1EO8

INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY

Summary for 1EO8

• Entry DOI: 10.2210/pdb1eo8/pdb
• Descriptor: HEMAGGLUTININ (HA1 CHAIN), HEMAGGLUTININ (HA2 CHAIN), ANTIBODY (LIGHT CHAIN), ... (8 entities in total)
• Functional Keywords: complex (hemagglutinin-immmunoglobulin), hemagglutinin, immunoglobulin, viral protein, immune system complex, viral protein-immune system complex, viral protein/immune system
• Biological source: Influenza A virus (A/X-31(H3N2)); More
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P03437 P03437
• Total number of polymer chains: 4
• Total formula weight: 104236.02

Authors

Fleury, D.,Gigant, B.,Daniels, R.S.,Skehel, J.J.,Knossow, M.,Bizebard, T. (deposition date: 2000-03-22, release date: 2000-04-12, Last modification date: 2024-11-20)

Primary citation

Fleury, D.,Daniels, R.S.,Skehel, J.J.,Knossow, M.,Bizebard, T.
Structural evidence for recognition of a single epitope by two distinct antibodies.
Proteins, 40:572-578, 2000

PubMed Abstract: The structure of a complex between the hemagglutinin of influenza virus and the Fab of a neutralizing antibody was determined by X-ray crystallography at 2.8 A resolution. This antibody and another which has only 56% sequence identity bind to the same epitope with very similar affinities and in the same orientation. One third of the interactions is conserved in the two complexes; a significant proportion of the interactions that differ are established by residues of the H3 complementarity-determining regions (CDR) which adopt distinct conformations in the two antibodies. This demonstrates that there is a definite flexibility in the selection of antibodies that bind to a given epitope, despite the high affinity of their complexes. This flexibility allows the humoral immune response to be redundant, a feature that may be useful in achieving longer lasting protection against evolving viral pathogens.

PubMed: 10899782
DOI: 10.1002/1097-0134(20000901)40:4<572::AID-PROT30>3.3.CO;2-E

Experimental method

X-RAY DIFFRACTION (2.8 Å)