GMP VHH Antibody
Manufacturing Platform

VHHs (Variable Heavy domain of Heavy-chain antibody) are single-domain antibody fragments derived from camelid heavy-chain antibodies; a VHH corresponds to the antigen recognition part of the camelid antibody. They are characterized by their small size (~15 kDa), high stability, and ability to bind challenging or cryptic epitopes that are often inaccessible to conventional antibodies.

A wide range of VHH-based formats can be generated, including monovalent VHHs, multivalent constructs, and engineered formats such as Fc-fused VHHs, depending on the target product profile and development needs.

VHHs offer several advantages, including high affinity and specificity with improved tissue penetration due to their small size, high solubility and stability, and flexibility in engineering complex or multi-specific formats.

Eurogentec’s VHH platform is built on extensive prior development work across multiple varied VHH molecules, enabling the definition of optimized expression and purification conditions.

This platform approach reduces development timelines by leveraging pre-established processes, allowing faster progression to GMP production.

At Eurogentec, VHHs are primarily produced using microbial expression systems such as Escherichia coli and Pichia pastoris (reclassified to K. Phaffii), enabling rapid and cost-effective production.

These systems are well-suited for VHH formats due to their robustness and scalability, and allow efficient production from early development to larger-scale manufacturing.

Yes. VHH production can be scaled from Research Cell Bank to GMP-compliant manufacturing, with processes designed to ensure consistency, robustness, and regulatory compliance for clinical applications from gram to kilogram scales.

A VHH-Fc fusion protein is an engineered molecule combining a VHH domain with the Fc region of an IgG. This format enables both specific target binding and Fc-mediated properties such as extended half-life and effector functions.

VHHs alone are rapidly cleared due to their small size. Fusion to an Fc domain increases molecular size and enables FcRn-mediated recycling, significantly extending circulation time and enhancing therapeutic potential. There are also alternatives to Fc domain strategies if alternatives are required, such as fusing to a VHH binding circulating albumin.

VHH-Fc fusion proteins are explored across multiple therapeutic areas, including oncology (e.g., immune checkpoint targeting), infectious diseases (viral neutralization), and inflammatory or autoimmune disorders.

Yes. Eurogentec supports the development and GMP manufacturing of VHH-based constructs, including Fc-fusion formats, by leveraging its expertise in microbial expression systems.