The DOI matches its Crossref record; 96 of the 96 references it cites were found in a registry or an index.
Properties, production, and applications of camelid single-domain antibody fragments
Open accessAbstract
Camelids produce functional antibodies devoid of light chains of which the single N-terminal domain is fully capable of antigen binding. These single-domain antibody fragments (VHHs or Nanobodies®) have several advantages for biotechnological applications. They are well expressed in microorganisms and have a high stability and solubility. Furthermore, they are well suited for construction of larger molecules and selection systems such as phage, yeast, or ribosome display. This minireview offers an overview of (1) their properties as compared to conventional antibodies, (2) their production in microorganisms, with a focus on yeasts, and (3) their therapeutic applications.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Given their high-affinity, solubility and stability also in absence of the partner VL domain, the camelid VH domains (VHH) [4] and the shark VH domains called V-NAR (New Antigen Receptor) [5], are currently used as templates to generate highly efficient and stable new antibody fragments collectively termed nanobodies [6,7,8].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [4]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Naturally occurring antibodies devoid of light chains
Hamers-Casterman, C., Atarhouch, T., Muyldermans, S., Robinson, G., Hammers, C., Songa, E. B., Bendahman, N., & Hammers, R. (1993) · Nature · doi:10.1038/363446a0 · Cited by 3,241 · cited 4×
“Sequence analysis (Hamers-Casterman et al. 1993; Muyldermans et al. 1994; Vu et al. 1997; Harmsen et al. 2000) and elucidation of the crystal structure (Desmyter et al.”
BackgroundInfluentialRapid generation of functional human IgG antibodies derived from Fab-on-phage display libraries
Jostock, T., Vanhove, M., Brepoels, E., van Gool, R., Daukandt, M., Wehnert, A., van Hegelsom, R., Dransfield, D., Sexton, D., Devlin, M., et al. (2004) · Journal of Immunological Methods · doi:10.1016/j.jim.2004.03.014 · Cited by 2,572
Engineered antibody fragments and the rise of single domains
Holliger, P., & Hudson, P. J. (2005) · Nature Biotechnology · doi:10.1038/nbt1142 · Cited by 1,928 · cited 1×
“As compared to human VH domains, the VHH FRs show a high sequence homology of more than 80%, and their 3D structures can be superimposed (Muyldermans et al. 2001; Holliger and Hudson 2005).”
BackgroundWard, E. S., Güssow, D., Griffiths, A. D., Jones, P., & Winter, G. P. (1989) · Nature · doi:10.1038/341544a0 · Cited by 1,010 · cited 2×
“Although isolated antibody heavy (Utsumi and Karush 1964) and light chains (Yoo et al. 1967) can retain antigenbinding specificity, their affinity and solubility is often reduced (Ward et al. 1989).”
BackgroundGreenberg, A. S., Avila, D. W., Hughes, M. K., Hughes, A. L., McKinney, E. C., & Flajnik, M. F. (1995) · Nature · doi:10.1038/374168a0 · Cited by 783 · cited 2×
“Although single-domain antibodies later were also identified in particular cartilaginous fish (Greenberg et al. 1995), most research on the biotechnological application of singledomain antibodies was done using camelids because of Appl Microbiol Biotechnol (2007) 77:13–22”
BackgroundSelection and identification of single domain antibody fragments from camel heavy‐chain antibodies
Ghahroudi, M. A., Desmyter, A., Wyns, L., HAMERS, R., & Muyldermans, S. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01062-4 · Cited by 775 · cited 1×
“Methods to isolate antigen-specific VHHs from immune ( Arbabi-Ghahroudi et al. 1997; Van der Linden et al. 2000a), nonimmune (Tanha et al. 2002; Yau et al. 2003; Verheesen et al. 2006), or semisynthetic (Goldman et al. 2006) libraries using phage, yeast, or ribosome display are now well established.”
BackgroundTargeting and tracing antigens in live cells with fluorescent nanobodies
Rothbauer, U., Zolghadr, K., Tillib, S. V., Nowak, D., Schermelleh, L., Gahl, A., Backmann, N., Conrath, K., Muyldermans, S., Cardoso, M. C., et al. (2006) · Nature Methods · doi:10.1038/nmeth953 · Cited by 715 · cited 1×
“Because of their stability, VHHs are especially suited for intrabody production because this requires expression in the reducing environment of the cytoplasm (Gueorguieva et al. 2006; Rothbauer et al. 2006).”
BackgroundMolecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies
Genst, E. D., Silence, K., Decanniere, K., Conrath, K., Loris, R., Kinne, J., Muyldermans, S., & Wyns, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505379103 · Cited by 681 · cited 4×
“Occasionally, VHHs with affinity constants (KD) as low as 100 pM are isolated (Saerens et al. 2004; De Genst et al. 2006; Harmsen et al. 2006), which equals the affinity ceiling proposed for natural antibodies (Sundberg and Mariuzza 2002).”
