Application of camelid heavy-chain variable domains (VHHs) in prevention and treatment of bacterial and viral infections - PubMed (original) (raw)
Review
. 2018 Jan 2;37(1):69-76.
doi: 10.1080/08830185.2017.1397657. Epub 2017 Nov 28.
Affiliations
- PMID: 29182399
- DOI: 10.1080/08830185.2017.1397657
Review
Application of camelid heavy-chain variable domains (VHHs) in prevention and treatment of bacterial and viral infections
Lucas Wilken et al. Int Rev Immunol. 2018.
Abstract
Camelid heavy-chain variable domains (VHHs) are the smallest, intact, antigen-binding units to occur in nature. VHHs possess high degrees of solubility and robustness enabling generation of multivalent constructs with increased avidity - characteristics that mark their superiority to other antibody fragments and monoclonal antibodies. Capable of effectively binding to molecular targets inaccessible to classical immunotherapeutic agents and easily produced in microbial culture, VHHs are considered promising tools for pharmaceutical biotechnology. With the aim to demonstrate the perspective and potential of VHHs for the development of prophylactic and therapeutic drugs to target diseases caused by bacterial and viral infections, this review article will initially describe the structural features that underlie the unique properties of VHHs and explain the methods currently used for the selection and recombinant production of pathogen-specific VHHs, and then thoroughly summarize the experimental findings of five distinct studies that employed VHHs as inhibitors of host-pathogen interactions or neutralizers of infectious agents. Past and recent studies suggest the potential of camelid heavy-chain variable domains as a novel modality of immunotherapeutic drugs and a promising alternative to monoclonal antibodies. VHHs demonstrate the ability to interfere with bacterial pathogenesis by preventing adhesion to host tissue and sequestering disease-causing bacterial toxins. To protect from viral infections, VHHs may be employed as inhibitors of viral entry by binding to viral coat proteins or blocking interactions with cell-surface receptors. The implementation of VHHs as immunotherapeutic agents for infectious diseases is of considerable potential and set to contribute to public health in the near future.
Keywords: Immunotherapy; infectious disease; nanobodies; single-domain antibody.
Similar articles
- Nanobodies®: new ammunition to battle viruses.
Vanlandschoot P, Stortelers C, Beirnaert E, Ibañez LI, Schepens B, Depla E, Saelens X. Vanlandschoot P, et al. Antiviral Res. 2011 Dec;92(3):389-407. doi: 10.1016/j.antiviral.2011.09.002. Epub 2011 Sep 10. Antiviral Res. 2011. PMID: 21939690 Review. - Construction of a camelid VHH yeast two-hybrid library and the selection of VHH against haemagglutinin-neuraminidase protein of the Newcastle disease virus.
Gao X, Hu X, Tong L, Liu D, Chang X, Wang H, Dang R, Wang X, Xiao S, Du E, Yang Z. Gao X, et al. BMC Vet Res. 2016 Feb 26;12:39. doi: 10.1186/s12917-016-0664-1. BMC Vet Res. 2016. PMID: 26920806 Free PMC article. - Alpaca (Lama pacos) as a convenient source of recombinant camelid heavy chain antibodies (VHHs).
Maass DR, Sepulveda J, Pernthaner A, Shoemaker CB. Maass DR, et al. J Immunol Methods. 2007 Jul 31;324(1-2):13-25. doi: 10.1016/j.jim.2007.04.008. Epub 2007 May 15. J Immunol Methods. 2007. PMID: 17568607 Free PMC article. - Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features.
Harmsen MM, Ruuls RC, Nijman IJ, Niewold TA, Frenken LG, de Geus B. Harmsen MM, et al. Mol Immunol. 2000 Aug;37(10):579-90. doi: 10.1016/s0161-5890(00)00081-x. Mol Immunol. 2000. PMID: 11163394 - Expression of single-domain antibody in different systems.
Liu Y, Huang H. Liu Y, et al. Appl Microbiol Biotechnol. 2018 Jan;102(2):539-551. doi: 10.1007/s00253-017-8644-3. Epub 2017 Nov 25. Appl Microbiol Biotechnol. 2018. PMID: 29177623 Review.
Cited by
- Revolutionizing antiviral therapy with nanobodies: Generation and prospects.
Mustafa MI, Mohammed A. Mustafa MI, et al. Biotechnol Rep (Amst). 2023 Jun 7;39:e00803. doi: 10.1016/j.btre.2023.e00803. eCollection 2023 Sep. Biotechnol Rep (Amst). 2023. PMID: 37332617 Free PMC article. Review. - A Small Virus to Deliver Small Antibodies: New Targeted Therapies Based on AAV Delivery of Nanobodies.
Silva-Pilipich N, Smerdou C, Vanrell L. Silva-Pilipich N, et al. Microorganisms. 2021 Sep 15;9(9):1956. doi: 10.3390/microorganisms9091956. Microorganisms. 2021. PMID: 34576851 Free PMC article. Review. - The role of nanotechnology in current COVID-19 outbreak.
Tavakol S, Zahmatkeshan M, Mohammadinejad R, Mehrzadi S, Joghataei MT, Alavijeh MS, Seifalian A. Tavakol S, et al. Heliyon. 2021 Apr;7(4):e06841. doi: 10.1016/j.heliyon.2021.e06841. Epub 2021 Apr 15. Heliyon. 2021. PMID: 33880422 Free PMC article. Review. - Perspective on therapeutic and diagnostic potential of camel nanobodies for coronavirus disease-19 (COVID-19).
Bessalah S, Jebahi S, Mejri N, Salhi I, Khorchani T, Hammadi M. Bessalah S, et al. 3 Biotech. 2021 Feb;11(2):89. doi: 10.1007/s13205-021-02647-5. Epub 2021 Jan 22. 3 Biotech. 2021. PMID: 33500874 Free PMC article. Review. - Role of antibody-dependent enhancement (ADE) in the virulence of SARS-CoV-2 and its mitigation strategies for the development of vaccines and immunotherapies to counter COVID-19.
Karthik K, Senthilkumar TMA, Udhayavel S, Raj GD. Karthik K, et al. Hum Vaccin Immunother. 2020 Dec 1;16(12):3055-3060. doi: 10.1080/21645515.2020.1796425. Epub 2020 Aug 26. Hum Vaccin Immunother. 2020. PMID: 32845733 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical
Miscellaneous