Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells
Abstract This study reports an identification of the major processing products of an exogenous protein antigen, viz. sperm‐whale myoglobin, as obtained after cell‐free processing with partially purified macrophage endosomes. It is demonstrated that such a system yields fragments that are indistingui...
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crwiley:10.1002/eji.1830210904 2024-06-02T08:14:52+00:00 Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells Van Noort, Johannes M. Boon, Jacqueline Van der Drift, Alfons C. M. Wagenaar, Josée P. A. Boots, Annemieke M. H. Boog, Claire J. P. 1991 http://dx.doi.org/10.1002/eji.1830210904 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Feji.1830210904 https://onlinelibrary.wiley.com/doi/pdf/10.1002/eji.1830210904 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor European Journal of Immunology volume 21, issue 9, page 1989-1996 ISSN 0014-2980 1521-4141 journal-article 1991 crwiley https://doi.org/10.1002/eji.1830210904 2024-05-03T11:08:24Z Abstract This study reports an identification of the major processing products of an exogenous protein antigen, viz. sperm‐whale myoglobin, as obtained after cell‐free processing with partially purified macrophage endosomes. It is demonstrated that such a system yields fragments that are indistinguishable by high performance liquid chromatography analysis from those generated after uptake of myoglobin inside live macrophages. The concerted action of the endosomal proteases cathepsin D and cathepsin B can account for nearly all cleavages observed. Cathepsin D appears to be mainly responsible for the initial cleavage of myoglobin, while cathepsin B catalyzes the C‐terminal trimming of initially released fragments. The fragments released by cathepsin D contain most, if not all, major epitopes for murine myoglobin‐specific helper T cells. Interestingly, each known T cell epitope of myoglobin is located at the very N terminus of a different myoglobin fragment released upon processing. In order to explain this correspondence, noted also in several other protein antigens, a structural relationship is proposed between antigen processing by cathepsin D and antigen recognition by major histocompatibility complex (MHC) class II products. As is demonstrated here, this relationship may be used as a predictive tool for the identification of MHC‐binding sequences as well as of T cell epitopes in their naturally occurring form. Article in Journal/Newspaper Sperm whale Wiley Online Library European Journal of Immunology 21 9 1989 1996 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract This study reports an identification of the major processing products of an exogenous protein antigen, viz. sperm‐whale myoglobin, as obtained after cell‐free processing with partially purified macrophage endosomes. It is demonstrated that such a system yields fragments that are indistinguishable by high performance liquid chromatography analysis from those generated after uptake of myoglobin inside live macrophages. The concerted action of the endosomal proteases cathepsin D and cathepsin B can account for nearly all cleavages observed. Cathepsin D appears to be mainly responsible for the initial cleavage of myoglobin, while cathepsin B catalyzes the C‐terminal trimming of initially released fragments. The fragments released by cathepsin D contain most, if not all, major epitopes for murine myoglobin‐specific helper T cells. Interestingly, each known T cell epitope of myoglobin is located at the very N terminus of a different myoglobin fragment released upon processing. In order to explain this correspondence, noted also in several other protein antigens, a structural relationship is proposed between antigen processing by cathepsin D and antigen recognition by major histocompatibility complex (MHC) class II products. As is demonstrated here, this relationship may be used as a predictive tool for the identification of MHC‐binding sequences as well as of T cell epitopes in their naturally occurring form. |
format |
Article in Journal/Newspaper |
author |
Van Noort, Johannes M. Boon, Jacqueline Van der Drift, Alfons C. M. Wagenaar, Josée P. A. Boots, Annemieke M. H. Boog, Claire J. P. |
spellingShingle |
Van Noort, Johannes M. Boon, Jacqueline Van der Drift, Alfons C. M. Wagenaar, Josée P. A. Boots, Annemieke M. H. Boog, Claire J. P. Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells |
author_facet |
Van Noort, Johannes M. Boon, Jacqueline Van der Drift, Alfons C. M. Wagenaar, Josée P. A. Boots, Annemieke M. H. Boog, Claire J. P. |
author_sort |
Van Noort, Johannes M. |
title |
Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells |
title_short |
Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells |
title_full |
Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells |
title_fullStr |
Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells |
title_full_unstemmed |
Antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by T cells |
title_sort |
antigen processing by endosomal proteases determines which sites of sperm‐whale myoglobin are eventually recognized by t cells |
publisher |
Wiley |
publishDate |
1991 |
url |
http://dx.doi.org/10.1002/eji.1830210904 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Feji.1830210904 https://onlinelibrary.wiley.com/doi/pdf/10.1002/eji.1830210904 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
European Journal of Immunology volume 21, issue 9, page 1989-1996 ISSN 0014-2980 1521-4141 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/eji.1830210904 |
container_title |
European Journal of Immunology |
container_volume |
21 |
container_issue |
9 |
container_start_page |
1989 |
op_container_end_page |
1996 |
_version_ |
1800738872066310144 |