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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Drug targets, mechanisms of drug action, and therapeutics against SARS-CoV-2
TL;DR: An overview of various attempts made to design different therapeutic agents against various structural and non-structural proteins of SARS-CoV-2 has been summarized in this article, where emphasis has been made to highlight the mechanisms of drug action and ways to design better inhibitors of these proteins.
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An infectivity-enhancing site on the SARS-CoV-2 spike protein is targeted by COVID-19 patient antibodies
Yafei Liu,Wai Tuck Soh,Asa Tada,Akemi Arakawa,Sumiko Matsuoka,Emi E. Nakayama,Songling Li,Chikako Ono,Shiho Torii,Kazuki Kishida,Hui Jin,Wataru Nakai,Noriko Arase,Atsushi Nakagawa,Yasuhiro Shindo,Masako Kohyama,Hironori Nakagami,Keisuke Tomii,Koichiro Ohmura,Shiro Ohshima,Masato Okada,Yoshiharu Matsuura,Daron M. Standley,Tatsuo Shioda,Hisashi Arase +24 more
TL;DR: The production of antibodies against SARS-CoV-2 infectivity-enhancing site could be considered as a possible exacerbating factors for COVID-19 and that a spike protein lacking such antibody epitopes may be required for safe vaccine development, especially for individuals with pre-existing enhancing antibodies.
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Structural and molecular perspectives of SARS-CoV-2.
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Insights into COVID-19 Vaccine Development Based on Immunogenic Structural Proteins of SARS-CoV-2, Host Immune Responses, and Herd Immunity
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Allosteric perspective on the mutability and druggability of the SARS-CoV-2 Spike protein
TL;DR: In this paper , the structure and dynamics of the SARS-CoV-2 Spike protein were investigated, and exhaustive allosteric signaling and probing maps provided a comprehensive picture of allostery in the spike protein.
References
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