Abstract:
:Mice infected with Listeria monocytogenes (LM) generate protective CD8 cells of varying specificity. One subset, unlike conventional LM-immune CD8 cells, can respond to antigen-presenting cells (APC) treated with heat-killed LM (HKLM). These cells proved to have surprisingly uniform specificity, recognizing a product we designated HKLM-associated antigen (HAA) presented by the non-classical class Ib product H2-M3wt. HAA proved to be extremely hydrophobic and the bioactive portion of the molecule was highly protease-resistant, leading us initially to speculate that it might be a non-peptide. Recent studies, however, identify HAA as a complex containing lemA, a listerial protein bearing the immunogenic amino terminal peptide sequence fMIGWII, tightly associated with bacterial cardiolipin. A variety of cell types can process and present exogenous HAA/lemA, and the phospholipid component appears essential for this processing. Endosomal acidification and proteolysis are required for processing, but the site where antigen binds to H2-M3wt within APC remains uncertain. HAA/lemA-immune effectors are unusually cross-reactive. We could readily detect H2-M3wt-restricted responses to APC incubated with unrelated N-formylated peptides, and bacteria. HAA-like products represent an intriguing new set of bacterial antigens recognizable by immune CD8 cells.
journal_name
Immunol Revjournal_title
Immunological reviewsauthors
Kurlander R,Nataraj Cdoi
10.1111/j.1600-065x.1997.tb00998.xsubject
Has Abstractpub_date
1997-08-01 00:00:00pages
123-8eissn
0105-2896issn
1600-065Xjournal_volume
158pub_type
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