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7CN2

Subparticle refinement of human papillomavirus type 16 pesudovirus in complex with H16.001 Fab

Summary for 7CN2
Entry DOI10.2210/pdb7cn2/pdb
EMDB information30414
DescriptorThe light chain variable region of H16.001 Fab fragment, The heavy chain variable region of H16.001 Fab fragment, Major capsid protein L1 (3 entities in total)
Functional Keywordsvirus, immune complex, immune system-viral protein complex, immune system/viral protein
Biological sourceHuman papillomavirus type 16
More
Total number of polymer chains18
Total formula weight486381.04
Authors
He, M.Z.,Li, S.W. (deposition date: 2020-07-29, release date: 2020-09-02, Last modification date: 2024-10-23)
Primary citationHuang, W.,He, M.,Ning, T.,Nie, J.,Zhang, F.,Zheng, Q.,Zhang, R.,Xu, Y.,Gu, Y.,Li, S.,Wang, Y.
Structural characterization of a neutralizing mAb H16.001, a potent candidate for a common potency assay for various HPV16 VLPs.
Npj Vaccines, 5:89-89, 2020
Cited by
PubMed Abstract: With more human papillomavirus (HPV) virus-like particle (VLP) vaccines to hit the market in future, a monoclonal antibody (mAb) with preferably comparable reactivity against vaccines from different expression systems and bioprocesses is urgently needed for the potency characterization. Among all mAbs against HPV16 collected, rabbit mAb H16.001 is potently neutralizing with the highest affinity, recognizes an immune-dominant epitope, and can comparably react with HPV16 vaccines from various sources. Cryo-electron microscopic (cryo-EM) structure demonstrated that 360 H16.001 Fabs could bind to HPV16 capsid in preferable binding manner without steric hindrance between neighboring Fabs, potentially supporting its identification for VLP structural integrity and utility in monitoring VLP structural probity. This structural analysis indicated that mAb H16.001 afforded unbiased potency characterization for various HPV16 vaccines and was potential for use in vaccine regulation practice. This study also showed a model process for selecting suitable mAbs for potency assays of other vaccines.
PubMed: 33042588
DOI: 10.1038/s41541-020-00236-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.43 Å)
Structure validation

226707

數據於2024-10-30公開中

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