Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai,Yongfei Cai,Jun Zhang,Jun Zhang,Tianshu Xiao,Tianshu Xiao,Hanqin Peng,Sarah M. Sterling,Richard M. Walsh,Shaun Rawson,Sophia Rits-Volloch,Bing Chen,Bing Chen +12 more
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TLDR
Two cryo–electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion and postfusion conformations, are reported, advancing the understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.Abstract:
Intervention strategies are urgently needed to control the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. The trimeric viral spike (S) protein catalyzes fusion between viral and target cell membranes to initiate infection. Here, we report two cryo-electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion (2.9-angstrom resolution) and postfusion (3.0-angstrom resolution) conformations, respectively. The spontaneous transition to the postfusion state is independent of target cells. The prefusion trimer has three receptor-binding domains clamped down by a segment adjacent to the fusion peptide. The postfusion structure is strategically decorated by N-linked glycans, suggesting possible protective roles against host immune responses and harsh external conditions. These findings advance our understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.read more
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SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination.
Markus Hoffmann,Markus Hoffmann,Heike Hofmann-Winkler,Nadine Krüger,Amy Kempf,Amy Kempf,Inga Nehlmeier,Luise Graichen,Luise Graichen,Prerna Arora,Prerna Arora,Anzhalika Sidarovich,Anzhalika Sidarovich,Anna-Sophie Moldenhauer,Martin Sebastian Winkler,Sebastian R. Schulz,Hans-Martin Jäck,Metodi V. Stankov,Georg M. N. Behrens,Stefan Pöhlmann,Stefan Pöhlmann +20 more
TL;DR: In this paper, the authors analyzed whether B.1.617 is more adept in entering cells and/or evades antibody responses, and they found that antibody evasion may contribute to the rapid spread of this variant.
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Heparan sulfate assists SARS-CoV-2 in cell entry and can be targeted by approved drugs in vitro
Qi Zhang,Catherine Z. Chen,Manju Swaroop,Miao Xu,Lihui Wang,Juhyung Lee,Amy Wang,Manisha Pradhan,Natalie Hagen,Lu Chen,Min Shen,Zhiji Luo,Xin Xu,Yue Xu,Wenwei Huang,Wei Zheng,Yihong Ye +16 more
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Comprehensive analysis of T cell immunodominance and immunoprevalence of SARS-CoV-2 epitopes in COVID-19 cases
Alison Tarke,Alison Tarke,John Sidney,Conner K. Kidd,Jennifer M. Dan,Jennifer M. Dan,Sydney I. Ramirez,Sydney I. Ramirez,Esther Dawen Yu,Jose Mateus,Ricardo da Silva Antunes,Erin Moore,Paul Rubiro,Nils Methot,Elizabeth J. Phillips,Simon Mallal,April Frazier,Stephen A. Rawlings,Jason A. Greenbaum,Bjoern Peters,Bjoern Peters,Davey M. Smith,Shane Crotty,Shane Crotty,Daniela Weiskopf,Alba Grifoni,Alessandro Sette,Alessandro Sette +27 more
TL;DR: To establish the patterns of immunodominance of different SARS-CoV-2 antigens, and precisely measure virus-specific CD4+ and CD8+ T cells, epitope-specific T cell responses of approximately 100 convalescent COVID-19 cases are studied.
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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