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Title: Adherence of Pseudomonas aeruginosa and Candida albicans to glycosphingolipid (Asialo-GM1) receptors is achieved by a conserved receptor-binding domain present on their adhesins.
identifier: 1373829
description:
epitope description:KCTSDQDEQFIPKGCSK
antigen name:Other Pseudomonas aeruginosa protein
host organism:Mus musculus BALB/c
antibody name:Fm16
aggregation:
instance of dataset
availability:
available
primaryPublications: 7525482
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1003825
landingPage: http://www.iedb.org/assay/1373829
type:
Literature
publicationVenue:
Infect Immun
dates:
1994
study type: b cell assays
subject species: Pseudomonas aeruginosa
fullName:
L Yu
K K Lee
R S Hodges
W Paranchych
R T Irvin
method:
antigen inhibition
name:
Adherence of Pseudomonas aeruginosa and Candida albicans to glycosphingolipid (Asialo-GM1) receptors is achieved by a conserved receptor-binding domain present on their adhesins.
description:
The epitope reduced binding of mAb Fm16 to C. albicans fimbriae by about 80%. The 7-mer peptide DEQFIPK, contained within the epitope, also inhibited binding at a higher concentration. The authors conclude that a conserved antigenic epitope present on C. albicans fimbriae is similar or identical to the epitope, in particular the sequence DEQFIPK, from the pilin molecule of P. aeruginosa PAK.

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