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Type-2 ribosome-inactivating proteins, composed of a toxic A-chain and lectin-like B-chain, display various biological functions, including cytotoxicity and immunomodulation. We here cloned the lectin-like B-chain encoding fragment of a newly identified type-2 RIP gene,  articulatin  gene, from  Viscum articulatum , into a bacterial expression vector to obtain nonglycosylated recombinant protein expressed in inclusion bodies. After purification and protein refolding, soluble refolded recombinant articulatin B-chain (rATB) showed lectin activity specific toward galactoside moiety and was stably maintained while stored in low ionic strength solution. Despite lacking glycosylation, rATB actively bound leukocytes with preferential binding to monocytes and  in vitro  stimulated PBMCs to release cytokines without obvious cytotoxicity. These results implicated such a B-chain fragment as a potential immunomodulator.

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Production of Active Nonglycosylated Recombinant B-Chain of Type-2 Ribosome-Inactivating Protein from<i>Viscum articulatum</i>and Its Biological Effects on Peripheral Blood Mononuclear Cells

Production of Active Nonglycosylated Recombinant B-Chain of Type-2 Ribosome-Inactivating Protein fromViscum articulatumand Its Biological Effects on Peripheral Blood Mononuclear Cells