[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 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 cytotoxic effect on 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.
Tonevitskiĭ
A G
AG
Institute of Transplantology and Artificial Organs, Moscow, 123182 Russia.
Agapov
I I
II
Maliuchenko
N V
NV
Moĭsenovich
M M
MM
Vediakov
A M
AM
D016475:3T3 Cells / Q000187:drug effects; D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D051379:Mice; D008969:Molecular Sequence Data; D028321:Plant Preparations / Q000737:chemistry* / Q000276:immunology / Q000494:pharmacology*; D010940:Plant Proteins; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000494:pharmacology; D054790:Ribosome Inactivating Proteins, Type 2; D017386:Sequence Homology, Amino Acid; D014118:Toxins, Biological / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000494:pharmacology*
D028321:Plant Preparations; D010940:Plant Proteins; D021122:Protein Subunits; D011994:Recombinant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological; C009674:ribosome inactivating protein, Viscum