TY - JOUR
T1 - H2-M3wt-restricted, Listeria monocytogenes-specific CD8 T cells recognize a novel, hydrophobic, protease-resistant, periodate-sensitive antigen
AU - Nataraj, Chandrasekaran
AU - Brown, Melinda L.
AU - Poston, Rebecca M.
AU - Shawar, Said M.
AU - Rich, Robert R.
AU - Lindahl, Kirsten Fischer
AU - Kurlander, Roger J.
N1 - Funding Information:
We wish to thank Nilabh Shastri for providing us with BW5147 cells for these studies, Franz Fiedler for his advice and material assistance in providing LM-derived lipoteichoic acid; Nicolas Kredich for technical and scientific advice and assistance; and Wendy Liu for technical assistance These studies were supported by NIH grant RO1 -Al 18073.
PY - 1996
Y1 - 1996
N2 - Mice infected with Listeria monocytogenes (LM) generate H2-M3wt-restricted CD8 effectors which recognize a heat-killed LM-associated antigen (HAA) presented by macrophages. To characterize HAA, we extracted a bioactive component from LM using SDS or NaOH. Extracted HAA aggregated in hydrophilic solvents but dissociated in the presence of SDS into a smaller subunit which migrated in Sephadex G-200 between chymotrypsinogen (25 kDa) and cytochrome c (12.5 kDa). HAA bioactivity and size was unaffected by proteinase K under conditions which degraded virtually all detectable protein. HAA was also unaffected by other proteases, RNase and DNase, but HAA bioactivity was destroyed by periodate, an agent that degrades carbohydrates. These studies demonstrate that H2-M3wt can present a hydrophobic, non-peptide, microbial antigen, probably glycolipid in origin, to CD8 T cells.
AB - Mice infected with Listeria monocytogenes (LM) generate H2-M3wt-restricted CD8 effectors which recognize a heat-killed LM-associated antigen (HAA) presented by macrophages. To characterize HAA, we extracted a bioactive component from LM using SDS or NaOH. Extracted HAA aggregated in hydrophilic solvents but dissociated in the presence of SDS into a smaller subunit which migrated in Sephadex G-200 between chymotrypsinogen (25 kDa) and cytochrome c (12.5 kDa). HAA bioactivity and size was unaffected by proteinase K under conditions which degraded virtually all detectable protein. HAA was also unaffected by other proteases, RNase and DNase, but HAA bioactivity was destroyed by periodate, an agent that degrades carbohydrates. These studies demonstrate that H2-M3wt can present a hydrophobic, non-peptide, microbial antigen, probably glycolipid in origin, to CD8 T cells.
KW - Antigen presentation
KW - Antigen processing
KW - Antigen-presenting cells
KW - MHC class I products
KW - Macrophage
KW - T cells
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U2 - 10.1093/intimm/8.3.367
DO - 10.1093/intimm/8.3.367
M3 - Article
C2 - 8671623
AN - SCOPUS:0029670930
SN - 0953-8178
VL - 8
SP - 367
EP - 378
JO - International Immunology
JF - International Immunology
IS - 3
ER -