Premium
Tetanus toxin receptor Specific cross‐linking of tetanus toxin to a protein of NGF‐differentiated PC 12 cells
Author(s) -
Schiavo Giampietro,
Ferrari Giovanna,
Rossetto Ornella,
Montecucco Cesare
Publication year - 1991
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 - 10.1016/0014-5793(91)81266-b
Subject(s) - toxin , tetanus , chemistry , proteases , receptor , microbiology and biotechnology , biochemistry , biology , immunology , enzyme , vaccination
A subclone of rat pheochromocytoma cells expresses high affinity receptors for tetanus toxin on differentiation with NGF [Walton, K.M., Sandberg, K., Rogers, T.B. and Schnaar, R.L. (1988) J. Biol. Chem. 263, 2055–2063]. In the presence of protein cross‐linking agents, [ 125 I]tetanus toxin, bound to these cells at 0°C, forms a cross‐linked product with apparent molecular weight of 120 kDa. The formation of [ 125 I]tetanus toxin conjugate involves the heavy chain of the toxin, is prevented by cold toxin and it is largely reduced by pretreating cells with proteases, The cross‐linked product is formed only upon incubation of the toxin with NGF‐differentiated cells. These results suggest that a protein with apparent molecular weight of 20 kDa is involved in the neurospecific binding of tetanus toxin.