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lysozyme/nicotiana

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Fungal and bacterial disease resistance in transgenic plants expressing human lysozyme.

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The human lysozyme gene, which is assembled by the stepwise ligation of chemically synthesized oligonucleotides, was introduced into tobacco (Nicotiana tabacum cv `SR1') by the Agrobacterium-mediated method. The introduced human lysozyme gene was highly expressed under the control of the cauliflower

Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme.

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A new PR (pathogenesis-related) protein was isolated from tobacco leaves (Nicotiana tabacum cv. Samsun NN), reacting hypersensitively to tobacco mosaic virus (TMV), by zinc chelate chromatography and was therefore named Pz. Its reactivity toward several lectins indicated the presence of bound sugar
Solanum tuberosum plants were transformed with three genetic constructions expressing the Nicotiana tabacum AP24 osmotine, Phyllomedusa sauvagii dermaseptin and Gallus gallus lysozyme, and with a double-transgene construction expressing the AP24 and lysozyme sequences. Re-transformation of

Assembly of two transgenes in an artificial chromatin domain gives highly coordinated expression in tobacco.

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The chromatin loop model predicts that genes within the same chromatin domain exhibit coordinated regulation. We here present the first direct experimental support for this model in plants. Two reporter genes, the E. coli beta-glucuronidase gene and the firefly luciferase gene, driven by different

Substrate specificity and antifungal activity of recombinant tobacco class I chitinases.

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Endochitinases contribute to the defence response of plants against chitin-containing pathogens. The vacuolar class I chitinases consist of an N-terminal cysteine-rich domain (CRD) linked by a glycine-threonine-rich spacer with 4-hydroxylated prolyl residues to the catalytic domain. We examined the

High-level expression of Camelid nanobodies in Nicotiana benthamiana.

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Nanobodies (or VHHs) are single-domain antigen-binding fragments derived from Camelid heavy chain-only antibodies. Their small size, monomeric behaviour, high stability and solubility, and ability to bind epitopes not accessible to conventional antibodies make them especially suitable for many
Many studies in both animal and plant systems have shown that matrix attachment regions (MARs) can increase the expression of flanking transgenes. However, our previous studies revealed no effect of the chicken lysozyme MARs (chiMARs) on transgene expression in the first generation transgenic
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