6Q23

Crystal structure of human 1G01 Fab in complex with influenza virus neuraminidase from A/California/04/2009 (H1N1)

Summary for 6Q23

• Entry DOI: 10.2210/pdb6q23/pdb
• Descriptor: Neuraminidase, 1G01 Fab IgG1 heavy chain, 1G01 Fab kappa light chain, ... (5 entities in total)
• Functional Keywords: broadly protective human antibody, inhibition, active site, antibody-neuraminidase complex, viral protein, hydrolase-immune system complex, hydrolase/immune system
• Biological source: Influenza A virus (A/California/04/2009 (H1N1); More
• Total number of polymer chains: 12
• Total formula weight: 372639.03

Authors

Zhu, X.,Wilson, I.A. (deposition date: 2019-08-06, release date: 2019-10-23, Last modification date: 2024-10-30)

Primary citation

Stadlbauer, D.,Zhu, X.,McMahon, M.,Turner, J.S.,Wohlbold, T.J.,Schmitz, A.J.,Strohmeier, S.,Yu, W.,Nachbagauer, R.,Mudd, P.A.,Wilson, I.A.,Ellebedy, A.H.,Krammer, F.
Broadly protective human antibodies that target the active site of influenza virus neuraminidase.
Science, 366:499-504, 2019

PubMed Abstract: 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.

PubMed: 31649200
DOI: 10.1126/science.aay0678

Experimental method

X-RAY DIFFRACTION (3.27 Å)