Unknown

Dataset Information

0

Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA .


ABSTRACT: The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A-G) based on a lack of cross antiserum neutralization. BoNTs utilize gangliosides as components of the host receptors for binding and entry into neurons. Members of BoNT/C and BoNT/D serotypes include mosaic toxins that are organized in D/C and C/D toxins. One D/C mosaic toxin, BoNT/D-South Africa (BoNT/D-SA), was not fully neutralized by immunization with BoNT serotype C or D, which stimulated this study. Here the crystal structures of the receptor binding domains of BoNT/C, BoNT/D, and BoNT/D-SA are presented. Biochemical and cell binding studies show that BoNT/C and BoNT/D-SA possess unique mechanisms for ganglioside binding. These studies provide new information about how the BoNTs can enter host cells as well as a basis for understanding the immunological diversity of these neurotoxins.

SUBMITTER: Karalewitz AP 

PROVIDER: S-EPMC2939319 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

Identification of a unique ganglioside binding loop within botulinum neurotoxins C and D-SA .

Karalewitz Andrew P-A AP   Kroken Abby R AR   Fu Zhuji Z   Baldwin Michael R MR   Kim Jung-Ja P JJ   Barbieri Joseph T JT  

Biochemistry 20100901 37


The botulinum neurotoxins (BoNTs) are the most potent protein toxins for humans. There are seven serotypes of BoNTs (A-G) based on a lack of cross antiserum neutralization. BoNTs utilize gangliosides as components of the host receptors for binding and entry into neurons. Members of BoNT/C and BoNT/D serotypes include mosaic toxins that are organized in D/C and C/D toxins. One D/C mosaic toxin, BoNT/D-South Africa (BoNT/D-SA), was not fully neutralized by immunization with BoNT serotype C or D, w  ...[more]

Similar Datasets

| S-EPMC3170675 | biostudies-literature
| S-EPMC3190786 | biostudies-literature
| S-EPMC4549225 | biostudies-literature
| S-EPMC5923309 | biostudies-literature
| S-EPMC1716154 | biostudies-literature
| S-EPMC5394922 | biostudies-literature
| S-EPMC5696347 | biostudies-literature
| S-EPMC5983264 | biostudies-literature
| S-EPMC1276967 | biostudies-literature
| S-EPMC6070880 | biostudies-literature