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Analogous amino acid sequences in myelin proteolipid and viral proteins
Computer analysis of the intrinsic membrane protein, myelin proteolipid, shows strong sequence similarities between the putative extramembrane segments of the proteolipid protein and a number of viral proteins, several of which infect humans. These similarities are even more striking than those repo...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
1986
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130213/ https://www.ncbi.nlm.nih.gov/pubmed/2429866 http://dx.doi.org/10.1016/0014-5793(86)81502-2 |
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author | Shaw, Shyh-Yu Laursen, Richard A. Lees, Marjorie B. |
author_facet | Shaw, Shyh-Yu Laursen, Richard A. Lees, Marjorie B. |
author_sort | Shaw, Shyh-Yu |
collection | PubMed |
description | Computer analysis of the intrinsic membrane protein, myelin proteolipid, shows strong sequence similarities between the putative extramembrane segments of the proteolipid protein and a number of viral proteins, several of which infect humans. These similarities are even more striking than those reported previously between viral proteins and the encephalitogenic myelin basic protein (MBP). These findings, along with other reports of molecular mimicry by viruses, suggest that immunological cross‐reactions between virus‐induced antibodies or T‐cells and analogous antigenic determinants (epitopes) in myelin proteolipid could be involved in the pathophysiology of multiple sclerosis or post‐infectious demyelinating syndromes. |
format | Online Article Text |
id | pubmed-7130213 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1986 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71302132020-04-08 Analogous amino acid sequences in myelin proteolipid and viral proteins Shaw, Shyh-Yu Laursen, Richard A. Lees, Marjorie B. FEBS Lett Full‐length Articles Computer analysis of the intrinsic membrane protein, myelin proteolipid, shows strong sequence similarities between the putative extramembrane segments of the proteolipid protein and a number of viral proteins, several of which infect humans. These similarities are even more striking than those reported previously between viral proteins and the encephalitogenic myelin basic protein (MBP). These findings, along with other reports of molecular mimicry by viruses, suggest that immunological cross‐reactions between virus‐induced antibodies or T‐cells and analogous antigenic determinants (epitopes) in myelin proteolipid could be involved in the pathophysiology of multiple sclerosis or post‐infectious demyelinating syndromes. John Wiley and Sons Inc. 1986-10-27 2002-04-26 /pmc/articles/PMC7130213/ /pubmed/2429866 http://dx.doi.org/10.1016/0014-5793(86)81502-2 Text en FEBS Letters 207 (1986) 1873-3468 © 2015 Federation of European Biochemical Societies This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency. |
spellingShingle | Full‐length Articles Shaw, Shyh-Yu Laursen, Richard A. Lees, Marjorie B. Analogous amino acid sequences in myelin proteolipid and viral proteins |
title | Analogous amino acid sequences in myelin proteolipid and viral proteins |
title_full | Analogous amino acid sequences in myelin proteolipid and viral proteins |
title_fullStr | Analogous amino acid sequences in myelin proteolipid and viral proteins |
title_full_unstemmed | Analogous amino acid sequences in myelin proteolipid and viral proteins |
title_short | Analogous amino acid sequences in myelin proteolipid and viral proteins |
title_sort | analogous amino acid sequences in myelin proteolipid and viral proteins |
topic | Full‐length Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7130213/ https://www.ncbi.nlm.nih.gov/pubmed/2429866 http://dx.doi.org/10.1016/0014-5793(86)81502-2 |
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