| Title: | The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1010947 |
| landingPage: |
http://www.iedb.org/assay/1478461 |
| type: |
Literature
|
| publicationVenue: |
FEBS Lett
|
| dates: |
1999
|
| study type: | b cell assays |
| subject species: | Streptococcus pneumoniae |
| fullName: |
M D Cima-Cabal
A Darji
F J Mé
ndez
F Vá
zquez
A A Jacobs
Y Shimada
Y Ohno-Iwashita
S Weiss
J R de los Toyos
|
| method: |
biological activity
|
| name: |
The conserved undecapeptide shared by thiol-activated cytolysins is involved in membrane binding.
|
| description: |
This conserved sequence is present in thiol-activated pore-forming cytolysins produced by several species of Gram-positive bacteria.
Binding of epitope-specific mAb PLY-5 to SLO prevented the binding of SLO to sheep RBC and neutralized its hemolytic activity.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |