Structural and Immunogenic Properties of a Major Antigenic Determinant in Neutral Salt‐Extracted Rat‐Skin Collagen

Authors:
  • HFHeinz Furthmayr
    Heinz Furthmayr
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Abstract
The major antigenic determinant of neutral salt‐extracted rat‐skin collagen is located in the C‐terminal CNBr peptide α1‐CB6b of the α1‐chain. This peptide is shortened by 20 amino acid residues from its C‐terminal nonhelical end if compared with α1‐CB6 obtained from collagen α1‐chains extracted under denaturating conditions. As reported earlier, degradation by tissue proteases during extraction was assumed as the main reason for the observed reduction in size.The C‐terminal sequence of α1‐CB6b was determined as Tyr‐Asp and was found to be essential for antigenic activity. Proportional loss of binding to antibodies with decrease in size was observed for appropriate proteolytic fragments derived from α1‐CB6b. Since this peptide extends only five amino acid residues beyond the helical collagen sequence, an important contribution of the conformational structure for this antigenic determinant is suggested. Decrease in ability to induce high antibody titers to α1‐CB6b was already observed at a higher structural level, e.g. after denaturation of triple‐helical collagen to random‐coiled α‐chains. The same result could be obtained if adjuvant was omitted in the priming injection.

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