Since 2007, Capralogics has proven to have strong expertise in antibody and nanobody development services for for llamas and alpacas. As members of the camelid family, llamas and alpacas produce both conventional antibodies with two heavy chains and two light chains and unique heavy-chain-only antibodies with a small ~15 KDa antigen-binding domain termed VHH. Antigen specific camelid RNA is purified and used to generate VHH libraries. Selected VHH are engineered to many types of functional VHH antibodies. The single chain VHH antibody form is often referred to as a nanobody. Other VHH antibodies engineered include bivalent forms capable of binding to two different epitopes simultaneously. Scaffold antibodies may be generated by fusing the VHH fragment to an immunoglobulin from another species such as a human. The outcome could be a humanized nanobody with value for therapeutics and diagnostics.
The VHH domain antibody has many valuable applications and advantages over a traditional IgG antibody including the following:
- VHH antibodies are small and they have the ability to recognize antigenic sites that are normally inaccessible to conventional antibodies such as enzyme-active sites.
- Rapid tissue penetration with the ability to cross the blood-brain barrier.
- High tolerance to extremes in pH and temperature, meaning retention of native structure and biologically active conformation making them ideal for biosensor applications.
- An alternative to monoclonal antibody production.
Some Llama and Alpaca Capralogics Custom Services Citations
Alpaca: Adhikari, Emily H., et al. “Diverging maternal and cord antibody functions from SARS-CoV-2 infection and vaccination in pregnancy.” The Journal of Infectious Diseases 229.2 (2024): 462-472. Article
Llama: Xu, Jianliang, et al. “Ultrapotent Broadly Neutralizing Human‐llama Bispecific Antibodies against HIV‐1.” Advanced Science: 2309268(2024). Article
Llama: Akpokiro, Prince, et al. “Characterization of Cavβ Nanobodies using Dimerization-Dependent Fluorescent Proteins.” Available at SSRN 4736689 (2024). Article
Llama: Mikkelsen, Jakob Hauge, et al. “Trypanosoma brucei Invariant Surface Glycoprotein 75 Is an Immunoglobulin Fc Receptor Inhibiting Complement Activation and Antibody-Mediated Cellular Phagocytosis.” The Journal of Immunology (2024). Abstract
Alpaca: Chen, Jin Y., et al. “A nanobody-based complement inhibitor targeting complement component 2 reduces hemolysis in a complement humanized mouse model of autoimmune hemolytic anemia.” Clinical Immunology 253 (2023): 109678. Abstract
Llama: Spillner, Edzard, et al. Single Domain Antibodies against Bee Venom Epitopes. WO2023170282A1, 14 Sept. 2023
Llama: Hollingsworth, Scott A., et al. “Discovery and multimerization of cross-reactive single-domain antibodies against SARS-like viruses to enhance potency and address emerging SARS-CoV-2 variants.” Scientific Reports 13.1 (2023): 13668. Article
Alpaca: Weinstein, Jules B., et al. “A potent alpaca-derived nanobody that neutralizes SARS-CoV-2 variants.” Iscience 25.3 (2022): 103960. Article
Alpaca: Bates, Timothy A., et al. “Vaccination before or after SARS-CoV-2 infection leads to robust humoral response and antibodies that effectively neutralize variants.” Science immunology 7.68 (2022): eabn8014. Article
Llama: Balthasar, Joseph P., et al. Compositions and Methods for Reducing Off-Target Toxicity of Antibody Drug Conjugates. WO2021113740A1, 10 June 2021
Llama: Mast, Fred D., et al. “Highly synergistic combinations of nanobodies that target SARS-CoV-2 and are resistant to escape.” Elife 10 (2021): e73027. Article
Llama: Xu, Jianliang, et al. “Nanobodies from camelid mice and llamas neutralize SARS-CoV-2 variants.” Nature 595.7866 (2021): 278-282. Article
Llama: Longhin, Elena, et al. “Isolation and characterization of nanobodies against a zinc-transporting p-type atpase.” Antibodies 7.4 (2018): 39. Article
Alpaca, Llama: Thompson, Mary K., et al. “Optimizing selection of large animals for antibody production by screening immune response to standard vaccines.” Journal of immunological methods 430 (2016): 56-60. Article
Llama: Nguyen, Van Son, et al. “Inhibition of type VI secretion by an anti-TssM llama nanobody.” PLoS One 10.3 (2015): e0122187. Article
Llama: Fridy, Peter C., et al. “A robust pipeline for rapid production of versatile nanobody repertoires.” Nature methods 11.12 (2014): 1253-1260. Article
Llama: Desmyter, Aline, et al. “Viral infection modulation and neutralization by camelid nanobodies.” Proceedings of the National Academy of Sciences 110.15 (2013): E1371-E1379. Article
We also offer custom antibody services in other host species: goat, rabbit, and sheep.
Place an order for llama and alpaca services using our custom antibody development order form Upon request, Capralogics can provide naive PBMCs and/or RNA from our non-immunized llamas and alpacas.
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