BackgroundInfluentialSingle‐domain antibody fragments with high conformational stability
Dumoulin, M., Conrath, K., Meirhaeghe, A. V., Meersman, F., Heremans, K., Frenken, L. G. J., Muyldermans, S., Wyns, L., & Matagne, A. (2002) · Protein Science · doi:10.1110/ps.34602 · Cited by 641 · cited 4×
“VHHs are especially suited for oral immunotherapy because of their resistance against extremes of pH and the capacity to bind to the target at high concentrations of chaotropic agents (Dumoulin et al. 2002, 2003).”
BackgroundInfluentialStructure-Immunogenicity Relationships of Therapeutic Proteins
Hermeling, S., Crommelin, D. J. A., Schellekens, H., & Jiskoot, W. (2004) · Pharmaceutical Research · doi:10.1023/b:pham.0000029275.41323.a6 · Cited by 617 · cited 1×
“This could rely on their high sequence homology to conventional VH domains and on their high stability because aggregation of proteins is known to increase immunogenicity (Hermeling et al. 2004).”
Background
Flagged first, then by citations
Research works printed but not linked: 1
- Estell D (2006) Adapting industry practices for the rapid, large-scale manufacture of pharmaceutical proteins. Bridge 36:39–44
Cited by
Sorted by citations
Items 501–600 of 809
Methods for Conjugating Antibodies with Quantum Dots
Sokolov, P. M., Кныш, А. А., Kriukova, I. S., Samokhvalov, P. S., & Kistenev, Y. V. (2025) · Molecules · doi:10.3390/molecules30193999 · Cited by 9
“…bispecific Abs [35], trispecific Abs [36], etc., as well as single-domain Abs (sdAbs) representing the variable domain of the heavy chain of camelid Ig (VHH) [37], or fragments of the variable domain of shark Ig (shark Ig new antigen receptor (IgNAR) Abs) are obtained using this approach [38].”
Development of anti-human IgM nanobodies as universal reagents for general immunodiagnostics
Scarrone, M., González‐Techera, A., Alvez-Rosado, R., Delfin-Riela, T., Modernell, Á., González‐Sapienza, G., & Lassabe, G. (2021) · New Biotechnology · doi:10.1016/j.nbt.2021.05.002 · Cited by 9
Targeting ErbB3 Receptor in Cancer with Inhibitory Antibodies from Llama
Eliseev, I. E., Ukrainskaya, V. M., Yudenko, A., Mikushina, A. D., Shmakov, S. V., Afremova, A. I., Ekimova, V. M., Vronskaia, A. A., Knyazev, N. A., & Валерьевна, Ш. О. (2021) · Biomedicines · doi:10.3390/biomedicines9091106 · Cited by 9
“These single-domain antibody fragments possess many advantages, including high solubility, stability, and facile biotechnological production [18].”
BackgroundKim, W. S., Chae, H. D., Jung, I., Lee, W., Lee, W. J., Lee, J., Gong, Y., Lee, D., Kim, B.-W., Kim, J.-K., et al. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.108807 · Cited by 9
Emerging immunologic approaches as cancer anti-angiogenic therapies
Azimi, M., Manavi, M. S., Afshinpour, M., Khorram, R., Vafadar, R., Rezaei‐Tazangi, F., Arabzadeh, D., Arabzadeh, S., Ebrahimi, N., & Aref, A. R. (2024) · Clinical & Translational Oncology · doi:10.1007/s12094-024-03667-2 · Cited by 10
“Finally, owing to their higher hydrophilicity in comparison to conventional mABs, their tendency for aggregation with nanobodies is much less in aqueous solutions [62].”
Genetic methods of antibody generation and their use in immunohistochemistry
Schofield, D. J., Lewis, A. R., & Austin, M. J. (2014) · Methods · doi:10.1016/j.ymeth.2014.02.031 · Cited by 9
Soluble Recombinant Protein Production in Pseudoalteromonas haloplanktis TAC125
Giuliani, M., Parrilli, E., Sannino, F., Apuzzo, G. A., Marino, G., & Tutino, M. L. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2205-5_13 · Cited by 9
Development of specific nanobodies (VHH) for CD19 immuno-targeting of human B-lymphocytes.
Banihashemi, S. R., Hosseini, A. Z., Rahbarizadeh, F., & Ahmadvand, D. (2018) · Europe PMC (PubMed Central) · doi:10.22038/ijbms.2018.26778.6557 · Cited by 9
“As a result, they may be considered as famous heavy chain antibodies (hcAbs) (14,15).”
