Selected article for: "bind affinity and high bind"

Author: Rappuoli, Rino; Bottomley, Matthew J.; D’Oro, Ugo; Finco, Oretta; De Gregorio, Ennio
Title: Reverse vaccinology 2.0: Human immunology instructs vaccine antigen design
  • Document date: 2016_4_4
  • ID: uyoerxvu_28
    Snippet: It was previously shown that a group of HIV crossneutralizing Abs from different donors, collectively called "VRC01 class Abs," targeting the CD4bs of HIV Env derive from the same germline variable heavy chain VH1-2*02 and a few variable light chains characterized by a short (only five amino acids) CDR3. In 2013, Jardine et al. (2013) reported the use of multiple rounds of computational design and structural analysis to engineer an external outer.....
    Document: It was previously shown that a group of HIV crossneutralizing Abs from different donors, collectively called "VRC01 class Abs," targeting the CD4bs of HIV Env derive from the same germline variable heavy chain VH1-2*02 and a few variable light chains characterized by a short (only five amino acids) CDR3. In 2013, Jardine et al. (2013) reported the use of multiple rounds of computational design and structural analysis to engineer an external outer domain (eOD) of the Env protein able to bind the germline precursors of VRC01 Abs with high affinity. The selected protein, eOD-GT6, was fused to a linker from a bacterial lumazine synthase to allow the formation of a 60-mer virus-like protein nanoparticle able to activate B cells expressing either a mature VRC01 B cell receptor or its germline precursor.

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