欢迎光临~杭州纽罗西敏生物科技有限公司
  咨询电话:0571-88254427

行业新闻及文献

Distinct conformational states of SARS-CoV-2 spike protein

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.

联系我们

联系人:

手 机:0571-88254427

邮 箱:info@neuro-hemin.com

公 司:杭州纽罗西敏生物科技有限公司

地 址:杭州市教工路316号