Role of the Interchain Interaction Domain of Chain A in Viscumin Cytotoxicity

The sequence coding for the viscumin (mistletoe lectin I, MLI) A-chain (MLA) was cloned from Viscum album genomic DNA with the use of synthetic primers. This yielded three recombinant (r) MLA variants differing in the number of amino acid substitutions. The rMLA structure and properties were probed...

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Published inMolecular biology (New York) Vol. 36; no. 4; p. 528
Main Authors Tonevitskii, A G, Agapov, I I, Malyuchenko, N V, Moisenovich, M M, Vedyakov, A M
Format Journal Article
LanguageEnglish
Published New York Springer Nature B.V 01.07.2002
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Proteins
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Summary:The sequence coding for the viscumin (mistletoe lectin I, MLI) A-chain (MLA) was cloned from Viscum album genomic DNA with the use of synthetic primers. This yielded three recombinant (r) MLA variants differing in the number of amino acid substitutions. The rMLA structure and properties were probed using monoclonal antibodies against native MLA. Native MLI B-chain (MLB) was shown to facilitate the rMLA folding. Native MLI and chimeric proteins consisting of rMLA and native MLB did not differ in their cytotoxicity toward 3T3 fibroblastoid cells. Residues were identified that are located in the MLB-contacting region and have a considerable effect on the immunochemical and cytotoxic properties of rMLA.[PUBLICATION ABSTRACT]
ISSN:0026-8933
1608-3245
DOI:10.1023/A:1019808612072