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Mistletoe lectin dissociates into catalytic and binding subunits before translocation across the membrane to the cytoplasm
Author(s) -
Agapov Igor I.,
Tonevitsky Alexander G.,
Moysenovich Mikhail M.,
Maluchenko Natalya V.,
Weyhenmeyer Roland,
Kirpichnikov Mikhail P.
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00639-0
Subject(s) - ricin , lectin , epitope , ribosome inactivating protein , viscum album , monoclonal antibody , chemistry , protein subunit , intracellular , microbiology and biotechnology , biochemistry , toxin , biology , antigen , antibody , ribosome , rna , immunology , ecology , gene
Hybridomas producing monoclonal antibodies (mAbs) against the mistletoe lectin A‐chain (MLA) were obtained to investigate the intracellular routing and translocation of ribosome‐inactivating proteins. Anti‐MLA mAb MNA5 did not bind the holotoxin but interacted with isolated MLA. This epitope was not recognized upon MLA denaturation or conjugation of MLA with the ricin binding subunit (RTB). Furthermore, the mAbs did not appreciably react with a panel of MLA synthetic octapeptides linked to the surface of polyethylene pins. A study of the cytotoxicity of mistletoe lectin, ricin, and chimeric toxin MLA/RTB for the hybridomas revealed that interchain disulfide bond reduction and subunit dissociation are required for cytotoxic activity of mistletoe lectin.