United Kingdom (UK)
Recombinant monoclonal antibody to HIV-1 GP120. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the human B cell clone PGT124.
UniProt Accession Number of Target Protein: P20871
Alternative Name(s) of Target: gp120; SU; Glycoprotein 120; Env protein; HIV Env; HIV-1 envelope glycoprotein; Envelope glycoprotein gp160; Envelope glycoprotein gp120; Glycoprotein 120;
Immunogen: The original antibody was isolated from culture supernatants of approximately 30,000 activated memory B cells from a clade A infected donor by using a high-throughput strategy for screening IgG against monomeric gp120 (JR-CSF) and gp41(HxB2 -Env) binding as well as neutralization activity against HIV-1(JR-CSF) and HIV-1(SF162).
Specificity: This antibody needs the N332 glycan and the GDIR motif to bind to the HIV-1 envelope glycoprotein (JRCSF strain).
Application Notes: This broadly neutralizing antibody is capable of neutralizing HIV-1 strains 92RW020, 94UG103, 92BR020, JR-CSF, IAVI C22, BG505 and SF162. ELISA was used to determine the EC50 value of the antibody (PMID:28883821). To characterize the exact binding of this antibody, ITC binding experiments were performed using the fab version of this antibody with gp120 monomer. Further PGT124 Fab in complex with BG505 SOSIP.664 gp140 produced in HEK 293S cells were analyzed by negative stain EM. Finally To identify the epitope of the fab version of this antibody, the antibody was co-crystallized in complex with a gp120 core containing a mini-V3 loop. This crystal was subsequently used for crystallography to determine the structure of the complex (Garces et al, 2014; pmid:25259921).
Antibody first published in:
Garces et al. Structural evolution of glycan recognition by a family of potent HIV antibodies. Cell. 2014 Sep 25; 159(1): 69–79. PMID:25259921
Note on publication:
It was examined how a particularly potent family of broadly neutralizing antibodies (Abs) has evolved common and distinct structural features to counter the glycan shield and interact with both glycan and protein components of HIV Env.