Optimization of the production of triabin, a novel thrombin inhibitor, in High Five™ insect cells infected with a recombinant baculovirus.

Cytotechnology
M Vallazza, T Petri

Abstract

The isolation of a new type of thrombin inhibitor, called triabin, from the saliva of the hematophagous bug Triatoma pallidipennis, has recently been described. In the in vitro platelet aggregation inhibition assay triabin has a similar potency as the thrombin inhibitor hirudin now in phase III clinical trials. However, in another in vitro assay using a low molecular weight substrate for thrombin, triabin does not inhibit thrombin completely even at 6 fold higher molar doses in comparison with hirudin. This means that triabin has a novel mode of action towards thrombin making triabin into an interesting candidate as a therapeutic agent. Recently it has been shown that a recombinant baculovirus can be efficiently used for the triabin production in insect cells and that the yields in adherent cultures of High Five™ cells (approx. 20 mg l-1) were about 7 fold higher than in adherent cultures of Sf9 cells (approx. 3 mg l- 1). To optimize the triabin yield from the baculovirus/insect cell expression system, experiments were performed with suspension adapted cultures of High Five™ cells to investigate the effects of the state of the host cell, of the multiplicity of infection, of the cell density at the time of infection and of suppl...Continue Reading

References

Dec 1, 1995·The Journal of Biological Chemistry·C Noeske-JungblutW D Schleuning
May 1, 1993·In Vitro Cellular & Developmental Biology. Animal·T R DavisH A Wood
Oct 29, 1997·Proceedings of the National Academy of Sciences of the United States of America·P Fuentes-PriorW Bode

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Citations

Jun 23, 2010·Protein Expression and Purification·Yael ElbazShimon Schuldiner
Jan 8, 2022·Biochemical Society Transactions·Jorge Ripoll-RozadaPedro José Barbosa Pereira

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