Designed, highly expressing, thermostable dengue virus 2 envelope protein dimers elicit quaternary epitope antibodies

Authors :: Michael K. McCracken
Stephan T. Kudlacek
Devina J Thiono
Jack Maguire
Aravinda M. de Silva
Thanh T. N. Phan
Alexander Matthew Payne
Sandrine Soman
Nathan I. Nicely
Richard G. Jarman
Shu Zhang
Ashutosh Tripathy
Stefan W. Metz
Joseph S. Harrison
Lawrence J. Forsberg
Lakshmanane Premkumar
Gregory D. Gromowski
Ian Seim
Brian Kuhlman
Shaomin Tian
Source :: Science Advances
Publication Year :: 2021
Publisher :: American Association for the Advancement of Science (AAAS), 2021.
Abstract: Description<br />A stabilized dimer of the surface protein from dengue virus has been engineered to elicit antibodies that neutralize the virus.<br />Dengue virus (DENV) is a worldwide health burden, and a safe vaccine is needed. Neutralizing antibodies bind to quaternary epitopes on DENV envelope (E) protein homodimers. However, recombinantly expressed soluble E proteins are monomers under vaccination conditions and do not present these quaternary epitopes, partly explaining their limited success as vaccine antigens. Using molecular modeling, we found DENV2 E protein mutations that induce dimerization at low concentrations (

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