BackgroundTunghirun, C., Narkthong, V., Chaicumpa, W., & Chimnaronk, S. (2020) · Antiviral Research · doi:10.1016/j.antiviral.2020.104921 · Cited by 9
Marine-derived microbes and molecules for drug discovery
Tanaka, Y., Nishikawa, M., Kamisaki, K., Hachiya, S., Nakamura, M., Kuwazuru, T., Tanimura, S., Soyano, K., & Takeda, K. (2022) · Inflammation and Regeneration · doi:10.1186/s41232-022-00207-9 · Cited by 9
Structure of a low-melting-temperature anti-cholera toxin: llama V H H domain
Legler, P. M., Zabetakis, D., Anderson, G. P., Lam, A. Y., Hol, W. G. J., & Goldman, E. R. (2013) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309112050750 · Cited by 10
Maffey, L., Vega, C. G., Parreño, V. G., & Garaicoechea, L. (2015) · Revista Argentina de Microbiología · doi:10.1016/j.ram.2015.09.005 · Cited by 9
Takahashi, K., Sunohara, M., Terai, T., Kumachi, S., & Nemoto, N. (2017) · Biophysics and Physicobiology · doi:10.2142/biophysico.14.0_23 · Cited by 9
Liddell, E. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097037-0.00017-8 · Cited by 10
Protein Biomarkers in Lung Cancer Screening: Technical Considerations and Feasibility Assessment
Orive, D., Echepare, M., Bernasconi-Bisio, F., Sanmamed, M. F., Pineda‐Lucena, A., de la Calle-Arroyo, C., Detterbeck, F., Hung, R. J., Johansson, M., Robbins, H. A., et al. (2024) · Archivos de Bronconeumología · doi:10.1016/j.arbres.2024.07.007 · Cited by 8
David, M., Cohen, R., Beuzelin, D., Ferracci, G., Cresci, M., Faucon, A., Abouzid, K., Godefroy, G., Masse, M., Mechioukhi, Y., et al. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.114344 · Cited by 9
Santoro, A., Grimaldi, M., Marino, C., Napolitano, E., Buonocore, M., & D’Ursi, A. M. (2025) · Life · doi:10.3390/life16010010 · Cited by 8
“Due to their size, simple structure, high antigen-binding affinity, and remarkable stability under extreme conditions, nanobodies have the potential to overcome many of the limitations of monoclonal antibodies [215].”
Nanobodies: A Promising Toolkit for Diagnostic Applications
Wu, W., Ali, A., Sun, L., Hu, J., Hameed, L., Shafi, S., Raza, A., Dinislam, K., Xing, W., Rong, L., et al. (2026) · SmartMat · doi:10.1002/smm2.70088 · Cited by 8
Cytoplasmic and periplasmic expression of recombinant shark VNAR antibody in Escherichia coli
Leow, H. C., Fischer, K., Leow, C. Y., Braet, K., Cheng, Q., & McCarthy, J. S. (2019) · Preparative Biochemistry & Biotechnology · doi:10.1080/10826068.2019.1566145 · Cited by 8
“region of camelids HCAbs is known as VHH (variable domain of the heavy chain of HCAbs) or NanobodyVR (Nb; Ablynx).([4]) In contrast to camelids, immunoglobulin new antigen receptor (IgNAR) is an intra-domain disulfide bond”
BackgroundParakasikron, N., Chaotham, C., Pithi Chanvorachote, B., Vinayanuwattikun, C., Buranasudja, V., Taweecheep, P., & Khantasup, K. (2021) · Drug Delivery · doi:10.1080/10717544.2021.1943055 · Cited by 8
Gevenois, P. J.-L. Y., Pauw, P. E. M. D., Schoonooghe, S., Delporte, C., Sebti, T., Amighi, K., Muyldermans, S., & Wauthoz, N. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2100250 · Cited by 8
Khodabakhsh, F., Shokri, S., Jalili, N., Moradi‐Kalbolandi, S., Dashtestani, F., & Farahmand, L. (2022) · Chemical Papers · doi:10.1007/s11696-022-02625-y · Cited by 8
“…the prokaryotic systems, high stability in various physicochemical conditions, rapid penetration into solid tissues, and detection of hidden antigenic sites because of their small size, and lower immunogenicity in humans due to the association between human VH with VHHs (Harmsen and De Haard 2007).”
