Structure and antigenic activity of rubella E1 glycoprotein synthetic peptides

✍ Scribed by P. Neri; M. Corti; L. Lozzi; P. E. Valensin

• Publisher: Wiley (John Wiley & Sons)
• Year: 1991
• Tongue: English
• Weight: 318 KB
• Volume: 31
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360310607

✦ Synopsis

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.

In order to establish for each epitope the shortest sequence that was able to give the maximum binding with human antirubella immunoglobulins, synthetic peptides with increasing number of residues flanking these essential parts of rubella E1 glycoprotein epitopes were synthesized and examined for their antigenic activity.

Usually higher activity was observed with progressively longer homologues, whereas the additions of Pro‐271, Pro‐278 to ^272^GEVWVT^277^ peptide, and additions of Ala‐248 to ^249^TPERP^253^and ^249^TPERPR^254^, led to an abrupt decrease in binding. Taken together, our results indicated that the antigenic activity of the whole antigen could be dissected and reproduced using synthetic peptides of appropriate structure for each epitope.