ArticlePloS one2014
Development and evaluation of single domain antibodies for vaccinia and the L1 antigen.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Review
- Bivalent single-domain antibodies show potent mpox virus neutralization through M1R antigen.Communications biology · 2025Article
- Functional epitopes and neutralizing antibodies of vaccinia virus.Frontiers in microbiology · 2023Review
- Bivalent single domain antibody constructs for effective neutralization of Venezuelan equine encephalitis.Scientific reports · 2022Article
- Developing Recombinant Antibodies by Phage Display Against Infectious Diseases and Toxins for Diagnostics and Therapy.Frontiers in cellular and infection microbiology · 2021Review
- Selection and Characterization of Single-Domain Antibodies for Detection of Lassa Nucleoprotein.Antibodies (Basel, Switzerland) · 2020Article
- Evaluation of a noncanonical Cys40-Cys55 disulfide linkage for stabilization of single-domain antibodies.Protein science : a publication of the Protein Society · 2019Article
- Selection and Characterization of Anti-Dengue NS1 Single Domain Antibodies.Scientific reports · 2018Article
- Selection of Single-Domain Antibodies towards Western Equine Encephalitis Virus.Antibodies (Basel, Switzerland) · 2018Article
- Genetic Fusion of an Anti-BclA Single-Domain Antibody with Beta Galactosidase.Antibodies (Basel, Switzerland) · 2018Article
- Article
- Pairing Alpaca and Llama-Derived Single Domain Antibodies to Enhance Immunoassays for Ricin.Antibodies (Basel, Switzerland) · 2017Article
- The role of intra-domain disulfide bonds in heat-induced irreversible denaturation of camelid single domain VHH antibodies.Journal of biochemistry · 2016Article
- Article
- Development of a Genus-Specific Antigen Capture ELISA for Orthopoxviruses - Target Selection and Optimized Screening.PloS one · 2016Article
- Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond.Microbial cell factories · 2015Article
- Improving the biophysical properties of anti-ricin single-domain antibodies.Biotechnology reports (Amsterdam, Netherlands) · 2015Article
- Evaluation of disulfide bond position to enhance the thermal stability of a highly stable single domain antibody.PloS one · 2014Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is ongoing interest to develop high affinity, thermal stable recognition elements to replace conventional antibodies in biothreat detection assays. As part of this effort, single domain antibodies that target vaccinia virus were developed. Two llamas were immunized with killed viral particles followed by boosts with the recombinant membrane protein, L1, to stimulate the immune response for envelope and membrane proteins of the virus. The variable domains of the induced heavy chain antibodies were selected from M13 phage display libraries developed from isolated RNA. Selection via biopanning on the L1 antigen produced single domain antibodies that were specific and had affinities ranging from 4×10(-9) M to 7.0×10(-10) M, as determined by surface plasmon resonance. Several showed good ability to refold after heat denaturation. These L1-binding single domain antibodies, however, failed to recognize the killed vaccinia antigen. Useful vaccinia binding single domain antibodies were isolated by a second selection using the killed virus as the target. The virus binding single domain antibodies were incorporated in sandwich assays as both capture and tracer using the MAGPIX system yielding limits of detection down to 4×10(5) pfu/ml, a four-fold improvement over the limit obtained using conventional antibodies. This work demonstrates the development of anti-vaccinia single domain antibodies and their incorporation into sandwich assays for viral detection. It also highlights the properties of high affinity and thermal stability that are hallmarks of single domain antibodies.
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