BackgroundInfluentialNew Virus Diagnostic Approaches to Ensuring the Ongoing Plant Biosecurity of Aotearoa New Zealand
Delmiglio, C., Waite, D. W., Lilly, S. T., Yan, J., Elliott, C. E., Pattemore, J., Guy, P. L., & Thompson, J. R. (2023) · Viruses · doi:10.3390/v15020418 · Cited by 8
Shen, C., Jin, J., Huang, Z., Meng, M., Lin, M., Hu, X., Zhu, Q., Xu, C., Chen, W., Lin, J., et al. (2024) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c07295 · Cited by 8
Selection by phage display of nanobodies directed against hypoxia inducible factor‐1α (HIF‐1α)
Li, M., Fan, X., Liu, J., Hu, Y., & Huang, H. (2014) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1340 · Cited by 8
Systems approaches to design of targeted therapeutic delivery
Myerson, J. W., Brenner, J. S., Greineder, C. F., & Muzykantov, V. R. (2015) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1304 · Cited by 8
Han, L., Peng, R., Jiang, W., Xu, T., Zhang, C., Chen, K., Zhang, Y., Song, H., & Jia, L. (2020) · Journal of Materials Chemistry B · doi:10.1039/d0tb00574f · Cited by 8
Construction of a Nanobodies Phage Display Library From an Escherichia coli Immunized Dromedary.
Salhi, I., Bessalah, S., Snoun, D., Khorchani, T., & Hammadi, M. (2020) · PubMed Central · doi:10.30498/ijb.2020.127753.2247 · Cited by 8
“They are highly soluble, physicochemically stable and can be produced with high yields in bacteria, fungi or plants (7, 8).”
BackgroundGeneration and Characterization of Nanobodies Against Tomato Leaf Curl Sudan Virus
Zakri, A. M., Al-Doss, A., Ali, A. A. M., Samara, E. M., Ahmed, B. S., Al-Saleh, M. A., Idris, A. M., Abdalla, O. A., & Sack, M. (2021) · Plant Disease · doi:10.1094/pdis-11-20-2407-re · Cited by 8
Targeting Human Papillomavirus-Associated Cancer by Oncoprotein-Specific Recombinant Antibodies
Donà, M. G., Bonito, P. D., Chiantore, M. V., Amici, C., & Accardi, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179143 · Cited by 8
Sroga, P., Sloan, A. M., Warner, B. M., Tierney, K. J., Lew, J. M., Liu, G., Chan, M., Deschambault, Y., Stein, D. R., Soule, G., et al. (2021) · Scientific Reports · doi:10.1038/s41598-021-96884-6 · Cited by 8
Temnopleurus reevesii as a new sea urchin model in genetics
Yaguchi, S., & Yaguchi, J. (2021) · Development Growth & Differentiation · doi:10.1111/dgd.12768 · Cited by 8
“Nanobodies might resolve this issue (Harmsen & De Haard, 2007) due to their smaller structure, but their use is still inconvenient in nonmodel organisms such as sea urchins.”
BackgroundhGRAD: A versatile “one-fits-all” system to acutely deplete RNA binding proteins from condensates
Arnold, B., Riegger, R. J., Okuda, E. K., Slišković, I., Keller, M., Bakisoglu, C., McNicoll, F., Zarnack, K., & Müller-McNicoll, M. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202304030 · Cited by 7
Eshak, F., Pion, L., Scholler, P., Névoltris, D., Chames, P., Rondard, P., Pin, J., Acher, F., & Goupil-Lamy, A. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.3c01620 · Cited by 9
Menzel, S., Rissiek, B., Haag, F., Goldbaum, F. A., & Koch‐Nolte, F. (2013) · FEBS Journal · doi:10.1111/febs.12313 · Cited by 8
New approaches in oral rotavirus vaccines
Defo, Z. K., & Lee, B. H. (2014) · Critical Reviews in Microbiology · doi:10.3109/1040841x.2014.962479 · Cited by 8
Integrated purification of a nanobody using ammonium sulfate precipitation and Capto MMC
Fan, X., Liang, Y., Li, F., Yu, J., Song, H., Feng, D., Xian, M., Liu, W., & Nian, R. (2019) · Journal of Chemical Technology & Biotechnology · doi:10.1002/jctb.6228 · Cited by 8
Immunoliposomes: Synthesis, Structure, and their Potential as Drug Delivery Carriers
Sandeep, D., AlSawaftah, N., & Husseini, G. A. (2020) · Current Cancer Therapy Reviews · doi:10.2174/1573394716666200227095521 · Cited by 8
DOWNSTREAM PROCESSING OF Fc FUSION PROTEINS, BISPECIFIC ANTIBODIES, AND ANTIBODY–DRUG CONJUGATES
Shukla, A. A., & Norman, C. (2017) · doi:10.1002/9781119126942.ch26 · Cited by 8
Nanobody CAR-T cells in cancer: From molecular design to clinical translation
Eisa, A. R., Razavi, F. T., Hoseinzadeh, A., Haghmorad, D., & Baharlou, R. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118819 · Cited by 7
Camel nanobodies: Promising molecular tools against leishmaniasis
Alshamat, E. A., Kweider, M., & Abbady, A. Q. (2020) · Parasite Immunology · doi:10.1111/pim.12718 · Cited by 7
Plant-derived single domain COVID-19 antibodies
Shen, A. M., Malekshah, O. M., Pogrebnyak, N., & Minko, T. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.05.030 · Cited by 7
“The VHH can bind to antigens without requiring domain pairing and can also recognize antigenic sites that are normally not recognized by conventional antibodies [20].”
