ArticleApplied and environmental microbiology2005
Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 123 citations in OpenAlex.
- Article
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- Nanobody: A Small Antibody with Big Implications for Tumor Therapeutic Strategy.International journal of nanomedicine · 2021Review
- Stabilization of a Broadly Neutralizing Anti-Chikungunya Virus Single Domain Antibody.Frontiers in medicine · 2021Article
- A nanobody-derived mimotope against VEGF inhibits cancer angiogenesis.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Construction of a Nanobodies Phage Display Library From an Escherichia coli Immunized Dromedary.Iranian journal of biotechnology · 2020Article
- Review
- Design of a humanized anti vascular endothelial growth factor nanobody and evaluation of itsIranian journal of basic medical sciences · 2018Article
- Selection, characterization, and thermal stabilization of llama single domain antibodies towards Ebola virus glycoprotein.Microbial cell factories · 2017Article
- Single Domain Antibodies as New Biomarker Detectors.Diagnostics (Basel, Switzerland) · 2017Review
- Fungal Glucosylceramide-Specific Camelid Single Domain Antibodies Are Characterized by Broad Spectrum Antifungal Activity.Frontiers in microbiology · 2017Article
- Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
As part of research exploring the feasibility of using antibody fragments to inhibit the growth of organisms implicated in dandruff, we isolated antibody fragments that bind to a cell surface protein of Malassezia furfur in the presence of shampoo. We found that phage display of llama single-domain antibody fragments (VHHs) can be extended to very harsh conditions, such as the presence of shampoo containing nonionic and anionic surfactants. We selected several VHHs that bind to the cell wall protein Malf1 of M. furfur, a fungus implicated in causing dandruff. In addition to high stability in the presence of shampoo, these VHHs are also stable under other denaturing conditions, such as high urea concentrations. Many of the stable VHHs were found to contain arginine at position 44. Replacement of the native amino acid at position 44 with arginine in the most stable VHH that lacked this arginine resulted in a dramatic further increase in the stability. The combination of the unique properties of VHHs together with applied phage display and protein engineering is a powerful method for obtaining highly stable VHHs that can be used in a wide range of applications.
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