5LBS

structural basis of Zika and Dengue virus potent antibody cross-neutralization

Summary for 5LBS

• Entry DOI: 10.2210/pdb5lbs/pdb
• Related: 4UTA 4UTB
• Descriptor: envelope protein E, BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C8, 1,2-ETHANEDIOL, ... (6 entities in total)
• Functional Keywords: immune system-viral protein complex, zika virus, broadly neutralizing antibody, immune system-viral protein
• Biological source: Zika virus (ZIKV); More
• Total number of polymer chains: 6
• Total formula weight: 158934.27

Authors

Vaney, M.C.,Rouvinski, A.,Barba-Spaeth, G.,Rey, F.A. (deposition date: 2016-06-17, release date: 2016-07-06, Last modification date: 2024-10-16)

Primary citation

Barba-Spaeth, G.,Dejnirattisai, W.,Rouvinski, A.,Vaney, M.C.,Medits, I.,Sharma, A.,Simon-Loriere, E.,Sakuntabhai, A.,Cao-Lormeau, V.M.,Haouz, A.,England, P.,Stiasny, K.,Mongkolsapaya, J.,Heinz, F.X.,Screaton, G.R.,Rey, F.A.
Structural basis of potent Zika-dengue virus antibody cross-neutralization.
Nature, 536:48-53, 2016

PubMed Abstract: Zika virus is a member of the Flavivirus genus that had not been associated with severe disease in humans until the recent outbreaks, when it was linked to microcephaly in newborns in Brazil and to Guillain-Barré syndrome in adults in French Polynesia. Zika virus is related to dengue virus, and here we report that a subset of antibodies targeting a conformational epitope isolated from patients with dengue virus also potently neutralize Zika virus. The crystal structure of two of these antibodies in complex with the envelope protein of Zika virus reveals the details of a conserved epitope, which is also the site of interaction of the envelope protein dimer with the precursor membrane (prM) protein during virus maturation. Comparison of the Zika and dengue virus immunocomplexes provides a lead for rational, epitope-focused design of a universal vaccine capable of eliciting potent cross-neutralizing antibodies to protect simultaneously against both Zika and dengue virus infections.

PubMed: 27338953
DOI: 10.1038/nature18938

Experimental method

X-RAY DIFFRACTION (2.41 Å)