BackgroundModular design of bi- and multi-specific knob domain fusions
Kuravsky, M. L., Gibbons, G. F., Joyce, C., Scott-Tucker, A., Macpherson, A., & Lawson, A. D. G. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1384467 · Cited by 7
A single-domain antibody library based on a stability-engineered human VH3 scaffold
Lee, N. J., Jung, M., Yang, H. Y., & Shim, H. (2024) · Scientific Reports · doi:10.1038/s41598-024-68680-5 · Cited by 10
“…variety of prokaryotic and eukaryotic host cells, high solubility, and modularity due to their small molecular size and good stability, which enables sdAbs to incorporate into bispecific antibodies, chimeric antigen receptors, and other molecular constructs that require target binding moieties 15 .”
BackgroundProtein Production in Yarrowia lipolytica Via Fusion to the Secreted Lipase Lip2p
Hofmeyer, T., Bulani, S. I., Grzeschik, J., Krah, S., Glotzbach, B., Uth, C., Avrutina, O., Brecht, M., Göringer, H. U., van Zyl, P. J., et al. (2013) · Molecular Biotechnology · doi:10.1007/s12033-013-9684-2 · Cited by 7
“Camelid heavy chain antibodies with their antigen binding site located in a single variable domain, referred to as VHH, exhibit a broad antigen-binding activity [44, 45] Mol Biotechnol”
BackgroundKabir, M. E., Krishnaswamy, S., Miyamoto, M., Furuichi, Y., & Komiyama, T. (2010) · Protein Expression and Purification · doi:10.1016/j.pep.2010.01.002 · Cited by 7
Cytotoxic potential of camel whey and milk on cervix cancer (HeLa) cell line
Abdallah, L., Sawafta, A. M., Ali, S. A. B., & Baradia, H. A. (2019) · Asian Journal of Medical and Biological Research · doi:10.3329/ajmbr.v5i3.43593 · Cited by 7
Perspective: Reducing SARS-CoV2 Infectivity and Its Associated Immunopathology
Dubey, A., Dahiya, S., Rouse, B. T., & Sehrawat, S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.581076 · Cited by 6
Barroeta, A. B., Marquart, J. A., Bakhtiari, K., Meijer, A. B., Urbanus, R. T., & Meijers, J. C. M. (2022) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.15815 · Cited by 7
Qiu, J., Li, J., Zhang, Z., Dong, S., Ling, X., Fang, Z., Ling, Q., & Huang, Z. (2023) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2023.1207048 · Cited by 7
Small biomolecular scaffolds for improved biosensor performance
Skottrup, P. D. (2010) · Analytical Biochemistry · doi:10.1016/j.ab.2010.06.042 · Cited by 7
Chen, J., Zhao, Y., & Feng, W. (2020) · Protein Expression and Purification · doi:10.1016/j.pep.2020.105627 · Cited by 7
Designing and Development of a Tandem Bivalent Nanobody against VEGF165
Khodabakhsh, F., Salimian, M., Ziaee, P., Kazemi‐Lomedasht, F., Behdani, M., & Cohan, R. A. (2021) · Avicenna Journal of Medical Biotechnology · doi:10.18502/ajmb.v13i2.5519 · Cited by 7
“Since Vascular Endothelial Growth Factor 165 (VEG F 165 ) isoform is a key factor in tumor angiogenesis and metastasis 18 , therefore, in the current study, a recombinant tandem bivalent single-domain antibody against VEGF 165 was designed, expressed, and purified.”
BackgroundSelection and Modelling of a New Single-Domain Intrabody Against TDP-43
Gilodi, M., Lisi, S., Dudás, E. F., Fantini, M., Puglisi, R., Louka, A., Marcatili, P., Cattaneo, A., & Pastore, A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.773234 · Cited by 8
Nanobody-as versatile tool emerging in autoimmune diseases
Wang, L., Luo, R., Zhang, W., Jiang, H., Yu, Y., Zhou, W., Zhang, F., Ma, J., & Mei, L. (2024) · Smart Materials in Medicine · doi:10.1016/j.smaim.2024.10.003 · Cited by 6
Al-Qaoud, K. M., Sana, Y., Abdulrahman, R., Khalil, R., & Sami, A.-H. (2015) · Allergy Asthma and Immunology Research · doi:10.4168/aair.2015.7.6.583 · Cited by 6
“Another factor that favors the use of camel HCAbs and makes them less anaphylactic is the retention of activity while being monovalent.(31) In contrast to the bivalent nature of human and mouse MAb, HCAb and its VHH nanobody are active as a single chain or domain format.”
