Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant.
Leonid Yurkovetskiy,Xue Wang,Kristen E. Pascal,Christopher Tomkins-Tinch,Thomas Nyalile,Yetao Wang,Alina Baum,William E. Diehl,Ann Dauphin,Claudia Carbone,Kristen Veinotte,Shawn B. Egri,Stephen F. Schaffner,Stephen F. Schaffner,Jacob E. Lemieux,James B. Munro,Ashique Rafique,Abhi Barve,Pardis C. Sabeti,Christos A. Kyratsous,Natalya Dudkina,Kuang Shen,Jeremy Luban +22 more
TLDR
It is shown that D614G was more infectious than the ancestral form on human lung cells, colon cells, and on cells rendered permissive by ectopic expression of human ACE2 or of ACE2 orthologs from various mammals, including Chinese rufous horseshoe bat and Malayan pangolin.About:
This article is published in Cell.The article was published on 2020-10-29 and is currently open access. It has received 840 citations till now. The article focuses on the topics: Virion membrane & Protein structure.read more
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Recognition of the SARS-CoV-2 receptor binding domain by neutralizing antibodies.
TL;DR: The binding sites and molecular features of monoclonal antibodies that target the SARS-CoV-2 RBD are reviewed, including a few that also cross-neutralize SARS -CoV.
Posted ContentDOI
Increased Resistance of SARS-CoV-2 Variant P.1 to Antibody Neutralization
Pengfei Wang,Ryan G. Casner,Manoj S. Nair,Maple Wang,Jian Yu,Gabriele Cerutti,Lihong Liu,Peter D. Kwong,Peter D. Kwong,Yaoxing Huang,Lawrence Shapiro,Lawrence Shapiro,David D. Ho,David D. Ho +13 more
TL;DR: The P.1 trimer as mentioned in this paper adopts a conformation in which one of the receptor-binding domains is in the "up" position, with the functional impact of mutations appearing to arise from local changes instead of global conformational alterations.
Posted ContentDOI
N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
Matthew McCallum,Anna De Marco,Florian A. Lempp,M. Alejandra Tortorici,Dora Pinto,Alexandra C. Walls,Martina Beltramello,Alexander Chen,Zhuoming Liu,Fabrizia Zatta,Samantha K Zepeda,Julia di Iulio,John E. Bowen,Martin Montiel-Ruiz,Jiayi Zhou,Laura E. Rosen,Siro Bianchi,Barbara Guarino,Chiara Silacci Fregni,Rana Abdelnabi,Shi Yan Caroline Foo,Paul W. Rothlauf,Louis Marie Bloyet,Fabio Benigni,Elisabetta Cameroni,Johan Neyts,Agostino Riva,Gyorgy Snell,Amalio Telenti,Sean P. J. Whelan,Herbert W. Virgin,Davide Corti,Matteo Samuele Pizzuto,David Veesler +33 more
TL;DR: In this paper, the authors describe 41 human monoclonal antibodies derived from memory B cells, which recognize the SARS-CoV-2 S N-terminal domain (NTD) and show that a subset of them neutralize SARS CoV2 ultrapotently.
Journal ArticleDOI
Enhanced binding of the N501Y-mutated SARS-CoV-2 spike protein to the human ACE2 receptor: insights from molecular dynamics simulations.
TL;DR: In this paper, the N501Y mutation within the receptor-binding domain (RBD) of the spike protein of these SARS-CoV-2 variants may enhance binding to the human angiotensin-converting enzyme 2 (hACE2).
Journal ArticleDOI
An infectivity-enhancing site on the SARS-CoV-2 spike protein targeted by antibodies
Yafei Liu,Wai Tuck Soh,Jun-ichi Kishikawa,Mika Hirose,Emi E. Nakayama,Songling Li,Miwa Sasai,Tatsuya Suzuki,Asa Tada,Akemi Arakawa,Sumiko Matsuoka,Kanako Akamatsu,Makoto Matsuda,Chikako Ono,Shiho Torii,Kazuki Kishida,Hui Jin,Wataru Nakai,Noriko Arase,Atsushi Nakagawa,Maki Matsumoto,Yukoh Nakazaki,Yasuhiro Shindo,Masako Kohyama,Keisuke Tomii,Koichiro Ohmura,Shiro Ohshima,Toru Okamoto,Masahiro Yamamoto,Hironori Nakagami,Yoshiharu Matsuura,Takayuki Kato,Masato Okada,Daron M. Standley,Tatsuo Shioda,Hisashi Arase +35 more
TL;DR: In this paper, a series of anti-spike monoclonal antibodies from coronavirus disease 2019 (COVID-19) patients were screened and found that some of the antibodies against the N-terminal domain induced the open conformation of RBD and thus enhanced the binding capacity of the spike protein to ACE2 and infectivity of SARS-CoV-2.
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