Browse by author
Lookup NU author(s): Dr Alexei von Delwig, Dr Julie Musson, Dr Jeong-Jin Lee, Professor John Robinson
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
We demonstrated that an epitope from the recombinant protective antigen (rPA) of Bacillus anthracis was presented by mature major histocompatibility complex class II (MHC-II) molecules, whereas an epitope from the recombinant virulent (rV) antigen of Yersinia, pestis was presented by newly synthesized MHC-II. We addressed which endosomal compartments were involved in the antigen processing of each epitope. Bone-marrow-derived macrophages were subjected to subcellular fractionation; fractions were analysed for the expression of endosomal markers and used as a source of enzyme activity for the processing of rPA and rV antigens. The rPA epitope was productively processed by dense lysosomal fractions and light membrane fractions expressing early endosomal markers Rab5 and early endosomal antigen-1 as well as markers of antigen-presenting compartments (MHC-II, DM, DO and Ii chain). In contrast, the rV epitope was productively processed only by dense fractions with lysosomal activity. No productive antigen-processing activity was associated with fractions of intermediate density expressing Rab7 and Rab9, characteristic of late endosomes. The data suggest that endosomal compartments expressing Rab5 guanosine triphosphatase can productively process protein antigens for presentation by mature MHC class II molecules. © 2005 Blackwell Publishing Ltd.
Author(s): Von Delwig A, Musson JA, Shim H-K, Lee JJ, Walker N, Harding CV, Williamson ED, Robinson JH
Publication type: Article
Publication status: Published
Journal: Scandinavian Journal of Immunology
Year: 2005
Volume: 62
Issue: 3
Pages: 243-250
Print publication date: 01/09/2005
ISSN (print): 0300-9475
ISSN (electronic): 1365-3083
Publisher: Wiley-Blackwell Publishing Ltd.
URL: http://dx.doi.org/10.1111/j.1365-3083.2005.01664.x
DOI: 10.1111/j.1365-3083.2005.01664.x
PubMed id: 16179011
Altmetrics provided by Altmetric