ArticleBMC biotechnology2011
Isolation of a highly thermal stable lama single domain antibody specific for Staphylococcus aureus enterotoxin B.
Article in BMC biotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- Analytical Performance of Nanobody-Based Immunoassay and Immunosensing Platforms for Bacteria and Toxin Detection: A Systematic Review.Antibodies (Basel, Switzerland) · 2026Review
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- Nanobodies in animal infectious disease control: diagnosis and therapy.Frontiers in cellular and infection microbiology · 2025Review
- A Multivalent and Thermostable Nanobody Neutralizing SARS-CoV-2 Omicron (B.1.1.529).International journal of nanomedicine · 2023Article
- Phage display for the detection, analysis, disinfection, and prevention ofSmart medicine · 2022Review
- Sequence Tolerance of a Single-Domain Antibody with a High Thermal Stability: Comparison of Computational and Experimental Fitness Profiles.ACS omega · 2019Article
- Selection and Characterization of Anti-Dengue NS1 Single Domain Antibodies.Scientific reports · 2018Article
- Article
- Article
- Enhancing Stability of Camelid and Shark Single Domain Antibodies: An Overview.Frontiers in immunology · 2017Review
- Investigational drugs to treat methicillin-resistant Staphylococcus aureus.Expert opinion on investigational drugs · 2016Review
- Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond.Microbial cell factories · 2015Article
- Antiviral activity of a single-domain antibody immunotoxin binding to glycoprotein D of herpes simplex virus 2.Antimicrobial agents and chemotherapy · 2015Article
- Development and utilization of camelid VHH antibodies from alpaca for 2,2',4,4'-tetrabrominated diphenyl ether detection.Analytical chemistry · 2014Article
- Isolation and epitope mapping of staphylococcal enterotoxin B single-domain antibodies.Sensors (Basel, Switzerland) · 2014Article
- Evaluation of disulfide bond position to enhance the thermal stability of a highly stable single domain antibody.PloS one · 2014Article
- Recombinant expression and purification of human placental growth factor 1 and specific camel heavy chain polyclonal antibody preparation.Saudi journal of biological sciences · 2014Article
- The staphylococcal enterotoxin (SE) family: SEB and siblings.Virulence · 2013Review
- Structure of a low-melting-temperature anti-cholera toxin: llama V(H)H domain.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Contributions of the complementarity determining regions to the thermal stability of a single-domain antibody.PloS one · 2013Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCamelids and sharks possess a unique subclass of antibodies comprised of only heavy chains. The antigen binding fragments of these unique antibodies can be cloned and expressed as single domain antibodies (sdAbs). The ability of these small antigen-binding molecules to refold after heating to achieve their original structure, as well as their diminutive size, makes them attractive candidates for diagnostic assays.
resultsHere we describe the isolation of an sdAb against Staphyloccocus aureus enterotoxin B (SEB). The clone, A3, was found to have high affinity (Kd = 75 pM) and good specificity for SEB, showing no cross reactivity to related molecules such as Staphylococcal enterotoxin A (SEA), Staphylococcal enterotoxin D (SED), and Shiga toxin. Most remarkably, this anti-SEB sdAb had an extremely high Tm of 85°C and an ability to refold after heating to 95°C. The sharp Tm determined by circular dichroism, was found to contrast with the gradual decrease observed in intrinsic fluorescence. We demonstrated the utility of this sdAb as a capture and detector molecule in Luminex based assays providing limits of detection (LODs) of at least 64 pg/mL.
conclusionThe anti-SEB sdAb A3 was found to have a high affinity and an extraordinarily high Tm and could still refold to recover activity after heat denaturation. This combination of heat resilience and strong, specific binding make this sdAb a good candidate for use in antibody-based toxin detection technologies.
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