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Expression of Triabin, a Novel Highly Potent Inhibitor of Thrombin, in Sf9 and High Five Insect Cells using a Recombinant Baculovirus

Authors: Thomas Petri, Birgit Neukamm, Marina Isernhagen, Brigitte Ockert, Christiane Noeske-Jungblut,

Publish Date: 1997
Volume: , Issue:, Pages: 525-528
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Abstract

Triabin is a novel thrombin inhibitor originally isolated from the saliva of the hematophageous bug Triatoma pallidipennis. The mechanism of thrombin inhibition by triabin is different from other known inhibitors like hirudin or heparin/anti-thrombin III, but the potency of triabin is similar to that of hirudin. Using the cloned cDNA of triabin, a recombinant baculovirus expressing this secreted protein was constructed. However, only low expression rates were obtained in Sf9 insect cells infected with this virus (1–3 mg per 1 culture). Therefore, the expression of triabin in High five insect cells was also investigated and it was found that from these cells 3–8 times higher yields could be obtained. Recombinant triabin purified from the insect culture supernatants had a biological activity similar to that of natural salivary triabin. The availability of an efficient production process and the unique biological properties of triabin suggest that this protein has a potential as a novel therapeutic.


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