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By using as a model the breast\/prostate cancer\u2010associated HER\u20102\/<jats:italic>neu<\/jats:italic>antigen, we analyzed the monoclonal and polyclonal humoral immune responses against HER\u20102\/<jats:italic>neu<\/jats:italic>peptide motifs not shared with the host proteome. We show here that<jats:italic>(i)<\/jats:italic>a mouse monoclonal antibody (MAb) raised against the extracellular domain (EC) of human HER\u20102\/neu oncoprotein recognized a linear peptide motif endowed with low similarity level to the mouse proteome;<jats:italic>(ii)<\/jats:italic>likewise, human sera from breast\/prostate cancer patients preferentially recognized peptide fragments from the EC of the HER\u20102\/<jats:italic>neu<\/jats:italic>oncoprotein having sequences that are not present in the human proteome. Together with previous results obtained in other disease models (cervical cancer\u2010associated HPV16 E7 oncoprotein and<jats:italic>Pemphigus vulgaris<\/jats:italic>auto\u2010antigen desmoglein\u20103), the present data suggest that a low level of sequence similarity to the host's proteome might be an important factor in shaping the pool of B cell epitopes. \u00a9 2002 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/ijc.10259","type":"journal-article","created":{"date-parts":[[2002,8,25]],"date-time":"2002-08-25T23:13:41Z","timestamp":1030317221000},"page":"741-747","source":"Crossref","is-referenced-by-count":26,"title":["Monoclonal and polyclonal humoral immune response to EC HER\u20102\/<i><scp>NEU<\/scp><\/i>peptides with low similarity to the host's 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