Minimal sequences of rubella E1 glycoprotein epitopes were previously identified as the tripeptide 250PER252 for the EP2 epitope, the tetrapeptide 260ADDP263 for the EP3 epitope, and the tripeptide 273EVW275 plus the octapeptide 278PVIGSQAR285 for the EP1 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 272GEVWVT277 peptide, and additions of Ala‐248 to 249TPERP253and 249TPERPR254, 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.

P., N., M., C., Lozzi, L., & P. E., V. (1991). Structure and antigenic activity of rubella E1 glycoprotein synthetic peptides. BIOPOLYMERS, 31(6), 631-635 [10.1002/bip.360310607].

Structure and antigenic activity of rubella E1 glycoprotein synthetic peptides

LOZZI, LUISA;
1991

Abstract

Minimal sequences of rubella E1 glycoprotein epitopes were previously identified as the tripeptide 250PER252 for the EP2 epitope, the tetrapeptide 260ADDP263 for the EP3 epitope, and the tripeptide 273EVW275 plus the octapeptide 278PVIGSQAR285 for the EP1 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 272GEVWVT277 peptide, and additions of Ala‐248 to 249TPERP253and 249TPERPR254, 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.
P., N., M., C., Lozzi, L., & P. E., V. (1991). Structure and antigenic activity of rubella E1 glycoprotein synthetic peptides. BIOPOLYMERS, 31(6), 631-635 [10.1002/bip.360310607].
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11365/409832