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Here, we use a panel of Env proteins and Ramos B cell lines expressing immunoglobulin M (IgM) B cell receptors (BCRs) with specificity for CD4-binding-site broadly neutralizing antibodies to study the role of antigen binding kinetic rates on both early (proximal/distal signaling) and late events (BCR/antigen internalization) in B cell activation. It is unclear whether affinity discrimination during B cell activation is based solely on Env protein binding K D and whether B cells discriminate among proteins of similar affinities that bind with different kinetic rates. HIV-1 envelope (Env) proteins designed to induce neutralizing antibody responses allow study of the role of affinities (equilibrium dissociation constant ) and kinetic rates (association/dissociation rates) on B cell antigen recognition. All authors reviewed and edited the manuscript. designed and produced eODGT6 and eODGT8 monomers and 60-mer NPs. designed and produced GT1.2 gp140 trimers and GT1.2 NPs. performed statistical analysis for correlation evaluation. phenotyped and sorted for high BCR-expressing Ramos cell lines expressing CH31, VRC01, or VRC01 UCA-IgM BCRs. assisted with the protocols for BCR/antigen downmodulation and internalization. performed and analyzed antigenicity of Env proteins. prepared and purified Fab-trimer complexes. performed and analyzed thermodynamics experiments. phenotyped Ramos cell lines and performed and analyzed cell-surface binding, phospho-signaling, and BCR/antigen downmodulation and internalization experiments. performed and analyzed SPR and Ca-flux experiments. provided collaborative support and revised and edited paper. conceived and designed the study and wrote the paper. You will see a variety of sizes and quality options. 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