ANTIGENIC AND IMMUNOGENIC MIMICRY OF THE HER2/NEU ONCOPROTEIN BY PHAGE-DISPLAYED PEPTIDES

作者：ORLANDI R^*; MENARD S; COLNAGHI MI; BOYER CM; FELICI F

来源：European Journal of Immunology, 1994, 24(11): 2868-2873.

DOI：10.1002/eji.1830241143

• PEPTIDE MIMICS
• EPITOPE LIBRARIES
• HER2
• NEU
• FILAMENTOUS PHAGE
• TUMOR

To recover peptides that antigenically and immunogenically mimic the p185(HER2) oncoprotein, we selected the phage-peptide libraries pVIII-9aa and pVIII-9aa. Cys using murine monoclonal antibodies (mAb) MGr2 and MGr6, directed against two distinct epitopes of the p185(HER2) extracellular domain. Phage-displayed peptides containing consensus amino acid motifs were recovered and shown to compete specifically for mAb binding on tumor cells that overexpress p185(HER2). The deduced amino acid sequence of the peptides suggests that both epitopes defined by the mAb on p185(HER2) are discontinuous and that hydrophobic interactions are involved in binding with the mAb. A phage clone displaying the GPLDSLFAQ peptide elicited a specific immune response against the p185(HER2) in BALB/c mice, demonstrating that this phage-displayed peptide represents an immunological equivalent of the MGr2 epitope on p185(HER2) and might be used as a substitute for this oncoprotein in in vitro and in vivo immunological studies.

• 出版日期1994-11