Open AccessProperties of a protease‐sensitive acceptor component in mouse brain synaptosomes for Clostridium botulinum type B neurotoxin
Author(s) -
Ogasawara Jun,
Kamata Yoichi,
Sakaguchi Genji,
Kozaki Shunji
Publication year - 1991
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1991.tb04554.x
Subject(s) - neurotoxin , clostridium botulinum , biochemistry , synaptosome , protease , endopeptidase , neuraminidase , chemistry , enzyme , ganglioside , membrane , toxin , biology
Summary To characterize an acceptor for Clostridium botulinum type B neurotoxin, its binding kinetics were examined with mouse brain synaptosomes treated with various enzymes. The amount of 125 I‐labelled neurotoxin bound to synaptosomes decreased upon treatment with lysyl endopeptidase, neuraminidase, or phospholipase C. The binding of the neurotoxin was partially recovered by incubation of neuraminidase‐treated synaptosomes with ganglioside G T1b or G D1a . Gangliosides incorporated into untreated, lysyl endopeptidase‐treated, and phospholipase C‐treated synaptosomes had no effect on the binding of the neurotoxin. These results may suggest that type B neurotoxin binds to gangliosides in cooperation with a certain protease‐sensitive substance on the neural membranes.