Characterization of the antigenic structure of human type II collagen

Christopher J. Krco, Jeff Pawelski, Jerry Harders, Daniel McCormick, Marie Griffiths, Harvindar S. Luthra, Chella S. David

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


A series of 101 peptides each 20 amino acids in length (10-residue overlap) spanning the helical portion of the mature α-chain of human type II collagen (CII) was synthesized. DBA/1 (H-2q) mice were immunized with individual peptides, and draining lymph node cells were challenged in vitro. Strong responses were measured to three peptides: peptide I (residues 74-93), peptide 14 (residues 254-273), and peptide 81 (residues 924-943), B10.Q (H-2q) mice were responsive to peptides I and 81 but not to peptide 14. B10.RIII (H-2r) mice, which are resistant to arthritis induction following immunization with human CII, were unresponsive to peptides I, 14, and 81. Using single amino acid truncated peptides, we determined minimal immunostimulatory lengths for peptides I and 81. Residues critical to antigenicity were identified by introducing alanine and glycine substitutions into minimal length immunostimuiatory peptides. The determinants within peptides I and 81 are 100% homologous to mouse CU and are autoantigens. Peptide 81 has homology to viral proteins. Peptide 14 is 90% homologous to mouse CII and has homology to heat shock proteins.

Original languageEnglish (US)
Pages (from-to)2761-2768
Number of pages8
JournalJournal of Immunology
Issue number8
StatePublished - Apr 15 1996

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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