Effect of natural mutations of SARS-CoV-2 on spike structure, conformation, and antigenicity

Author:

Gobeil Sophie M.-C.1ORCID,Janowska Katarzyna1,McDowell Shana1ORCID,Mansouri Katayoun1,Parks Robert1ORCID,Stalls Victoria1ORCID,Kopp Megan F.1,Manne Kartik1ORCID,Li Dapeng1,Wiehe Kevin12ORCID,Saunders Kevin O.1345ORCID,Edwards Robert J.12ORCID,Korber Bette6ORCID,Haynes Barton F.125ORCID,Henderson Rory12ORCID,Acharya Priyamvada137ORCID

Affiliation:

1. Duke Human Vaccine Institute, Durham, NC 27710, USA.

2. Department of Medicine, Duke University, Durham, NC 27710, USA.

3. Department of Surgery, Duke University, Durham, NC 27710, USA.

4. Department of Molecular Genetics and Microbiology, Duke University, Durham, NC 27710, USA.

5. Department of Immunology, Duke University, Durham, NC 27710, USA.

6. Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.

7. Department of Biochemistry, Duke University, Durham, NC 27710, USA.

Abstract

SARS-CoV-2 from alpha to epsilon As battles to contain the COVID-19 pandemic continue, attention is focused on emerging variants of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virus that have been deemed variants of concern because they are resistant to antibodies elicited by infection or vaccination or they increase transmissibility or disease severity. Three papers used functional and structural studies to explore how mutations in the viral spike protein affect its ability to infect host cells and to evade host immunity. Gobeil et al . looked at a variant spike protein involved in transmission between minks and humans, as well as the B1.1.7 (alpha), B.1.351 (beta), and P1 (gamma) spike variants; Cai et al . focused on the alpha and beta variants; and McCallum et al . discuss the properties of the spike protein from the B1.1.427/B.1.429 (epsilon) variant. Together, these papers show a balance among mutations that enhance stability, those that increase binding to the human receptor ACE2, and those that confer resistance to neutralizing antibodies. —VV

Funder

National Institutes of Health

NC State CARE funding for COVID research

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3