody response due to previous immune history, can influence vaccine effectiveness. While this phenomenon has been reported for viruses such as influenza, there is little understanding of how prior immune history affects the antibody response to SARS-CoV-2. This study provides evidence for antigenic imprinting through immunization with two Sarbecoviruses, the subgenus that includes SARS-CoV-2. Mice were immunized subsequently with two antigenically distinct Sarbecovirus strains, namely SARS-CoV-1 and SARS-CoV-2. We found that sequential heterologous immunization induced cross-reactive binding antibodies for both viruses and delayed the emergence of neutralizing antibody responses against the booster strain. Our results provide fundamental knowledge about the immune response to Sarbecovirus and important insights into the development of pan-sarbecovirus vaccines and guiding therapeutic interventions.
Keywords	Severe acute respiratory syndrome coronavirus ; Severe acute respiratory syndrome coronavirus 2 ; antibody formation ; immunization ; influenza ; vaccines
Language	English
Dates of publication	2022-0624
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v14071382
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Genetic diversity and molecular epidemiology of Middle East Respiratory Syndrome Coronavirus in dromedaries in Ethiopia, 2017-2020.

Zhou, Ziqi / Ali, Abraham / Walelign, Elias / Demissie, Getnet F / El Masry, Ihab / Abayneh, Takele / Getachew, Belayneh / Krishnan, Pavithra / Ng, Daisy Y M / Gardner, Emma / Makonnen, Yilma / Miguel, Eve / Chevalier, Véronique / Chu, Daniel K / So, Ray T Y / Von Dobschuetz, Sophie / Mamo, Gezahegne / Poon, Leo L M / Peiris, Malik

Emerging microbes & infections

2022 Volume 12, Issue 1, Page(s) e2164218

Abstract: Middle East respiratory syndrome coronavirus (MERS-CoV) is enzootic in dromedary camels and causes zoonotic infection and disease in humans. Although over 80% of the global population of infected dromedary camels are found in Africa, zoonotic disease had ...

Abstract	Middle East respiratory syndrome coronavirus (MERS-CoV) is enzootic in dromedary camels and causes zoonotic infection and disease in humans. Although over 80% of the global population of infected dromedary camels are found in Africa, zoonotic disease had only been reported in the Arabia Peninsula and travel-associated disease has been reported elsewhere. In this study, genetic diversity and molecular epidemiology of MERS-CoV in dromedary camels in Ethiopia were investigated during 2017-2020. Of 1766 nasal swab samples collected, 61 (3.5%) were detected positive for MERS-CoV RNA. Of 484 turbinate swab samples collected, 10 (2.1%) were detected positive for MERS-CoV RNA. Twenty-five whole genome sequences were obtained from these MERS-CoV positive samples. Phylogenetically, these Ethiopian camel-originated MERS-CoV belonged to clade C2, clustering with other East African camel strains. Virus sequences from camel herds clustered geographically while in an abattoir, two distinct phylogenetic clusters of MERS-CoVs were observed in two sequential sampling collections, which indicates the greater genetic diversity of MERS-CoV in abattoirs. In contrast to clade A and B viruses from the Arabian Peninsula, clade C camel-originated MERS-CoV from Ethiopia had various nucleotide insertions and deletions in non-structural gene nsp3, accessory genes ORF3 and ORF5 and structural gene N. This study demonstrates the genetic instability of MERS-CoV in dromedaries in East Africa, which indicates that the virus is still actively adapting to its camel host. The impact of the observed nucleotide insertions and deletions on virus evolution, viral fitness, and zoonotic potential deserves further study.
MeSH term(s)	Animals ; Humans ; Middle East Respiratory Syndrome Coronavirus/genetics ; Camelus ; Phylogeny ; Ethiopia/epidemiology ; Molecular Epidemiology ; Travel ; Coronavirus Infections/epidemiology ; Coronavirus Infections/veterinary ; Zoonoses/epidemiology ; Genetic Variation ; RNA
Chemical Substances	RNA (63231-63-0)
Language	English
Publishing date	2022-12-24
Publishing country	United States
Document type	Journal Article
ZDB-ID	2681359-2
ISSN	2222-1751 ; 2222-1751
ISSN (online)	2222-1751
ISSN	2222-1751
DOI	10.1080/22221751.2022.2164218
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Article ; Online: Homologous and heterologous serological response to the N-terminal domain of SARS-CoV-2 in humans and mice.