BackgroundInhibitory Potential of Polyclonal Camel Antibodies against New Delhi Metallo-β-lactamase-1 (NDM-1)
Abderrazek, R. B., Chammam, S., Ksouri, A., Perilli, M., Dhaouadi, S., Mdini, I., Benlasfar, Z., Amicosante, G., Bouhaouala‐Zahar, B., & Piccirilli, A. (2020) · Molecules · doi:10.3390/molecules25194453 · Cited by 6
“The unique characteristic of the variable domain of HcAbs termed nanobodies [21,22] has sped up progress in antibody development against various antigens such as enzymes [23–25].”
BackgroundKhaleghi, S., Rahbarizadeh, F., & Nikkhoi, S. K. (2021) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892816666210806150929 · Cited by 6
Promises and Challenges of the Type Three Secretion System Injectisome as an Antivirulence Target
Fasciano, A. C., Shaban, L., & Mecsas, J. C. (2019) · ASM Press eBooks · doi:10.1128/9781683670285.ch21 · Cited by 6
VH-Based Mini Q-Body: A Novel Quench-Based Immunosensor
Dong, J., Banwait, B., Ueda, H., & Kristensen, P. K. (2023) · Sensors · doi:10.3390/s23042251 · Cited by 6
Kabir, M. E., Krishnaswamy, S., Miyamoto, M., Furuichi, Y., & Komiyama, T. (2011) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-011-3123-8 · Cited by 6
Anti-infective antibodies—Reviving an old paradigm
Lachmann, P. J. (2009) · Vaccine · doi:10.1016/j.vaccine.2009.09.137 · Cited by 6
Avances biotecnológicos en el diagnóstico de enfermedades infecciosas
Hernández‐Hernández, F. D. L. C., & Rodriguez, M. H. (2009) · Salud Pública de México · doi:10.1590/s0036-36342009000900008 · Cited by 6
Saqafi, B., & Rahbarizadeh, F. (2017) · Journal of Bioactive and Compatible Polymers · doi:10.1177/0883911517707775 · Cited by 6
Advances in Neurotherapeutic Delivery Technologies
Mr Pradeep, K. (2015) · OMICS International eBooks · doi:10.4172/978-1-63278-036-2-037 · Cited by 6
The Development of Single Domain Antibodies for Diagnostic and Therapeutic Applications
Leow, C. H., Cheng, Q., Fischer, K., & McCarthy, J. S. (2018) · InTech eBooks · doi:10.5772/intechopen.73324 · Cited by 6
Chen, X., Nie, K., Zhang, X., Tan, S., Zheng, Q., Wang, Y., Chen, X., Tang, Z., Liu, R., Yan, M., et al. (2020) · Bioscience Reports · doi:10.1042/bsr20194515 · Cited by 6
Chin-Fatt, A., & Menassa, R. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.686421 · Cited by 6
Schmitt, M. G., Rajendra, Y., Hougland, M. D., Boyles, J. S., & Barnard, G. C. (2017) · Biotechnology Progress · doi:10.1002/btpr.2527 · Cited by 6
Challenges in developing mucosal vaccines and antibodies against infectious diarrhea in children
Tokuhara, D. (2017) · Pediatrics International · doi:10.1111/ped.13497 · Cited by 6
Half‐Life Extension through PEGylation
Jevševar, S., & Kunstelj, M. (2012) · doi:10.1002/9783527644827.ch3 · Cited by 6
Lei, E. K., Ryan, S., van Faassen, H., Foss, M., Robotham, A. C., Baltat, I., Fulton, K. M., Henry, K. A., Chen, W., & Hussack, G. (2023) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12594-1 · Cited by 5
“The weaker but measurable response generated against 17978 and LAC-4 OMV preparations suggests there could be other non-CsuA/B targets recognized by the heavy-chain IgGs.”
BackgroundInfluentialFranz, L., Rubil, T., Balázs, A., Overtus, M., Kemnitz‐Hassanin, K., Govaerts, C., Mall, M. A., & Hackenberger, C. P. R. (2026) · Nature Chemical Biology · doi:10.1038/s41589-026-02199-w · Cited by 6
“To assess these effects, we used a range of biochemical and functional methods, including confocal fluorescence live-cell microscopy, flow cytometry, western blot analysis and transepithelial short-circuit current ( I sc ) measurements.”
Auditeau, C., Nguyen, T.-S., Devaux, F., Saller, F., Peyron, I., Blandinières, A., Repérant, C., Daramé, S., Denis, C. V., Lenting, P. J., et al. (2024) · Thrombosis and Haemostasis · doi:10.1055/a-2373-2829 · Cited by 5
“37 Alternatively, ZPI-sdAb2 ’ s mild procoagulant activity could also be considered as an asset for the therapeutic rebalancing of hemostasis in patients with bleeding disorders in which an over-enhancement of thrombin generation is not necessarily sought.”
