These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Two Listeria monocytogenes CTL epitopes are processed from the same antigen with different efficiencies.
    Author: Sijts AJ, Neisig A, Neefjes J, Pamer EG.
    Journal: J Immunol; 1996 Jan 15; 156(2):683-92. PubMed ID: 8543821.
    Abstract:
    Listeria monocytogenes is an intracellular bacterium that elicits MHC class I-restricted CTL in infected mice. A major CTL specificity is the nonamer peptide p60 217-225, which is derived from the bacterial murein hydrolase p60 and presented by the H-2Kd MHC class I molecule. In this report, we identify a second H-2Kd presented peptide, encompassing residues 449-457 of p60, that is detected by L. monocytogenes-specific CTL. Both p60-derived CTL epitopes are good competitors for H-2Kd binding and TAP (transporter associated with Ag processing) transport. CTL clone WP11.12 lyses L. monocytogenes infected cells and recognizes naturally processed p60 449-457 acid eluted from L. monocytogenes-infected macrophages. Although both epitopes derive from the same Ag and bind the same allelic form of MHC class I, quantitative analysis reveals that the amount of p60 449-457 in infected cells is approximately 10-fold greater than the amount of p60 217-225. Shuffling p60 217-225 into position 449-457 decreases its processing efficiency, indicating that the large number of p60 449-457 epitopes cannot be entirely attributed to epitope-flanking sequences. Our findings indicate that CTL epitopes can be processed from Ags with markedly different kinetics and efficiencies. Intrinsic qualities of an epitope and its location within a protein influence the efficiency of Ag processing.
    [Abstract] [Full Text] [Related] [New Search]