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5U4R

Crystal structure of the broadly neutralizing Influenza A antibody VRC 315 53-1A09 Fab.

Summary for 5U4R
Entry DOI10.2210/pdb5u4r/pdb
DescriptorVRC 315 53-1A09 Fab Heavy chain, VRC 315 53-1A09 Fab Light chain (3 entities in total)
Functional Keywordsimmune system, antibody, influenza, human vaccine trial
Biological sourceHomo sapiens
More
Total number of polymer chains4
Total formula weight97074.20
Authors
Joyce, M.G.,Andrews, S.F.,Mascola, J.R.,McDermott, A.B.,Kwong, P.D. (deposition date: 2016-12-05, release date: 2017-11-15, Last modification date: 2024-10-16)
Primary citationAndrews, S.F.,Joyce, M.G.,Chambers, M.J.,Gillespie, R.A.,Kanekiyo, M.,Leung, K.,Yang, E.S.,Tsybovsky, Y.,Wheatley, A.K.,Crank, M.C.,Boyington, J.C.,Prabhakaran, M.S.,Narpala, S.R.,Chen, X.,Bailer, R.T.,Chen, G.,Coates, E.,Kwong, P.D.,Koup, R.A.,Mascola, J.R.,Graham, B.S.,Ledgerwood, J.E.,McDermott, A.B.
Preferential induction of cross-group influenza A hemagglutinin stem-specific memory B cells after H7N9 immunization in humans.
Sci Immunol, 2:-, 2017
Cited by
PubMed Abstract: Antigenic drift and shift of influenza strains underscore the need for broadly protective influenza vaccines. One strategy is to design immunogens that elicit B cell responses against conserved epitopes on the hemagglutinin (HA) stem. To better understand the elicitation of HA stem-targeted B cells to group 1 and group 2 influenza subtypes, we compared the memory B cell response to group 2 H7N9 and group 1 H5N1 vaccines in humans. Upon H7N9 vaccination, almost half of the HA stem-specific response recognized the group 1 and group 2 subtypes, whereas the response to H5N1 was largely group 1-specific. Immunoglobulin repertoire analysis of HA-specific B cells indicated that the H7N9 and H5N1 vaccines induced genetically similar cross-group HA stem-binding B cells, albeit at a much higher frequency upon H7N9 vaccination. These data suggest that a group 2-based stem immunogen could prove more effective than a group 1 immunogen at eliciting broad cross-group protection in humans.
PubMed: 28783708
DOI: 10.1126/sciimmunol.aan2676
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.762 Å)
Structure validation

226707

數據於2024-10-30公開中

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