6S8D

Structure of ZEBOV GP in complex with 1T0227 antibody

Summary for 6S8D

• Entry DOI: 10.2210/pdb6s8d/pdb
• EMDB information: 10118
• Descriptor: Light chain, Heavy chain, Envelope glycoprotein, ... (5 entities in total)
• Functional Keywords: ebola, glycoprotein, antibodies, viral protein
• Biological source: Homo sapiens; More
• Total number of polymer chains: 12
• Total formula weight: 309021.11

Authors

Diskin, R.,Cohen-Dvashi, H. (deposition date: 2019-07-09, release date: 2020-02-12, Last modification date: 2020-07-29)

Primary citation

Cohen-Dvashi, H.,Zehner, M.,Ehrhardt, S.,Katz, M.,Elad, N.,Klein, F.,Diskin, R.
Structural Basis for a Convergent Immune Response against Ebola Virus.
Cell Host Microbe, 27:418-427.e4, 2020

PubMed Abstract: Ebola virus disease is a severe health problem in Africa. Vaccines that display the Zaire ebolavirus glycoprotein spike complex are a prime component for the effort to combat it. The V3-15/V1-40-based class of antibodies was recently discovered to be a common response in individuals who received the Ebola virus vaccines. These antibodies display attractive properties, and thus likely contribute to the efficacy of the vaccines. Here, we use cryo-EM to elucidate how three V3-15/V1-40 antibodies from different individuals target the virus and found a convergent mechanism against a partially conserved site on the spike complex. Our study rationalizes the selection of the V3-15/V1-40 germline genes for specifically targeting this site and highlights Ebolavirus species-specific sequence divergences that may restrict breadth of V3-15/V1-40-based humoral response. The results from this study could help develop improved immunization schemes and further enable the design of immunogens that would be efficacious against a broader set of Ebolavirus species.

PubMed: 32059794
DOI: 10.1016/j.chom.2020.01.007

Experimental method

ELECTRON MICROSCOPY (3.49 Å)