| Autor: |
Yajima, Hisano, Anraku, Yuki, Kaku, Yu, Kimura, Kanako Terakado, Plianchaisuk, Arnon, Okumura, Kaho, Nakada-Nakura, Yoshiko, Atarashi, Yusuke, Hemmi, Takuya, Kuroda, Daisuke, Takahashi, Yoshimasa, Kita, Shunsuke, Sasaki, Jiei, Sumita, Hiromi, Matsuno, Keita, Nao, Naganori, Sawa, Hirofumi, Mizuma, Keita, Li, Jingshu, Kida, Izumi |
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| Zdroj: |
Nature Communications; 10/7/2024, Vol. 15 Issue 1, p1-14, 14p |
| Abstrakt: |
Since 2019, SARS-CoV-2 has undergone mutations, resulting in pandemic and epidemic waves. The SARS-CoV-2 spike protein, crucial for cellular entry, binds to the ACE2 receptor exclusively when its receptor-binding domain (RBD) adopts the up-conformation. However, whether ACE2 also interacts with the RBD in the down-conformation to facilitate the conformational shift to RBD-up remains unclear. Herein, we present the structures of the BA.2.86 and the JN.1 spike proteins bound to ACE2. Notably, we successfully observed the ACE2-bound down-RBD, indicating an intermediate structure before the RBD-up conformation. The wider and mobile angle of RBDs in the up-state provides space for ACE2 to interact with the down-RBD, facilitating the transition to the RBD-up state. The K356T, but not N354-linked glycan, contributes to both of infectivity and neutralizing-antibody evasion in BA.2.86. These structural insights the spike-protein dynamics would help understand the mechanisms underlying SARS-CoV-2 infection and its neutralization. JN.1 lineage is a globally dominant variant of SARS-CoV-2. Here, the authors examine structural insights into the BA.2.86 and JN.1 spike dynamics to help understand the mechanisms underlying SARS-CoV-2 infection and its neutralizing-antibody evasion. [ABSTRACT FROM AUTHOR] |
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Complementary Index |
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