| 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/1478454 |
| 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: |
antigen inhibition
|
| 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.
The epitope sequence was deduced through study of overlapping peptides. The region of overlap indicated the core sequence to be WEWWRT. The epitope blocked the ability of mAb PLY-5 to neutralize the hemolytic activity of PLY. The epitope corresponds to the conserved undecapeptide shared by thiol-activated cytolysins.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |