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

Authors
  • Sherman, L A1
  • Burke, T A
  • Biggs, J A
  • 1 Department of Immunology, Scripps Research Institute, La Jolla, California 92037.
Type
Published Article
Journal
The Journal of experimental medicine
Publication Date
May 01, 1992
Volume
175
Issue
5
Pages
1221–1226
Identifiers
PMID: 1314884
Source
Medline
License
Unknown

Abstract

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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