ArticleFrontiers in endocrinology2017
Exploiting Nanobodies in the Detection and Quantification of Human Growth Hormone
Article in Frontiers in endocrinology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 12 citations in OpenAlex.
- A multispecies competitive nanobody-based ELISA for the detection of antibodies against hepatitis E virus.Scientific reports · 2023Article
- Engineered Yeast Displaying Specific Norovirus-Binding Nanobodies for the Concentration and Detection of Human Norovirus in Food Matrix.Journal of agricultural and food chemistry · 2023Article
- Characterization of rabbit polyclonal antibody against camel recombinant nanobodies.Open life sciences · 2022Article
- Application of Single-Domain Antibodies ("Nanobodies") to Laboratory Diagnosis.Annals of laboratory medicine · 2021Review
- Development and Evaluation of a Novel VHH-Based Immunocapture Assay for High-Sensitivity Detection of Shiga Toxin Type 2 (Stx2) in Stool Samples.Journal of clinical microbiology · 2020Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMonitoring blood levels of human growth hormone (hGH) in most children with short stature deficiencies is crucial for taking a decision of treatment with extended course of daily and expensive doses of recombinant hGH (rhGH or Somatropin
methodsA fully nanobody-based sandwich ELISA method was developed in this work for direct measurement of GH in biological samples.
resultsTwo major characteristics of nanobody were exploited for this goal: the robust and stable structure of the nanobody (NbGH04) used to capture hGH from tested samples, and the great ability of tailoring, enabling the display of the anti-GH detector nanobody (NbGH07) on the tip of M13-phage. Such huge, stable, and easy-to-prepare phage-Nb was used in ELISA to provide an amplified signal. Previously, NbGH04 was retrieved on immobilized hGH by phage display from a wide "immune" cDNA library prepared from a hGH-immunized camel. Here, and in order to assure epitope heterogeneity, NbGH07 was isolated from the same library using NbGH04-captured hGH as bait. Interaction of both nanobodies with hGH was characterized and compared with different anti-GH nanobodies and antibodies. The sensitivity (~0.5 ng/ml) and stability of the nanobody-base sandwich ELISA were assessed using rhGH before testing in the quantification of hGH in blood sera and cell culture supernatants.
conclusionIn regard to all advantages of nanobodies; stability, solubility, production affordability in
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