| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1006678 |
| landingPage: |
http://www.iedb.org/assay/1472687 |
| type: |
Literature
|
| publicationVenue: |
Protein Eng
|
| dates: |
2003
|
| study type: | b cell assays |
| subject species: |
| fullName: |
Tuomas Heiskanen
Xiao-Dong Li
Jussi Hepojoki
Elisabeth Gustafsson
Ake Lundkvist
Antti Vaheri
Hilkka Lankinen
|
| method: |
western blot
|
| name: |
Improvement of binding of Puumala virus neutralization site resembling peptide with a second-generation phage library.
|
| description: |
The epitope is a deduced minimal binding unit from from a phage display library. The larger mimotope from which it is derived defines a conformational epitope formed by the combined surfaces of the G1 and G2 glycoproteins of Puumala virus, and has similarities to residues 931-934 in G2.
Alanine scanning showed that mutation of the amino acids Cys3, Asp4, Gly8, Tyr9, Glu11, Arg12, Gly13, Ile14, Pro15, and Pro17 in the cc5 peptide fragment (FTCDRLSGYWERGIPLPCG) decreased or eliminated binding to mAb 1C9. Selective mutation of individual amino acids was also used in these assays to show that mutation of Trp to Tyr at amino acid position 10 in the cc5 peptide fragment dramatically increased binding to mAb 1C9. Overlapping peptides from the cc5 fragment were used to define a minimal reactive epitope by immunoblot.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |