6IW1

Crystal structure of YFV-17D sE in postfusion state

Summary for 6IW1

• Entry DOI: 10.2210/pdb6iw1/pdb
• Descriptor: Envelope protein E (1 entity in total)
• Functional Keywords: yellow fever virus, envelope protein, flavivirus, viral protein
• Biological source: Yellow fever virus (strain 17D vaccine) (YFV)
• Total number of polymer chains: 3
• Total formula weight: 129704.54

Authors

Lu, X.S.,Xiao, H.X.,Li, S.H.,Pang, X.F. (deposition date: 2018-12-04, release date: 2019-02-13, Last modification date: 2024-10-30)

Primary citation

Lu, X.,Xiao, H.,Li, S.,Pang, X.,Song, J.,Liu, S.,Cheng, H.,Li, Y.,Wang, X.,Huang, C.,Guo, T.,Ter Meulen, J.,Daffis, S.,Yan, J.,Dai, L.,Rao, Z.,Klenk, H.D.,Qi, J.,Shi, Y.,Gao, G.F.
Double Lock of a Human Neutralizing and Protective Monoclonal Antibody Targeting the Yellow Fever Virus Envelope.
Cell Rep, 26:438-446.e5, 2019

PubMed Abstract: Yellow fever virus (YFV), a deadly human pathogen, is the prototype of the genus Flavivirus. Recently, YFV re-emerged in Africa and Brazil, leading to hundreds of deaths, with some cases imported to China. Prophylactic or therapeutic countermeasures are urgently needed. Previously, several human monoclonal antibodies against YFV were screened out by phage display. Here, we find that one of them, 5A, exhibits high neutralizing potency and good protection. Crystallographic analysis of the YFV envelope (E) protein in its pre- and post-fusion states shows conformations similar to those observed in other E proteins of flaviviruses. Furthermore, the structures of 5A in complex with the E protein in both states are resolved, revealing an invariant recognition site. Structural analysis and functional data suggest that 5A has high neutralization potency because it interferes with virus entry by preventing both virus attachment and fusion. These findings will be instrumental for immunogen or inhibitor design.

PubMed: 30625326
DOI: 10.1016/j.celrep.2018.12.065

Experimental method

X-RAY DIFFRACTION (3.1 Å)