Extracellular processing of peptide antigens that bind class I major histocompatibility molecules

doi:10.1084/jem.175.5.1221

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Extracellular processing of peptide antigens that bind class I major histocompatibility molecules

LA Sherman, TA Burke and JA Biggs
Department of Immunology, Scripps Research Institute, La Jolla, California 92037.

One problem associated with the use of synthetic peptides as antigens in vivo is their susceptibility to inactivation by proteolytic degradation. A situation is described in which a serum protease, angiotensin-converting enzyme (ACE), is actually responsible for the class I binding activity of a commonly used influenza antigen, nucleoprotein (NP)(147-158R-). This peptide has been reported to be a highly efficient class I antigen. Evidence is presented that demonstrates that the peptide is inactive until cleaved by ACE, which is a normal constituent of serum. The enzyme removes a COOH-terminal dipeptide resulting in the sequence NP(147-155), which is identical to the naturally processed peptide. Such extracellular processing of peptides and proteins may occur for a variety of antigens both in vitro and in vivo, and could have important implications for the design of proteolytically resistant vaccines.
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