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Antigenic protein modifications in Ehrlichia
To develop effective vaccination strategies againstEhrlichia, we have previously reported developing an animal model of cross-protection in which C57BL/6 mice primed withE. muris were resistant to lethal infection withIxodes ovatus ehrlichia (IOE). Polyclonal antibody produced in mice after priming...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Blackwell Publishing Ltd
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2731653/ https://www.ncbi.nlm.nih.gov/pubmed/19493209 http://dx.doi.org/10.1111/j.1365-3024.2009.01099.x |
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author | THOMAS, S THIRUMALAPURA, N CROSSLEY, E C ISMAIL, N WALKER, D H |
author_facet | THOMAS, S THIRUMALAPURA, N CROSSLEY, E C ISMAIL, N WALKER, D H |
author_sort | THOMAS, S |
collection | PubMed |
description | To develop effective vaccination strategies againstEhrlichia, we have previously reported developing an animal model of cross-protection in which C57BL/6 mice primed withE. muris were resistant to lethal infection withIxodes ovatus ehrlichia (IOE). Polyclonal antibody produced in mice after priming withE. muris and later injected with IOE-detected antigenic proteins inE. muris and IOE cell lysates. Cross-reaction of antigenic proteins was observed when we probed both theE. muris and IOE cell lysates with IOE andE. muris-specific polyclonal antibody. Analysis of the total proteins ofE. muris and IOE by two dimensional electrophoresis showed that bothE. muris and IOE have the same antigenic proteins. Finally, studies on post-translational protein modifications using a novel technique, Eastern blotting, showed thatE. muris proteins are more lipoylated and glycosylated than those of IOE. |
format | Text |
id | pubmed-2731653 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Blackwell Publishing Ltd |
record_format | MEDLINE/PubMed |
spelling | pubmed-27316532010-06-01 Antigenic protein modifications in Ehrlichia THOMAS, S THIRUMALAPURA, N CROSSLEY, E C ISMAIL, N WALKER, D H Parasite Immunol Original Articles To develop effective vaccination strategies againstEhrlichia, we have previously reported developing an animal model of cross-protection in which C57BL/6 mice primed withE. muris were resistant to lethal infection withIxodes ovatus ehrlichia (IOE). Polyclonal antibody produced in mice after priming withE. muris and later injected with IOE-detected antigenic proteins inE. muris and IOE cell lysates. Cross-reaction of antigenic proteins was observed when we probed both theE. muris and IOE cell lysates with IOE andE. muris-specific polyclonal antibody. Analysis of the total proteins ofE. muris and IOE by two dimensional electrophoresis showed that bothE. muris and IOE have the same antigenic proteins. Finally, studies on post-translational protein modifications using a novel technique, Eastern blotting, showed thatE. muris proteins are more lipoylated and glycosylated than those of IOE. Blackwell Publishing Ltd 2009-06 /pmc/articles/PMC2731653/ /pubmed/19493209 http://dx.doi.org/10.1111/j.1365-3024.2009.01099.x Text en Journal compilation © 2009 Blackwell Publishing Ltd http://creativecommons.org/licenses/by/2.5/ Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation. |
spellingShingle | Original Articles THOMAS, S THIRUMALAPURA, N CROSSLEY, E C ISMAIL, N WALKER, D H Antigenic protein modifications in Ehrlichia |
title | Antigenic protein modifications in Ehrlichia |
title_full | Antigenic protein modifications in Ehrlichia |
title_fullStr | Antigenic protein modifications in Ehrlichia |
title_full_unstemmed | Antigenic protein modifications in Ehrlichia |
title_short | Antigenic protein modifications in Ehrlichia |
title_sort | antigenic protein modifications in ehrlichia |
topic | Original Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2731653/ https://www.ncbi.nlm.nih.gov/pubmed/19493209 http://dx.doi.org/10.1111/j.1365-3024.2009.01099.x |
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