6HJQ

Structure of Full-length Influenza Hemagglutinin (A/duck/Alberta/35/76) in complex with FISW84 Fab Fragment

Summary for 6HJQ

• Entry DOI: 10.2210/pdb6hjq/pdb
• EMDB information: 0236
• Descriptor: Hemagglutinin, Heavy chain of FISW84 Fab, Light chain of FISW84 Fab, ... (8 entities in total)
• Functional Keywords: influenza virus, hemagglutinin, membrane protein, membrane fusion, viral protein
• Biological source: Homo sapiens; More
• Total number of polymer chains: 12
• Total formula weight: 322903.90

Authors

Benton, D.J.,Rosenthal, P.B. (deposition date: 2018-09-04, release date: 2018-09-26, Last modification date: 2024-10-09)

Primary citation

Benton, D.J.,Nans, A.,Calder, L.J.,Turner, J.,Neu, U.,Lin, Y.P.,Ketelaars, E.,Kallewaard, N.L.,Corti, D.,Lanzavecchia, A.,Gamblin, S.J.,Rosenthal, P.B.,Skehel, J.J.
Influenza hemagglutinin membrane anchor.
Proc. Natl. Acad. Sci. U.S.A., 115:10112-10117, 2018

PubMed Abstract: Viruses with membranes fuse them with cellular membranes, to transfer their genomes into cells at the beginning of infection. For Influenza virus, the membrane glycoprotein involved in fusion is the hemagglutinin (HA), the 3D structure of which is known from X-ray crystallographic studies. The soluble ectodomain fragments used in these studies lacked the "membrane anchor" portion of the molecule. Since this region has a role in membrane fusion, we have determined its structure by analyzing the intact, full-length molecule in a detergent micelle, using cryo-EM. We have also compared the structures of full-length HA-detergent micelles with full-length HA-Fab complex detergent micelles, to describe an infectivity-neutralizing monoclonal Fab that binds near the ectodomain membrane anchor junction. We determine a high-resolution HA structure which compares favorably in detail with the structure of the ectodomain seen by X-ray crystallography; we detect, clearly, all five carbohydrate side chains of HA; and we find that the ectodomain is joined to the membrane anchor by flexible, eight-residue-long, linkers. The linkers extend into the detergent micelle to join a central triple-helical structure that is a major component of the membrane anchor.

PubMed: 30224494
DOI: 10.1073/pnas.1810927115

Experimental method

ELECTRON MICROSCOPY (4.1 Å)