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Pinellia ternata agglutinin produced in Bombyx mori cells exhibits bioactivity

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Xu T., Wang B., Wang L., Zhang Y., Lv Z.
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2012
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vol. 59
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issue 2
231-236
EN
Pinellia ternata agglutinin (PTA) is highly homologous to many other monocot mannose-binding lectins which reportedly possess antitumor activities. Its production in silkworm cells has great application potential because the baculovirus expression system can produce post-translationally modified proteins at low cost. In the current study, the pta gene was cloned and expressed in silkworm cells, and the expressed protein was analyzed using a hemagglutination assay. A preliminary in vitro study on its anti-proliferative activity was performed. The results show that the recombinant PTA with an apparent molecular mass of 29 kDa can hemagglutinate rabbit erythrocytes and this activity can be inhibited by D-mannan at a low concentration. In addition, the recombinant hemagglutinin exhibited a dose-dependent anti-proliferative activity on hepatoma cells. The results of the current study suggest that PTA and other important bioactive proteins could be produced by silkworm bioreactor for biomedicine research and application.
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