AI Article Synopsis
- Haemoglobin (Hb) is crucial for transporting oxygen in vertebrates, and its low levels can indicate health issues like anaemia or colon cancer.
- A new sandwich-ELISA test using llama-derived nanobodies (NbE11 and NbB9) has been developed to detect human Hb without reacting to other vertebrates' Hb.
- Researchers have determined the crystal structure of NbE11 paired with human Hb, revealing high affinity binding mainly to the β-Hb subunit, which helps explain the test's specificity for human Hb.
Article Abstract
Haemoglobin (Hb) is a vital oxygen carrier in vertebrates. Low blood Hb levels may indicate anaemia or genetic disorders, while its presence in the lower digestive system suggests colon cancer. Detecting and quantifying human Hb is essential for medical diagnostics. A nanobody-based sandwich-ELISA test was recently developed utilising llama-derived nanobodies NbE11 and NbB9. These nanobodies specifically bind to human Hb without cross-reacting with Hb from other vertebrates. Here, we determine the crystal structure of NbE11 in complex with human Hb. NbE11 binds Hb with high affinity, predominantly binding the β-Hb subunit. Structural differences between human Hb and other vertebrates at the NbE11 binding interface likely explain the assay's lack of cross-reactivity, providing insights for developing Hb binding diagnostics.
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| http://dx.doi.org/10.1002/1873-3468.14958 | DOI Listing |
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