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https://www.arca.fiocruz.br/handle/icict/20494
DE NOVO DESIGN AND BIOPHYSICAL CHARACTERIZATION OF AN AFFINITY-ENHANCED PROTEIN DISPLAYING THE STRUCTURE OF THE BROADLY NEUTRALIZING HIV-1 2F5 ANTIBODY EPITOPE
Author
Affilliation
Center for Vaccine Research and Infectious Diseases and Microbiology Department. University of Pittsburgh. Pittsburgh, PA, USA.
Microbiology and Molecular Genetics Department. University of Pittsburgh. Pittsburgh, PA, USA.
Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.
Microbiology and Molecular Genetics Department. University of Pittsburgh. Pittsburgh, PA, USA.
Infectious Diseases and Microbiology Department. University of Pittsburgh. Pittsburgh, PA, USA.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Recife, PE, Brasil.
Microbiology and Molecular Genetics Department. University of Pittsburgh. Pittsburgh, PA, USA.
Microbiology and Molecular Genetics Department. University of Pittsburgh. Pittsburgh, PA, USA.
Fundação Oswaldo Cruz. Instituto Carlos Chagas. Curitiba, PR, Brasil.
Microbiology and Molecular Genetics Department. University of Pittsburgh. Pittsburgh, PA, USA.
Infectious Diseases and Microbiology Department. University of Pittsburgh. Pittsburgh, PA, USA.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Recife, PE, Brasil.
Fundação Oswaldo Cruz. Centro de Pesquisas Aggeu Magalhães. Recife, PE, Brasil.
Microbiology and Molecular Genetics Department. University of Pittsburgh. Pittsburgh, PA, USA.
Abstract
Suggest new approaches focus on engineer antigenic structures capable of exposing a stable
conformation of these epitopes and thus inducing B-cell secretion of HIV-1
pnAbs. We postulated that conformationally
stable structures are better immunogens and can elicit the production
of better antibodies and results show that MD simulations
can help engineer vaccine antigens capable of enhancing protective
antibody responses.
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