| identifier: | 1931359 |
| description: |
epitope description:HA1: E341; HA2: E360, G361, I363, D364, R370, E375, T377, G378, Q379, A380, A381, L383, N491, E495 + GLYC(2:N499)
antigen name:Hemagglutinin
host organism:Homo sapiens
antibody name:CR8020
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
21737702 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1022349 |
| landingPage: |
http://www.iedb.org/assay/1931359 |
| type: |
Literature
|
| publicationVenue: |
Science
|
| dates: |
2011
|
| study type: | b cell assays |
| subject species: | Influenza A virus (A/Hong Kong/1/1968(H3N2)) |
| fullName: |
Damian C Ekiert
Robert H E Friesen
Gira Bhabha
Ted Kwaks
Mandy Jongeneelen
Wenli Yu
Carla Ophorst
Freek Cox
Hans J W M Korse
Boerries Brandenburg
Ronald Vogels
Just P J Brakenhoff
Ronald Kompier
Martin H Koldijk
Lisette A H M Cornelissen
Leo L M Poon
Malik Peiris
Wouter Koudstaal
Ian A Wilson
Jaap Goudsmit
|
| method: |
bio-layer interferometry assay
|
| name: |
A highly conserved neutralizing epitope on group 2 influenza A viruses.
|
| description: |
The epitope specific Fab CR8020 bound to hemmagglutin from the influenza virus, as well as to HAs (H3,H4, H7, H10, H14, H15) from other group 2 subtype viruses, but did not bind to HAs (H1, H5, H6 H9, H13, H16) from group 1 subtype influenza viruses. KD's were determined by bio-layer interferometry, which is conceptually similar to surface plasmon resonance. Most single amino acid substitutions of the epitope residues did significantly reduce binding. Mutants D19N and G33E, also selected as escape mutants with CR8020, had about 300-fold decreased affinity.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |