TY - JOUR
T1 - Broadly protective human antibodies that target the active site of influenza virus neuraminidase
AU - Stadlbauer, Daniel
AU - Zhu, Xueyong
AU - McMahon, Meagan
AU - Turner, Jackson S.
AU - Wohlbold, Teddy J.
AU - Schmitz, Aaron J.
AU - Strohmeier, Shirin
AU - Yu, Wenli
AU - Nachbagauer, Raffael
AU - Mudd, Philip A.
AU - Wilson, Ian A.
AU - Ellebedy, Ali H.
AU - Krammer, Florian
N1 - Publisher Copyright:
© 2019 American Association for the Advancement of Science. All rights reserved.
PY - 2019/10/25
Y1 - 2019/10/25
N2 - Better vaccines against influenza virus are urgently needed to provide broader protection against diverse strains, subtypes, and types. Such efforts are assisted by the identification of novel broadly neutralizing epitopes targeted by protective antibodies. Influenza vaccine development has largely focused on the hemagglutinin, but the other major surface antigen, the neuraminidase, has reemerged as a potential target for universal vaccines. We describe three human monoclonal antibodies isolated from an H3N2-infected donor that bind with exceptional breadth to multiple different influenza A and B virus neuraminidases. These antibodies neutralize the virus, mediate effector functions, are broadly protective in vivo, and inhibit neuraminidase activity by directly binding to the active site. Structural and functional characterization of these antibodies will inform the development of neuraminidase-based universal vaccines against influenza virus.
AB - Better vaccines against influenza virus are urgently needed to provide broader protection against diverse strains, subtypes, and types. Such efforts are assisted by the identification of novel broadly neutralizing epitopes targeted by protective antibodies. Influenza vaccine development has largely focused on the hemagglutinin, but the other major surface antigen, the neuraminidase, has reemerged as a potential target for universal vaccines. We describe three human monoclonal antibodies isolated from an H3N2-infected donor that bind with exceptional breadth to multiple different influenza A and B virus neuraminidases. These antibodies neutralize the virus, mediate effector functions, are broadly protective in vivo, and inhibit neuraminidase activity by directly binding to the active site. Structural and functional characterization of these antibodies will inform the development of neuraminidase-based universal vaccines against influenza virus.
UR - http://www.scopus.com/inward/record.url?scp=85074108269&partnerID=8YFLogxK
U2 - 10.1126/science.aay0678
DO - 10.1126/science.aay0678
M3 - Article
C2 - 31649200
AN - SCOPUS:85074108269
SN - 0036-8075
VL - 366
SP - 499
EP - 504
JO - Science
JF - Science
IS - 6464
ER -