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1 envelope glycoprotein gp120 are resistant to ibalizumab.
2 al to gp120 V5 may restore susceptibility to ibalizumab.
3 IV-1 variants with reduced susceptibility to ibalizumab.
4 , including 10 strains resistant to parental ibalizumab.
6 3 in domain 2 were found to be important for ibalizumab binding, with E77 and S79 in domain 1 also co
7 cular, clones with reduced susceptibility to ibalizumab contained fewer potential asparagine-linked g
11 ein not only provide an appreciation for why ibalizumab has not had significant adverse immunological
13 hat combine the HIV-1 inhibitory activity of ibalizumab (iMab), a humanized mAb directed to domain 2
16 t by engineering an N-linked glycan into the ibalizumab light chain at a position spatially proximal
17 lls a void between the gp120 V5 loop and the ibalizumab light chain, perhaps causing steric hindrance
25 mouse monoclonal antibody that competes with ibalizumab, was localized entirely within domain 2 on re
26 this void contributes to HIV-1 resistance to ibalizumab, we reasoned that 'refilling' it by engineeri
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