Antibody 2C06 partially accommodates, but antibody 2C09 clashes with, glycan241
MUTANT
We next investigated the parameters governing breadth of recognition by antibodies 2C06 and 2C09. As described in the aforementioned structural analysis, both 2C06 and 2C09 epitopes involved S241, a rare glycan hole in BG505 among HIV isolates; specifically, in both 2C06 and 2C09, heavy-chain residues D61 and R64 were within 4–5 Å from S241 side chain, and PISA analysis indicated both 2C06 and 2C09 to bury 14–22 ÅWe therefore created an S241N mutant of glycan-base BG505 (glycan-base BG505-N241), which introduced To understand the roles of glycan241 in the recognition of Env trimers by antibodies, we compared the known structures of fusion-peptide-directed antibodies in complex with Env trimers. Except for PGT151,