Herein, we rationally engineered an IgG–VHH format bsAb based on a human antibody R15‐F7 and a humanized nanobody P14‐F8‐35, both with broad and potent in vitro and in vivo activities.

2022年10月27日 · Bispecific antibodies (bsAbs) represent a unique platform to increase antibody breadth and to reduce neutralization escape. Herein, a novel immunoglobulin G-variable domains of heavy-chain-only antibody (IgG-VHH) format bsAb derived from a potent human antibody R15-F7 and a humanized nanobody P14-F8-35 are rationally engineered.

Here, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains. Consequently, a VHH is …

2020年2月11日 · Here, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains.

To study the impact and mechanism of V H replacement, we generated mice in which antibody production depends on the replacement of a nonproductive V H D H J H rearrangement inserted into its physiological position in the immunoglobulin heavy chain locus.

2024年3月27日 · The VHH molecules are the smallest naturally occurring antibody binding domains derived from heavy-chain only antibodies that can be found naturally in camelids and sharks. The VHH domains are monomeric and thus do …

2020年1月15日 · For several years, we explored ways to substitute antibodies by nanobodies (also known as VHHs), the smallest recognizing part of camelids' heavy-chain antibodies: production of those small proteins in host microorganisms, minute analyses, characterization, and qualification of their affinity towards designed targets.

Here, we report the characterization of a VHH-derived IgG-like bi- and trispecific antibody platform that essentially relies on the replacement of the VH and VL regions of a conventional antibody by two independently functioning VHH domains.

2020年8月11日 · VHH antibodies are the isolated VHH domains of heavy-chain only IgG2 and IgG3 antibodies produced by camelid species, such as alpaca, llama, and camel. These proteins consist of framework regions and three highly variable loops; H1, H2 and H3.

Conventional antibodies prefer binding to the convex portion of the antigen, whereas VHHs prefer epitopes, such as crevices and clefts on the antigen. Therefore, developing candidates with the binding characteristics of camelid VHHs is important.