Molecular Characterization of the Recombinant A-chain of a Type Ⅱ Ribosome-Inactivating Protein (RIP) from Viscum album coloratum and Structural Basis on its Ribosome-Inactivating Activity and the Sugar-binding Properties of the B-chain

Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with c...

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Published inBMB reports Vol. 39; no. 5; pp. 560 - 570
Main Authors Ye, Wenhui (Nanyang Technological University, Singapore), Nanga, Ravi Prakash Reddy (Nanyang Technological University, Singapore), Kang, C.B. (Nanyang Technological University, Singapore), Song, J.H. (Handong University, Pohang, Republic of Korea), Song, S.K. (Handong University, Pohang, Republic of Korea), Yoon, H.S. (Nanyang Technological University, Singapore), E-mail: hsyoon@ntu.edu.sg
Format Journal Article
LanguageEnglish
Published Korea (South) 30.09.2006
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Abstract Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described.
AbstractList Mistletoe (Viscum album) lectins, which are classified as a type II ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the Achain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described. However, the detailed mechanism in exerting unique cytotoxic effect on cancer cells still remains unclear. Here, we aim to understand and define the molecular basis and biological effects of the type II RIPs, through the studies of the recombinant Korean mistletoe lectin. To this end, we expressed, purified the recombinant Korean mistletoe lectin (rKML), and investigated its molecular characteristics in vitro, its cytotoxicity and ability to induce apoptotic cell death in cancer cells. To gain structural basis for its catalytic activity and sugar binding properties, we performed homology modeling studies based on the high degree of sequence identity and conserved secondary structure prediction between Korean and European, Himalayan mistletoe lectins, and Ricin.
Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described.
Author Yoon, H.S. (Nanyang Technological University, Singapore), E-mail: hsyoon@ntu.edu.sg
Nanga, Ravi Prakash Reddy (Nanyang Technological University, Singapore)
Song, S.K. (Handong University, Pohang, Republic of Korea)
Song, J.H. (Handong University, Pohang, Republic of Korea)
Ye, Wenhui (Nanyang Technological University, Singapore)
Kang, C.B. (Nanyang Technological University, Singapore)
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Snippet Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the...
Mistletoe (Viscum album) lectins, which are classified as a type II ribosome-inactivating protein (RIP) due to their unique biological function and the...
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SubjectTerms Amino Acid Sequence
Apoptosis
Carbohydrates - chemistry
Catalytic Domain
Cell Line, Tumor
Cell Survival - drug effects
Circular Dichroism
Glycosylation
Humans
Inhibitory Concentration 50
LECTINAS
LECTINE
LECTINS
Magnetic Resonance Spectroscopy
Models, Molecular
Molecular Sequence Data
N-Glycosyl Hydrolases - metabolism
Plant Preparations - chemistry
Plant Preparations - metabolism
Plant Preparations - pharmacology
Plant Proteins - chemistry
Plant Proteins - genetics
Plant Proteins - metabolism
Plant Proteins - pharmacology
Protein Folding
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Recombinant Proteins - pharmacology
Ribosome Inactivating Proteins
Ribosome Inactivating Proteins, Type 2
Ribosome-inactivating protein
Ricin - chemistry
Ricin - genetics
Structural Homology, Protein
Sugar binding
Toxins, Biological - chemistry
Toxins, Biological - genetics
Toxins, Biological - metabolism
Toxins, Biological - pharmacology
Viscum album - chemistry
Viscum album coloratum
Title Molecular Characterization of the Recombinant A-chain of a Type Ⅱ Ribosome-Inactivating Protein (RIP) from Viscum album coloratum and Structural Basis on its Ribosome-Inactivating Activity and the Sugar-binding Properties of the B-chain
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Volume 39
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