Lv, Huibin / Tsang, Owen Tak-Yin / So, Ray T Y / Wang, Yiquan / Yuan, Meng / Liu, Hejun / Yip, Garrick K / Teo, Qi Wen / Lin, Yihan / Liang, Weiwen / Wang, Jinlin / Ng, Wilson W / Wilson, Ian A / Peiris, J S Malik / Wu, Nicholas C / Mok, Chris K P

European journal of immunology

2021 Volume 51, Issue 9, Page(s) 2296–2305

Abstract: The increasing numbers of infected cases of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) poses serious threats to public health and the global economy. Most SARS-CoV-2 neutralizing antibodies ... ...

Abstract	The increasing numbers of infected cases of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) poses serious threats to public health and the global economy. Most SARS-CoV-2 neutralizing antibodies target the receptor binding domain (RBD) and some the N-terminal domain (NTD) of the spike protein, which is the major antigen of SARS-CoV-2. While the antibody response to RBD has been extensively characterized, the antigenicity and immunogenicity of the NTD protein are less well studied. Using 227 plasma samples from COVID-19 patients, we showed that SARS-CoV-2 NTD-specific antibodies could be induced during infection. As compared to the results of SARS-CoV-2 RBD, the serological response of SARS-CoV-2 NTD is less cross-reactive with SARS-CoV, a pandemic strain that was identified in 2003. Furthermore, neutralizing antibodies are rarely elicited in a mice model when NTD is used as an immunogen. We subsequently demonstrate that NTD has an altered antigenicity when expressed alone. Overall, our results suggest that while NTD offers a supplementary strategy for serology testing, it may not be suitable as an immunogen for vaccine development.
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/immunology ; COVID-19/immunology ; Cell Line ; Chlorocebus aethiops ; Cross Reactions/immunology ; Female ; Humans ; Mice ; Mice, Inbred BALB C ; Pandemics/prevention & control ; Protein Binding/immunology ; Protein Domains/immunology ; SARS-CoV-2/immunology ; Sf9 Cells ; Vero Cells
Chemical Substances	Antibodies, Neutralizing ; Antibodies, Viral
Language	English
Publishing date	2021-06-22
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	120108-6
ISSN	1521-4141 ; 0014-2980
ISSN (online)	1521-4141
ISSN	0014-2980
DOI	10.1002/eji.202149234
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Article ; Online: A highly conserved cryptic epitope in the receptor-binding domains of SARS-CoV-2 and SARS-CoV

Yuan, Meng / Wu, Nicholas C. / Zhu, Xueyong / Lee, Chang-Chun D. / So, Ray T. Y. / Lv, Huibin / Mok, Chris K. P. / Wilson, Ian A.

bioRxiv

Abstract: The outbreak of COVID-19, which is caused by SARS-CoV-2 virus, continues to spread globally, but there is currently very little understanding of the epitopes on the virus. In this study, we have determined the crystal structure of the receptor-binding ... ...

Abstract	The outbreak of COVID-19, which is caused by SARS-CoV-2 virus, continues to spread globally, but there is currently very little understanding of the epitopes on the virus. In this study, we have determined the crystal structure of the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein in complex with CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient. CR3022 targets a highly conserved epitope that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding site can only be accessed when at least two RBDs on the trimeric S protein are in the “up” conformation. Overall, this study provides structural and molecular insight into the antigenicity of SARS-CoV-2. ONE SENTENCE SUMMARY Structural study of a cross-reactive SARS antibody reveals a conserved epitope on the SARS-CoV-2 receptor-binding domain.
Keywords	covid19
Publisher	BioRxiv; WHO
Document type	Article ; Online
DOI	10.1101/2020.03.13.991570
Database	COVID19

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