Molecular engineering of nanobodies as tools in allergology: diagnostics and beyond
Aagaard, J. B., Ballegaard, A. R., Ommen, P., & Spillner, E. (2023) · Allergo Journal International · doi:10.1007/s40629-023-00261-w · Cited by 6
“Signal sequences often enable secretion into the culture medium even in bacteria and straightforward purification, making production and downstream characterization highly convenient [36, 40].”
BackgroundIdentification and In Vitro Characterization of Phage-Displayed VHHs Targeting VEGF
Farajpour, Z., Rahbarizadeh, F., Kazemi, B., Ahmadvand, D., & Mohaghegh, M. H. (2013) · SLAS DISCOVERY · doi:10.1177/1087057113514275 · Cited by 5
Chow, K. M., Whiteheart, S. W., Smiley, J. R., Sharma, S., Boaz, K., Coleman, M. J., Maynard, A., Hersh, L. B., & Kooi, C. W. V. (2019) · Journal of Visualized Experiments · doi:10.3791/58471-v · Cited by 5
Les systèmes alternatifs de production d’anticorps monoclonaux thérapeutiques
Olivier, S., & Mehtali, M. (2009) · médecine/sciences · doi:10.1051/medsci/200925121163 · Cited by 5
“La découverte en 1993 que les camélidés produisent naturellement des anticorps de forte affinité mais de petite taille, composés uniquement d’une chaîne lourde, plus résistants aux variations de température et de pH et donc plus aptes à être efficacement produits en bactéries, a relancé l’intérêt de ce système de prod…”
Nakayama, H., Murakami, A., Yoshida, M., Muraoka, J., Wakai, J., Kenjyou, N., & Ito, Y. (2016) · Monoclonal Antibodies in Immunodiagnosis and Immunotherapy · doi:10.1089/mab.2016.0003 · Cited by 5
“In contrast, the phage display method, reported by Smith et al., (10) is one tool for generating a monoclonal antibody (mAb)fragment,suchastheVHHantibodyfromtheCamelidae family, (11,12) single-chain variable fragments (scFv), and antigen-binding fragments from various animals.”
[Progress in nanobody and its application in diagnosis].
Kong, Q., Yao, Y., Chen, R., & Lu, S. (2014) · PubMed · Cited by 5
Single-domain antibodies for functional targeting of the signaling scaffold Shoc2
Jang, H., Wilson, P. G., Sau, M., Chawla, U., Rodgers, D. W., & Galperin, E. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.12.010 · Cited by 5
Antibody Engineering for Biosensor Applications
Hopkins, N. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0919-0_12 · Cited by 5
Phage display and Shiga toxin neutralizers
Bernedo‐Navarro, R. A., & Yano, T. (2016) · Toxicon · doi:10.1016/j.toxicon.2016.02.009 · Cited by 5
Timofeeva, A. M., Sedykh, S. E., & Nevinsky, G. A. (2025) · Vaccines · doi:10.3390/vaccines13121224 · Cited by 4
“Their simple architecture facilitates the construction of robust single-domain antibody libraries [94].”
Applications of Nanobodies in Biological Imaging
Sheng, L., Sheng, K., & Lü, P. (2025) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/cbr.2025.0005 · Cited by 4
“5,24 In contrast, Nbs, due to their small size, can address these de fi ciencies effectively.”
InfluentialProtein-based tools for the detection and characterisation of Oropouche virus infection
Merchant, M., Souza, J. D. P., Abdelkarim, S., Chakraborty, S., Neto, T. A. N., Manchay, K. I. G., Jorge, D. M. D. M., do Nascimento, V. A., Sun, Y., Caroe, E. R., et al. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00291-7 · Cited by 4
“In this study, we generated a panel of Variable Heavy-chain domains of camelid Heavy-chain antibodies (VHHs; a.k.a. nanobodies) (Harmsen and De Haard, 2007) that speci fi cally detect the nucleoprotein and surface glycoprotein of OROV.”
