Cloned immunoglobulin (Ig) genes from HIV-1 infected patients with elite antibody responses yield potent and broad HIV neutralizing antibodies (bnAb) with unusually long and highly mutated CDRH3 domains. Passive infusions with these bnAb give sterilising protection against lentiviral infection in animal transmission models. A vaccinated with HIV Env-gp140 produced antibodies that neutralise d 90% of 27 Env-pseudotyped reporter viruses including Env from clade A, B and C reference panels. The antibodies from this cow inhibited human broadly neutralizing antibody VRC01 binding to CD4bs epitope. So, we used RSC3 core protein and RSC3 Δ373I/P363N to isolate VRC01-like producing memory B cells. The IgG+, WC4 (CD19 like)+, RSC3+, RSC3 Δ373I/P363N- cells were FACS sorted and variable heavy (VH) and light (VL) genes were amplified and cloned into human constant region expression vector. The antibodies were expressed and characterised for envelope binding and neutralisation activity. In total, 52 monoclonal antibodies were isolated belonging to 4 main clonal families. The antibodies in each clonal family had the same VH but different VL genes. The antibodies had VH size of between 121 a.a (CDRH3: 13 a.a) and 134 a.a (CDRH3: 26 a.a). Out of all expressed antibodies, nine monoclonal antibodies were selected for further characterisation. Five antibodies were able to bind RSC3 but not RSC3 Δ373I/P363N but only one of these antibodies (124b) could neutralise AD8 pseudovirus specifically. This antibody also showed heterologous neutralization against tier 1 pseudoviruses (MN and SF162). Further characterization is needed to investigate how this CD4bs antibody neutralise HIV.