Recognition of peptidyl epitopes by polymorphic epithelial mucin (PEM)- specific monoclonal antibodies

A. S. Dion, N. I. Smorodinsky, C. J. Williams, D. H. Wreschner, P. P. Major, I. Keydar

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12 Scopus citations


Peptidyl epitope recognition by several murine monoclonal antibodies (MAbs E29, H23, HMFG-1, HMFG-2, MA5, MA6 and MA9) which react with the polymorphic epithelial mucins [PEM; epithelial membrane antigen (EMA)] was studied by using ten synthetic peptides representative of the 20 residue tandem repeat as test antigens. Antibody binding to 6-10 residue overlaps and to peptides having a common carboxy-terminus and staggered amino-termini (8-31 residues) was assessed by solid phase and competition ELISA techniques. From these analyses, all MAbs except MA9 were found to react predominantly with the carboxy-terminal half of the repeat motif. Polyclonal antibody responses in mice immunized with intact EMA/PEM-containing preparations also displayed significant reactivities against synthetic repeat peptide antigens and, conversely, synthetic peptides as carrier-conjugated immunogens induced antibodies recognizing intact antigens. These results are discussed vis-a-vis peptide conformation, the potential effects of O-glycosylation on secondary structure, and the possible effects of these parameters on immunogenicity and antigenicity.

Original languageEnglish (US)
Pages (from-to)595-610
Number of pages16
Issue number5
StatePublished - 1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Immunology
  • Genetics


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