C
Cesar Lopez-Camacho
Researcher at University of Oxford
Publications - 45
Citations - 4813
Cesar Lopez-Camacho is an academic researcher from University of Oxford. The author has contributed to research in topics: Epitope & Population. The author has an hindex of 18, co-authored 44 publications receiving 2526 citations. Previous affiliations of Cesar Lopez-Camacho include Benemérita Universidad Autónoma de Puebla & University of Vermont.
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Journal ArticleDOI
Broad and strong memory CD4 + and CD8 + T cells induced by SARS-CoV-2 in UK convalescent individuals following COVID-19.
Yanchun Peng,Alexander J. Mentzer,G Liu,G Liu,X Yao,Z Yin,D Dong,D Dong,Wanwisa Dejnirattisai,T Rostron,P Supasa,C Liu,Cesar Lopez-Camacho,J Slon-Campos,Yuguang Zhao,David I. Stuart,Guido C. Paesen,Jonathan M. Grimes,Alfred A. Antson,Oliver W. Bayfield,Hawkins Dedp.,Ker D-S.,B Wang,Lance Turtle,Krishanthi Subramaniam,Paul Thomson,P Zhang,Christina Dold,Jeremy Ratcliff,Peter Simmonds,T I de Silva,Paul Sopp,Dannielle Wellington,U S Rajapaksa,Chen Y-L.,Mariolina Salio,Giorgio Napolitani,Wayne Paes,Persephone Borrow,Benedikt M. Kessler,J W Fry,N F Schwabe,Malcolm G Semple,Malcolm G Semple,J K Baillie,Shona C Moore,Openshaw Pjm.,M A Ansari,Susanna Dunachie,Eleanor Barnes,John Frater,G Kerr,Philip J. R. Goulder,T Lockett,R Levin,Y Zhang,Y Zhang,R Jing,Ho L-P.,Richard J. Cornall,Christopher P. Conlon,Paul Klenerman,Gavin R. Screaton,Juthathip Mongkolsapaya,Andrew J. McMichael,Julian C. Knight,Graham S. Ogg,Tao Dong +67 more
TL;DR: The identification of T cell responses associated with milder disease will support an understanding of protective immunity and highlights the potential of including non-spike proteins within future COVID-19 vaccine design.
Journal ArticleDOI
Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera.
D. Zhou,Wanwisa Dejnirattisai,P Supasa,Chang Liu,Alexander J. Mentzer,Helen M. Ginn,Yuguang Zhao,Duyvesteyn Hme.,Aekkachai Tuekprakhon,R Nutalai,Beibei Wang,Guido C. Paesen,Cesar Lopez-Camacho,J Slon-Campos,Bassam Hallis,Naomi Coombes,Kevin R. Bewley,Sue Charlton,Thomas S. Walter,Donal T. Skelly,Sheila F Lumley,Christina Dold,R Levin,Tao Dong,Andrew J. Pollard,Julian C. Knight,Derrick W. Crook,Teresa Lambe,Elizabeth A. Clutterbuck,S Bibi,Amy Flaxman,M Bittaye,Sandra Belij-Rammerstorfer,Sarah C. Gilbert,William James,Miles W. Carroll,Paul Klenerman,Eleanor Barnes,Susanna Dunachie,Elizabeth E. Fry,Juthathip Mongkolsapaya,Jingshan Ren,David I. Stuart,Gavin R. Screaton +43 more
TL;DR: In this paper, a structure-function analysis of B.1.351 was performed using a large cohort of convalescent and vaccinee serum samples, and it was shown that the receptor-binding domain mutations provide tighter ACE2 binding and widespread escape from monoclonal antibody neutralization largely driven by E484K, although K417N and N501Y act together against some important antibody classes.
Journal ArticleDOI
Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum.
