The first 5 to 11 amino acids of the N-terminus of a family of proteins from the North American Opossum (<i>Didelphis virginiana</i>) has been shown to completely neutralize the hemorrhagic toxins found in certain snake venoms. This has significant implications for certain regions of the world where the majority of snakebite morbidity is due to the hemorrhagens. In order to increase the stability and bioactivity of the opossum peptide, it was attached to the N-terminus of a camelid nanobody (<i>Lama glama</i>) and expressed in E. coli (Bl21(DE3)) using a PelB secretion signal. Mass spectrometry has confirmed the protein, secreted into the culture broth and purified with a Protein A column, has been folded with intact disulfide bond. The presentation will describe the expression and purification of the nanobody conjugate and the resulting activity of the protein.

Engineered nanobody for neutralization of snake venom toxins

ACS Spring 2022

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