Broadly protective human antibodies that target the active site of influenza virus neuraminidase

Author:

Stadlbauer Daniel12ORCID,Zhu Xueyong3ORCID,McMahon Meagan1ORCID,Turner Jackson S.4ORCID,Wohlbold Teddy J.156ORCID,Schmitz Aaron J.4ORCID,Strohmeier Shirin1,Yu Wenli3,Nachbagauer Raffael1ORCID,Mudd Philip A.7ORCID,Wilson Ian A.38ORCID,Ellebedy Ali H.4,Krammer Florian1ORCID

Affiliation:

1. Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA.

2. Department of Biotechnology, University of Natural Resources and Life Sciences, A-1190 Vienna, Austria.

3. Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

4. Division of Immunobiology, Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.

5. Department of Pediatrics, Columbia Irving Medical Center, New York, NY 10032, USA.

6. NewYork-Presbyterian Morgan Stanley Children’s Hospital, New York, NY 10032, USA.

7. Division of Emergency Medicine, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, USA.

8. Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Abstract

Alternative influenza target There is a pressing need for a broadly protective influenza vaccine that can neutralize this constantly varying, deadly virus. Stadlbauer et al. turned their attention away from the current vaccine target—the mutable hemagglutinin—and investigated an alternative, less variable virus-coat glycoprotein: neuraminidase. The authors extracted monoclonal antibodies (mAbs) from a human donor naturally infected with the H3N2 virus subtype. In mice, the mAbs were broadly protective against influenza virus A groups 1 and 2 (human, avian, and swine origin) and some influenza B viruses. These mAbs were also therapeutically effective as late as 72 hours after infection. The wide range of reactivity probably relates to the infection history of the donor, whose plasmablasts generated antibodies with long regions that insert into the active site of the neuraminidase enzyme. Science , this issue p. 499

Funder

U.S. Department of Energy

National Cancer Institute

National Institute of General Medical Sciences

National Institute of Allergy and Infectious Diseases

National Center for Advancing Translational Sciences

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