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Structure of rubella E1 glycoprotein epitopes established by multiple peptide synthesis

โœ Scribed by L. Lozzi; M. Rustici; M. Corti; M. G. Cusi; P. E. Valensin; L. Bracci; A. Santucci; P. Soldani; A. Spreafico; P. Neri


Publisher
Springer Vienna
Year
1990
Tongue
English
Weight
376 KB
Volume
110
Category
Article
ISSN
1432-8798

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๐Ÿ“œ SIMILAR VOLUMES


Structure and antigenic activity of rube
โœ P. Neri; M. Corti; L. Lozzi; P. E. Valensin ๐Ÿ“‚ Article ๐Ÿ“… 1991 ๐Ÿ› Wiley (John Wiley & Sons) ๐ŸŒ English โš– 318 KB

## Abstract Minimal sequences of rubella E1 glycoprotein epitopes were previously identified as the tripeptide ^250^PER^252^ for the EP~2~ epitope, the tetrapeptide ^260^ADDP^263^ for the EP~3~ epitope, and the tripeptide ^273^EVW^275^ plus the octapeptide ^278^PVIGSQAR^285^ for the EP~1~ epitope.

Mapping T-cell epitopes of rubella virus
โœ Dawei Ou; Pele Chong; Aubrey J. Tingle; Shirley Gillam ๐Ÿ“‚ Article ๐Ÿ“… 1993 ๐Ÿ› John Wiley and Sons ๐ŸŒ English โš– 985 KB

## Abstract To design a safe and effective synthetic peptide vaccine against rubell virus (RV) infection, it is necessary to identify immunodominant Tโ€cell epitopes of RV structural proteins. To define such epitopes, 49 overlapping synthetic peptides (17โ€“34 residues in length) corresponding to more