Designed, highly expressing, thermostable dengue virus 2 envelope protein dimers elicit quaternary epitope antibodies-Reference-Cited by-同舟云学术

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

Published:2021-10-15 Issue:42 Volume:7 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Kudlacek Stephan T.¹^ORCID,Metz Stefan²^ORCID,Thiono Devina²^ORCID,Payne Alexander M.¹^ORCID,Phan Thanh T. N.¹^ORCID,Tian Shaomin²^ORCID,Forsberg Lawrence J.³^ORCID,Maguire Jack¹^ORCID,Seim Ian⁴⁵⁶^ORCID,Zhang Shu¹^ORCID,Tripathy Ashutosh¹,Harrison Joseph¹^ORCID,Nicely Nathan I.³^ORCID,Soman Sandrine⁷,McCracken Michael K.⁷^ORCID,Gromowski Gregory D.⁷,Jarman Richard G.⁷^ORCID,Premkumar Lakshmanane²^ORCID,de Silva Aravinda M.²^ORCID,Kuhlman Brian¹⁵^ORCID

Affiliation:

1. Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27514, USA.

2. Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27514, USA.

3. Department of Pharmacology, University of North Carolina, Chapel Hill, NC 27514, USA.

4. Curriculum in Bioinformatics and Computational Biology, University of North Carolina, Chapel Hill, NC 27514, USA.

5. Department of Biology, University of North Carolina, Chapel Hill, NC 27514, USA.

6. Department of Applied Physical Sciences, University of North Carolina, Chapel Hill, NC 27514, USA.

7. Viral Diseases Branch, Walter Reed Army Institute of Research, Silver Spring, MD 20910, USA.

Abstract

A stabilized dimer of the surface protein from dengue virus has been engineered to elicit antibodies that neutralize the virus.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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