Antibody Epitope region Epitope type Structure known? Hurdles to overcome Key references
2F5, 4E10 gp41MPER Continuous, conformational and composite (protein-lipid) Yes, but only in context of antibody-peptide complex Instructing B cells to recognize peptide-lipid antigens. Overcoming immune tolerance mechanisms without inducing autoimmune pathology [70,71,73,74,82]
b12 VRC01   gp120CD4bs Discontinuous protein Yes, in context of core gp120 and also at lower resolution with cryo-EM in context of trimer Focusing B cell responses towards ‘site of vulnerability’, overcoming low immunogenicity, instructing antibody ‘angle of approach’ to trimer [37,38,86,87,88,93,112, 114,127]
PG9, PG16 gp120 quaternary V1/V2 Continuous, conformational, composite (protein-glycan) Yes in context of constrained mimetic Instructing B cells to recognize glycopeptide epitopes [95]
PGT 128 Gp120 glycopeptideV3 Continuous, conformational, composite (protein-glycan) Yes in context of outer domain construct of gp120 Instructing B cells to recognize glycopeptide epitopes [97]
2G12 gp120 glycan Discontinuous glycan Yes in context of synthetic glycans Instructing B cells to recognize glycans. Presenting glycan arrays that appear foreign to host and may not require breaking of immune self tolerance [101]
Table 1: A summary of bNMAb families with their epitope type, structure and major hurdles to overcome to develop an antigen capable of eliciting bNMAb.
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