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Proteolytic processing is required for viral superantigen activity
The mouse mammary tumor virus-7 superantigen (vSAG7) is proteolytically processed in B cells at as many as three positions. Proteolytic processing appears to be important for superantigen activity because a processed form of vSAG7 was predominant among those forms that were found to bind to major hi...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1995
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192000/ https://www.ncbi.nlm.nih.gov/pubmed/7722465 |
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collection | PubMed |
description | The mouse mammary tumor virus-7 superantigen (vSAG7) is proteolytically processed in B cells at as many as three positions. Proteolytic processing appears to be important for superantigen activity because a processed form of vSAG7 was predominant among those forms that were found to bind to major histocompatibility complex class II molecules. To determine the functional significance of proteolytic processing, a mutation was introduced in vSAG7 at one of the sites where proteolytic cleavage is thought to take place in B cells. Elimination of the putative processing site at position 171 abrogated detectable vSAG7 surface expression in B cells, indicating that proteolytic processing is required for vSAG7 function. Coexpression in insect cells of vSAG7 and furin, a proprotein-processing enzyme, also demonstrated that furin could process vSAG7 at position 171. |
format | Text |
id | pubmed-2192000 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1995 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21920002008-04-16 Proteolytic processing is required for viral superantigen activity J Exp Med Articles The mouse mammary tumor virus-7 superantigen (vSAG7) is proteolytically processed in B cells at as many as three positions. Proteolytic processing appears to be important for superantigen activity because a processed form of vSAG7 was predominant among those forms that were found to bind to major histocompatibility complex class II molecules. To determine the functional significance of proteolytic processing, a mutation was introduced in vSAG7 at one of the sites where proteolytic cleavage is thought to take place in B cells. Elimination of the putative processing site at position 171 abrogated detectable vSAG7 surface expression in B cells, indicating that proteolytic processing is required for vSAG7 function. Coexpression in insect cells of vSAG7 and furin, a proprotein-processing enzyme, also demonstrated that furin could process vSAG7 at position 171. The Rockefeller University Press 1995-05-01 /pmc/articles/PMC2192000/ /pubmed/7722465 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Proteolytic processing is required for viral superantigen activity |
title | Proteolytic processing is required for viral superantigen activity |
title_full | Proteolytic processing is required for viral superantigen activity |
title_fullStr | Proteolytic processing is required for viral superantigen activity |
title_full_unstemmed | Proteolytic processing is required for viral superantigen activity |
title_short | Proteolytic processing is required for viral superantigen activity |
title_sort | proteolytic processing is required for viral superantigen activity |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2192000/ https://www.ncbi.nlm.nih.gov/pubmed/7722465 |