Structural and computational analyses of germline antibody/HIV-1 gp120 complexes provide both general principles relevant to the unusual evolution of potent CD4-binding site antibodies and guidelines for structure-based immunogen design.
A new, high-throughput in vivo MHC-I peptide minigene library platform shows that the naive immune system cannot eliminate cells presenting immunogenic antigens found at low frequencies within a growing tumor.
The crystal structure of neutralizing antibody AR3X in complex with HCV E2 glycoprotein reveals unusual features of antibody recognition in which a conserved epitope is recognized by distinct antibody poses.
An attenuated Herpes simplex type 2 virus deleted in glycoprotein D can be used as an effective vaccine to provide robust transferable humoral immunity and complete protection in murine intravaginal and skin infection models.
Computer simulations of the evolution of broadly neutralizing antibodies against HIV suggest that non-traditional pathways involving framework mutations which lead initially to increased antibody flexibility do occur, but can be avoided by appropriate vaccine design.
An integrative structural and biophysical workflow indicates engagement of VRC01 germline antibodies can occur with a gp120 426c core construct containing all wild-type N-linked glycosylation sites, including the Asn276 glycan.