Kai Xu

TL;DR: The identification of a neutralizing antibody, N123-VRC34.01, which targets the fusion peptide and blocks viral entry by inhibiting conformational changes in gp120 and gp41 subunits of Env required for entry.

TL;DR: High-resolution structures of the complete EphA2 ectodomain and complexes with ephrin-A1 and A5 as the base unit of an Eph cluster reveal an elongated architecture with novel Eph/Eph interactions, both within and outside of the Eph ligand-binding domain, that suggest the molecular mechanism underlying EPh/ephrin clustering.

TL;DR: It is shown that focusing the immune response to exposed N-terminal residues of the fusion peptide, a critical component of the viral entry machinery and the epitope of antibodies elicited by HIV-1 infection, through immunization with fusion peptIDE-coupled carriers and prefusion stabilized envelope trimers, induces cross-clade neutralizing responses.

TL;DR: Analysis of the structural data reveals the molecular basis for the highly specific interactions of the henipavirus G glycoproteins with only two members of the very large ephrin family and suggests how they mediate in a unique fashion both cell attachment and the initiation of membrane fusion during the virus infection processes.

TL;DR: Targeted deglycosylated trimers are proposed as priming immunogens to increase the frequency of site-targeting antibodies in Env and to measure the impact of the glycan shield on elicitation of antibodies against the CD4 supersite.