Chang Liu,Helen M. Ginn,Wanwisa Dejnirattisai,P Supasa,Beibei Wang,Aekkachai Tuekprakhon,R Nutalai,D. Zhou,Alexander J. Mentzer,Yuguang Zhao,Duyvesteyn Hme.,Cesar Lopez-Camacho,J Slon-Campos,Thomas S. Walter,Donal T. Skelly,S A Johnson,T G Ritter,C Mason,S A Costa Clemens,F. Gomes Naveca,Valdinete Alves do Nascimento,Fabrícia F. Nascimento,C Fernandes da Costa,Paola Cristina Resende,Alex Pauvolid-Corrêa,Marilda M. Siqueira,Christina Dold,Nigel J. Temperton,Tao Dong,Andrew J. Pollard,James C. Knight,D W Crook,Teresa Lambe,Elizabeth A. Clutterbuck,S Bibi,Amy Flaxman,M Bittaye,Sandra Belij-Rammerstorfer,Sarah C. Gilbert,T Malik,Miles W. Carroll,Paul Klenerman,Eleanor Barnes,Susanna Dunachie,Vicky L. Baillie,Vicky L. Baillie,N Serafin,N Serafin,Z Ditse,Z Ditse,K Da Silva,K Da Silva,Neil G. Paterson,Mark A. Williams,David Hall,Shabir A. Madhi,Shabir A. Madhi,M C Nunes,M C Nunes,P Goulder,Elizabeth E. Fry,Juthathip Mongkolsapaya,Juthathip Mongkolsapaya,Jingshan Ren,David I. Stuart,Gavin R. Screaton +65 more
TL;DR: In this paper, the ability of monoclonal antibodies and convalescent and vaccine sera to neutralize B.617.1 and B.1.2 has been studied.
Journal ArticleDOI
Antibody evasion by the P.1 strain of SARS-CoV-2.
Wanwisa Dejnirattisai,D. Zhou,P Supasa,Chang Liu,Alexander J. Mentzer,Helen M. Ginn,Yuguang Zhao,Duyvesteyn Hme.,Aekkachai Tuekprakhon,R Nutalai,Beibei Wang,Cesar Lopez-Camacho,J Slon-Campos,Thomas S. Walter,Donal T. Skelly,S A Costa Clemens,Felipe Gomes Naveca,Valdinete Alves do Nascimento,Fabrícia F. Nascimento,C Fernandes da Costa,Paola Cristina Resende,Alex Pauvolid-Corrêa,Marilda M. Siqueira,Christina Dold,R Levin,Tao Dong,Andrew J. Pollard,Julian C. Knight,D W Crook,Teresa Lambe,Elizabeth A. Clutterbuck,S Bibi,Amy Flaxman,M Bittaye,Sandra Belij-Rammerstorfer,Sarah C. Gilbert,Miles W. Carroll,Paul Klenerman,E Barnes,Susanna Dunachie,Neil G. Paterson,Mark A. Williams,David R. Hall,Hulswit Rjg.,Thomas A. Bowden,Elizabeth E. Fry,Juthathip Mongkolsapaya,Juthathip Mongkolsapaya,Jingshan Ren,David I. Stuart,Gavin R. Screaton +50 more
TL;DR: In this paper, structural analysis of the ACE2 binding sites of the SARS-CoV-2 pandemic strain has been carried out and the authors show that the 222 light chain is able to largely restore neutralization potency to a major class of public antibodies.
Journal ArticleDOI
Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera.
P Supasa,D. Zhou,Wanwisa Dejnirattisai,Chang Liu,Alexander J. Mentzer,Helen M. Ginn,Yuguang Zhao,Duyvesteyn Hme.,R Nutalai,Aekkachai Tuekprakhon,Beibei Wang,Guido C. Paesen,J Slon-Campos,Cesar Lopez-Camacho,Bassam Hallis,Naomi Coombes,Kevin R. Bewley,Sue Charlton,Thomas S. Walter,Eleanor Barnes,Susanna Dunachie,Donal T. Skelly,Sheila F Lumley,Natalie Baker,I Shaik,Holly E. Humphries,Kerry J Godwin,N Gent,A Sienkiewicz,Christina Dold,R Levin,Tao Dong,Andrew J. Pollard,Julian C. Knight,Paul Klenerman,D W Crook,Teresa Lambe,Elizabeth A. Clutterbuck,S Bibi,Amy Flaxman,M Bittaye,Sandra Belij-Rammerstorfer,Sarah C. Gilbert,David R. Hall,Mark A. Williams,Neil G. Paterson,William James,Miles W. Carroll,Elizabeth E. Fry,Juthathip Mongkolsapaya,Jingshan Ren,David I. Stuart,Gavin R. Screaton +52 more
TL;DR: In this article, the authors examined the ability of B.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination, and found that B. 1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light chain contacts with residue 501.