Premium
Hemagglutinin‐33 of type A botulinum neurotoxin complex binds with synaptotagmin II
Author(s) -
Zhou Yu,
Foss Sean,
Lindo Paul,
Sarkar Hemanta,
Singh Bal Ram
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.04688.x
Subject(s) - clostridium botulinum , neurotoxin , botulinum neurotoxin , botulism , proteolysis , protease , hemagglutinin (influenza) , clostridiaceae , chemistry , synaptotagmin 1 , synaptotagmin i , biochemistry , biology , microbiology and biotechnology , toxin , gene , enzyme , vesicle , synaptic vesicle , membrane
Botulinum neurotoxin type A (BoNT/A), the most toxic substance known to mankind, is produced by Clostridium botulinum type A as a complex with a group of neurotoxin‐associated proteins (NAPs) through polycistronic expression of a clustered group of genes. NAPs are known to protect BoNT against adverse environmental conditions and proteolytic digestion. Hemagglutinin‐33 (Hn‐33) is a 33 kDa subcomponent of NAPs that is resistant to protease digestion, a feature likely to be involved in the protection of the botulinum neurotoxin from proteolysis. However, it is not known whether Hn‐33 plays any role other than the protection of BoNT. Using immunoaffinity column chromatography and pull‐down assays, we have now discovered that Hn‐33 binds to synaptotagmin II, the putative receptor of botulinum neurotoxin. This finding provides important information relevant to the design of novel antibotulism therapeutic agents targeted to block the entry of botulinum neurotoxin into nerve cells.