Abstract

A DNA fragment encoding the N-terminal half (N-lobe) of the human lactoferrin (hLfN) gene has now been cloned into recombinant Potexvirus potato virus X (PVX) vector and expressed in Nicotiana benthmiana using agroinfection. Western blot analysis showed the recombinant protein with an apparent molecular mass on electrophoresis of ca. 40 kDa, corresponding to the predicted size of the hLfN. The yield of hLfN reached a maximum (up to 0.6% of total soluble proteins) when recombinant PVX systemically infected an entire plant. Protein extracts from infected plants had antibacterial activity.

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