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Brefeldin A implicates egress from endoplasmic reticulum in class I restricted antigen presentation
J G Nuchtern1, J S Bonifacino, W E Biddison
1Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, Maryland 20892.
Nature
|May 18, 1989
Summary
Brefeldin A (BFA) blocks protein transport from the endoplasmic reticulum (ER). This study shows BFA treatment halts the cell
Area of Science:
- Immunology
- Cell Biology
Background:
- Antigen presentation requires intracellular processing and association with MHC molecules.
- Class I restricted antigens originate from intracellular proteins, including cytosolic and viral proteins.
- The precise mechanism of processed antigen translocation into the secretory pathway for MHC class I binding remains unclear.
Purpose of the Study:
- To investigate the role of the endoplasmic reticulum (ER) in the presentation of endogenous antigens.
- To determine if pharmacologically blocking ER export affects antigen presentation.
Main Methods:
- Utilized Brefeldin A (BFA), a fungal antibiotic known to inhibit ER protein export.
- Assessed the presentation of endogenously synthesized antigens to class I restricted cytotoxic T cells following BFA treatment.
Main Results:
- Brefeldin A (BFA) completely abolished the presentation of endogenously synthesized antigens.
- This indicates that the transport of proteins out of the ER is critical for MHC class I antigen presentation.
Conclusions:
- The endoplasmic reticulum (ER) is a crucial site for the processing and presentation of endogenous antigens via MHC class I molecules.
- Inhibition of ER export effectively blocks the presentation of intracellular antigens to T cells.