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7UTR

CPV Affinity Purified Polyclonal Fab B Site Fab

This is a non-PDB format compatible entry.
Summary for 7UTR
Entry DOI10.2210/pdb7utr/pdb
EMDB information26787
DescriptorCapsid protein VP1, Light chain antibody fragment, Heavy chain antibody fragment (3 entities in total)
Functional Keywordscpv, polyclonal fab, b site, vaccination, virus, virus-immune system complex, virus/immune system
Biological sourceCanine parvovirus type 2 (isolate Dog/United States/CPV-b/1978) (CPV-2)
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Total number of polymer chains10
Total formula weight509726.15
Authors
Hartmann, S.R.,Hafenstein, S.L.,Charnesky, A.J. (deposition date: 2022-04-27, release date: 2023-10-04)
Primary citationHartmann, S.R.,Charnesky, A.J.,Fruh, S.P.,Lopez-Astacio, R.A.,Weichert, W.S.,DiNunno, N.,Cho, S.H.,Bator, C.M.,Parrish, C.R.,Hafenstein, S.L.
Cryo EM structures map a post vaccination polyclonal antibody response to canine parvovirus.
Commun Biol, 6:955-955, 2023
Cited by
PubMed Abstract: Canine parvovirus (CPV) is an important pathogen that emerged by cross-species transmission to cause severe disease in dogs. To understand the host immune response to vaccination, sera from dogs immunized with parvovirus are obtained, the polyclonal antibodies are purified and used to solve the high resolution cryo EM structures of the polyclonal Fab-virus complexes. We use a custom software, Icosahedral Subparticle Extraction and Correlated Classification (ISECC) to perform subparticle analysis and reconstruct polyclonal Fab-virus complexes from two different dogs eight and twelve weeks post vaccination. In the resulting polyclonal Fab-virus complexes there are a total of five distinct Fabs identified. In both cases, any of the five antibodies identified would interfere with receptor binding. This polyclonal mapping approach identifies a specific, limited immune response to the live vaccine virus and allows us to investigate the binding of multiple different antibodies or ligands to virus capsids.
PubMed: 37726539
DOI: 10.1038/s42003-023-05319-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

227111

數據於2024-11-06公開中

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