HUGO-Nano™: Nanobodies with a human framework, discovered in mice
LIVE WEBINAR
HUGO-Nano™: Nanobodies with a human framework, discovered in mice
Nanobodies are increasingly used as building blocks for multispecific antibodies, T-cell engagers, ADCs, CAR-T cells and radioligand therapies. But every existing discovery route forces a trade-off: binders are either human in sequence or behave like natural camelid VHHs (soluble, stable, single-domain), rarely both.
DATE
November 19, 2026 | 16:00 CEST - 10:00 ET
LOCATION
Online｜hosted by Pharma D-mand
Introduction
VHHs (single-domain antibodies, also called nanobodies) are about 15 kDa, roughly a tenth the size of a conventional IgG (~150 kDa). They fold on their own without a light chain and can bind hidden or recessed epitopes that full-size antibodies cannot reach. The nanobody therapeutics market is projected to grow from $439M in 2026 to $1.83B by 2034 (19.5% CAGR), driven largely by multivalent and multispecific formats entering large chronic-disease indications. However, each current discovery route has a drawback. Camelid-derived VHHs come from slow large-animal immunizations and must be humanized afterwards, which can reduce affinity. Human VH domains from transgenic rodents tend to aggregate and are less soluble. Camelid VHHs raised in transgenic mice usually still need humanization.
This session introduces HUGO-Nano™, the newest member of Cyagen's HUGO-Ab™ fully human antibody discovery family. HUGO-Nano™ mice carry a human heavy-chain locus with two changes. First, the CH1 domain is deleted, so heavy chains are expressed without a light chain. Second, a few framework 2 (FR2) residues are replaced with the hallmark residues found in camelid VHHs, which keep the single domain soluble. The mice therefore produce VHH-like antibodies with a human framework and the solubility, stability and single-domain behavior of natural nanobodies. Because the binders are already human in sequence, no humanization step is needed, and discovery follows a standard mouse immunization workflow.
Summary
This webinar covers the limitations of existing VHH discovery routes and how a human-framework nanobody platform addresses them. We will explain how the HUGO-Nano™ locus was designed, walk through the four-step discovery workflow from immunization to leads ready for engineering, and present validation data on repertoire diversity, immune cell profiling and binder characterization.
Topics include
- Platform design and workflow: How deleting CH1 and adding camelid FR2 hallmark residues creates a VHH locus with a human framework, and how leads are recovered by hybridoma, single B-cell sorting or phage display.
- How HUGO-Nano™ compares: A side-by-side comparison of camelid-derived VHHs, human VH rodent platforms, camelid-VHH mouse platforms and HUGO-Nano™ on need for humanization, immunogenicity, developability, epitope access, time to lead and IP position.
- Validation data: V(D)J sequencing showing broad germline gene usage and diverse CDR3 lengths; flow cytometry showing immune cell populations comparable to wild-type mice; serum titers against difficult targets; and ELISA and FACS binding data for panels of nanobody candidates.
- Developability and formats: Thermal stability (melting temperature >60°C by DSF; stable for 14 days at 40°C), and examples of VHHs used in bispecifics, T-cell engagers, ADCs, CAR-T, radioligand and molecular imaging agents, and blood–brain barrier (BBB)-crossing constructs.
- Access and IP: Options to access the mouse model, access the HUGO-LAb™ antibody library, or commission custom discovery and development, supported by a freedom-to-operate (FTO) assessment covering China, the United States, Japan and Europe.
Who Should Attend
- Antibody discovery scientists and platform leads evaluating single-domain antibody sources for new programs.
- Protein engineers designing bispecifics, multispecifics, T-cell engagers or ADCs that need small binding domains.
- Cell and gene therapy researchers designing CAR-T targeting domains and other engineered cell therapies.
- Radiopharmaceutical and molecular imaging teams who need binders with fast tissue penetration and rapid clearance.
- Neuroscience and CNS drug developers working on receptor-mediated delivery across the blood–brain barrier.
- Biotech and pharma program leaders assessing platform access, licensing and freedom-to-operate for nanobody pipelines.
Key Learning Objectives
- Compare the strengths and limitations of camelid-derived VHHs, human VH rodent platforms and camelid-VHH mouse platforms, and where each one falls short.
- Understand how a human VHH locus with camelid FR2 residues gives the low immunogenicity of a human sequence while keeping camelid-like solubility, stability and single-domain folding.
- Learn how the HUGO-Nano™ discovery workflow uses standard mouse immunization and in vivo affinity maturation to produce leads ready for engineering, with no humanization step.
- Review validation data on repertoire diversity, immune cell profiling, serum titers against difficult targets, and binding of nanobody candidates to purified protein and to cells.
- See how HUGO-Nano™ binders can be built into bispecifics, T-cell engagers, ADCs, CAR-T, radioligand conjugates and BBB-crossing constructs.
- Identify which engagement model — model access, library access or custom discovery — best fits your pipeline and IP strategy.
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