Camelid Single Domain Antibodies
Single domain antibody fragments (sdAbs) from camelids retain full antigen-binding capacity. These so-called VHHs or nanobodies offer advantages compared to conventional antibodies. They possess unique properties such as small size, excellent solubility, superior stability, quick clearance from blood and deep tissue penetration. These distinctive qualities make them useful tools in a diverse array of applications such as biosensing, affinity-capture, protein crystallization, molecular imaging, tools for diagnosis and therapeutics.
Wageningen Bioveterinary Research (WBVR) offers single domain antibody services.
- Looking for VHHs for your research? We have an elaborate collection of VHHs for various antigens. The majority of them are directed against veterinary infectious diseases.
- In need of a custom produced VHH/nanobody? We can generate single domain antibodies against antigens supplied by our customers and customize according to their requirement.
VHH phage display library
There are many ways to generate single domain antibodies in vivo and in vitro. The most common is generating an immunized or naive library, and screening by phage/yeast display. The most successfully applied platform technology in the context of antibody discovery is phage display. With the controlled selection and screening strategies, display technologies allow the generation of single domain antibodies against the defined antigens, their conformations or epitopes.
We offer you VHH isolation services against a wide variety of antigens, including native antigens, toxins and self-antigens. We have developed a naive VHH phage display library from 2 camels and 21 llamas with a size of 3 × 109, along with our immunized libraries to cater your requirements. Usually, we conduct two to four rounds of panning followed by screening of individual clones by ELISA to obtain high affinity binders.
1. Immune phage display library
We will immunize llamas against the antigen provided by customers and will deliver the phage display library generated from the immunized llamas in 9-11 weeks.
Flow chart: Immune phage display library
2. Immune phage display library, along with screening
We will immunize the llamas against the antigen provided by customers. Our deliverables will be unique clone sequences after screening the phage display library generated from the immunized llamas in 15-17 weeks, or the purified VHHs from the selected clones in 20-22 weeks.
Flow chart: Immune phage display library and deep sequencing
3. Naive library screening
See our research showcase about our naive VHH library project:
We have generated a naive VHH phage display library from 21 llamas and 2 camels. Our deliverables will be unique clone sequences selected from the naive llama or camel libraries in 5-6 weeks, or the purified VHHs from the selected clones in 4-8 weeks.
Flow chart: Naive library screening
4. Customized project
We can customize your project depending on your requirements or the desired output, starting from generating an immune phage display library, to affinity measurement of the identified binders.
5. Affinity measurement
6. Deep sequencing
With the aid of our in-house MiSeq next-generation sequencing (NGS) techniques, we offer customers a high throughput analysis of the antibody repertoire of the libraries in terms of diversity and quality. This facilitates the process of phage display selections, clonal enrichment and identification of rare antibody sequences.
We offer many single domain antibodies from llamas, developed at our institute over the last three decades. These VHHs from llamas are produced in baker’s yeast and sold at 100 microgram to several mg quantities in unlabelled and biotinylated form. Especially a unique panel of foot-and-mouth disease virus (FMDV) and influenza A virus (IAV) binding VHHs are available. These are excellent reagents for quality control of vaccines. See our list of references below for more information on available VHHs.
View our key references
Small-Scale Secretory VHH Expression in Saccharomyces cerevisiaeIn: Single-Domain Antibodies / , Hussack, Greg, Henry, Kevin A.. - : Springer (Methods in molecular biology (Clifton, N.J.) ) - ISBN 9781071620755 - p. 159 - 179.
Structural and molecular basis for foot-and-mouth disease virus neutralization by two potent protective antibodiesProtein & Cell 13 (2022)6. - ISSN 1674-8018 - p. 446 - 453.
A novel single-domain antibody multimer that potently neutralizes tetanus neurotoxinVaccine: X 8 (2021). - ISSN 2590-1362
Novel capsid-specific single-domain antibodies with broad foot-and-mouth disease strain recognition reveal differences in antigenicity of virions, empty capsids, and virus-like particlesVaccines 9 (2021)6. - ISSN 2076-393X
Multimeric single-domain antibody complexes protect against bunyavirus infectionseLife 9 (2020). - ISSN 2050-084X
Isolation of single-domain antibody fragments that preferentially detect intact (146s) particles of foot-and-mouth disease virus for use in vaccine quality controlFrontiers in Immunology 8 (2017). - ISSN 1664-3224 - 12 p.
Effect of thiomersal on dissociation of intact (146S) foot-and-mouth disease virions into 12S particles as assessed by novel ELISAs specific for either 146S or 12S particlesVaccine 29 (2011)15. - ISSN 0264-410X - p. 2682 - 2690.
Properties, production and applications of camelid single-domain antibody fragmentsApplied Microbiology and Biotechnology 77 (2007)1. - ISSN 0175-7598 - p. 13 - 22.
Selection and optimization of proteolytically stable llama single-domain antibody fragments for oral immunotherapyApplied Microbiology and Biotechnology 72 (2006)3. - ISSN 0175-7598 - p. 544 - 551.