Genetically modified helminths as pharmaceutical biofactories
Walther, D., Smout, M. J., Giacomin, P., Brindley, P. J., Mitreva, M., Moyle, M., & Loukas, A. C. (2025) · Advances in Parasitology/Advances in parasitology · doi:10.1016/bs.apar.2025.08.001 · Cited by 4
Engineering nanobodies for drug delivery systems in Alzheimer’s disease
Jootar, T., Hongeng, S., & Chiangjong, W. (2026) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2026.2617707 · Cited by 4
Kavousipour, S., Mohammadi, S., Eftekhar, E., Barazesh, M., & Morowvat, M. H. (2020) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201021666201012162904 · Cited by 4
(Photo-)chemical roadmap to strategic antimicrobial photodynamic and photothermal therapies
Bongaerts, G. P. A., Williams, R. M., van der Wielen, M. W. J., & Feiters, M. C. (2022) · Journal of Porphyrins and Phthalocyanines · doi:10.1142/s1088424622500493 · Cited by 4
Zhang, T., Yang, D., Tang, L., & Hu, Y. (2024) · Molecular Medicine Reports · doi:10.3892/mmr.2024.13272 · Cited by 5
“…large‑scale production via prokaryotic expression systems in a matter of weeks, which allows for their swift deployment in an emergency situation (129). a nb termed nb6 has been previously reported to stabilize two adjacent rBds in the ‘down’ state after binding to S proteins, which may then…”
BackgroundZhang, Y., Tian, C., Yu, X., Yu, G., Han, X., Wang, Y., Zhou, H., Zhang, S., Li, M., Yang, T., et al. (2024) · Vaccines · doi:10.3390/vaccines12121315 · Cited by 4
Prygiel, M., Mosiej, E., Wdowiak, K., & Zasada, A. A. (2024) · Biomedicines · doi:10.3390/biomedicines12122920 · Cited by 4
“Despite their simple structure, these antibodies have unique properties such as high solubility and remarkable stability, even in extreme conditions (e.g., over a wide range of pH and temperatures) [22].”
Nanobody, New Agent for Combating Against Breast Cancer Cells
Rahbarizadeh, F., Rahimi, F. C., & Sofla, F. J. I. (2011) · InTech eBooks · doi:10.5772/22927 · Cited by 4
Production of active single-chain antibodies in seeds using trimeric polyoleosin fusion
Winichayakul, S., Pernthaner, A., Livingston, S., Cookson, R., Scott, R., & Roberts, N. (2012) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2012.07.195 · Cited by 4
Brummelhuis, W. J., Joles, J. A., Stam, J. C., Adams, H., Goldschmeding, R., Detmers, F. J. M., Khattabi, M. E., Maassen, B., Verrips, C. T., & Braam, B. G. (2010) · Shock · doi:10.1097/shk.0b013e3181cdc556 · Cited by 4
“Recently, a technique has been developed that enables easy, low-cost, large-scale selection and production of the variable domain of the heavy chain Camelidae Abs (VHH) (5).”
MethodYang, S., Li, Y., YouJun, S., Wu, J., Liu, X., Zhang, J., PEJSAK, Z., Podgórska, K., Stępniewska, K., Khan, M. U. Z., et al. (2020) · BioMed Research International · doi:10.1155/2020/3201630 · Cited by 4
“)ese advantageous properties arise from their single-domain nature and from crucial amino acid mutations in the framework 2 (FR2) region; these mutations render the overall structure of sdAbs more hydrophilic than that of conventional antibody fragments [12].”
BackgroundRuffolo, C., Ferrara, F., Trevellin, E., Cataldo, I., Fornasier, C., Pozza, A., Dell'Orto, M. C., Angriman, I., Tos, A. P. D., Bardini, R., et al. (2020) · European Surgical Research · doi:10.1159/000510266 · Cited by 4
Selection of Antibody Fragments by Yeast Display
Scholler, N. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8648-4_12 · Cited by 4
Design of single-domain VHH antibodies to increase the binding activity in SPR amine coupling
Hirao, A., Nagatoishi, S., Ikeuchi, E., Yamawaki, T., Mori, C., Nakakido, M., & Tsumoto, K. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.04.048 · Cited by 4
Metadata
- Authors
- Harmsen, M. M., & De Haard, H. J.
- Affiliations
- Wageningen University & Research (NL)
- Ablynx (Belgium) (BE)
- Corresponding author
- Harmsen, M. M.
- Venue
- Applied Microbiology and Biotechnology
- Published
- 2007-08-18
- Volume
- 77
- Issue
- 1
- Pages
- 13-22
- ISSN
- 0175-7598 (ISSN-L)
- 1432-0614
- PMC
- PMC2039825
- OpenAlex
- W2147451568
- Cited by
- 809
- References
- 96
- Citations by year
- 2026: 31 · 2025: 43 · 2024: 48 · 2023: 41 · 2022: 41 · 2021: 65 · 2020: 57 · 2019: 49 · 2018: 53 · 2017: 42 · 2016: 46 · 2015: 48 · 2014: 53 · 2013: 40 · 2012: 52
- FWCI
- 2.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Applied Microbiology and Biotechnology (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Socio-Environmental Systems Modeling (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Life Sciences › Agricultural and Biological Sciences › Food Science › Animal Diversity and Health Studies
- Keywords
- single-domain antibody fragments, VHH, nanobodies, camelid antibodies, recombinant antibody production, yeast expression system, phage display, ribosome display, yeast surface display, therapeutic applications
- MeSH terms
- Animals, Camelids, New World, Immunoglobulin Fragments, Immunoglobulin Heavy Chains, Models, Biological
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
