Summary for 7UTS
| Entry DOI | 10.2210/pdb7uts/pdb |
| EMDB information | 26788 |
| Descriptor | Capsid protein VP1, Light chain antibody fragment, Heavy chain antibody fragment (3 entities in total) |
| Functional Keywords | cpv, polyclonal fab, a site, vaccination, virus, virus-immune system complex, virus/immune system |
| Biological source | Canis lupus familiaris (dog) More |
| Total number of polymer chains | 10 |
| Total formula weight | 509811.26 |
| Authors | Hartmann, S.R.,Hafenstein, S.L.,Charnesky, A.J. (deposition date: 2022-04-27, release date: 2023-10-04, Last modification date: 2024-10-16) |
| Primary citation | Hartmann, 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: 37726539DOI: 10.1038/s42003-023-05319-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
Download full validation report
