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Surface-Exposed Proteins ofEhrlichia chaffeensis
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Zeitschriftentitel: | Infection and Immunity |
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Personen und Körperschaften: | , |
In: | Infection and Immunity, 75, 2007, 8, S. 3833-3841 |
Format: | E-Article |
Sprache: | Englisch |
veröffentlicht: |
American Society for Microbiology
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Schlagwörter: |
author_facet |
Ge, Yan Rikihisa, Yasuko Ge, Yan Rikihisa, Yasuko |
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author |
Ge, Yan Rikihisa, Yasuko |
spellingShingle |
Ge, Yan Rikihisa, Yasuko Infection and Immunity Surface-Exposed Proteins ofEhrlichia chaffeensis Infectious Diseases Immunology Microbiology Parasitology |
author_sort |
ge, yan |
spelling |
Ge, Yan Rikihisa, Yasuko 0019-9567 1098-5522 American Society for Microbiology Infectious Diseases Immunology Microbiology Parasitology http://dx.doi.org/10.1128/iai.00188-07 <jats:title>ABSTRACT</jats:title><jats:p>The surface proteins of<jats:italic>Ehrlichia chaffeensis</jats:italic>provide an important interface for pathogen-host interactions. To investigate the surface proteins of<jats:italic>E. chaffeensis</jats:italic>, membrane-impermeable, cleavable Sulfo-NHS-SS-Biotin was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin-agarose affinity purification. The affinity-captured proteins were separated by electrophoresis, and five relatively abundant protein bands containing immunoreactive proteins were subjected to capillary-liquid chromatography-nanospray tandem mass spectrometry analysis. Nineteen out of 22 OMP-1/P28 family proteins, including P28 (which previously was shown to be surface exposed), were detected in<jats:italic>E. chaffeensis</jats:italic>cultured in human monocytic leukemia THP-1 cells. For the first time, with the exception of P28 and P28-1, 17 OMP-1/P28 family proteins were demonstrated to be expressed at the protein level. The surface exposure of OMP-1A and OMP-1N was verified by immunofluorescence microscopy. OMP-1B was undetectable either by surface biotinylation or by Western blotting of the whole bacterial lysate, suggesting that it is not expressed by<jats:italic>E. chaffeensis</jats:italic>cultured in THP-1 cells. Additional<jats:italic>E. chaffeensis</jats:italic>surface proteins detected were OMP85, hypothetical protein ECH_0525 (here named Esp73), immunodominant surface protein gp47, and 11 other proteins. The identification of<jats:italic>E. chaffeensis</jats:italic>surface-exposed proteins provides novel insights into the<jats:italic>E. chaffeensis</jats:italic>surface and lays the foundation for rational studies on pathogen-host interactions and vaccine development.</jats:p> Surface-Exposed Proteins of<i>Ehrlichia chaffeensis</i> Infection and Immunity |
doi_str_mv |
10.1128/iai.00188-07 |
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Medizin Biologie |
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American Society for Microbiology, 2007 |
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American Society for Microbiology, 2007 |
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2007 |
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American Society for Microbiology |
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Infection and Immunity |
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49 |
title |
Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_unstemmed |
Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_full |
Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_fullStr |
Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_full_unstemmed |
Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_short |
Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_sort |
surface-exposed proteins of<i>ehrlichia chaffeensis</i> |
topic |
Infectious Diseases Immunology Microbiology Parasitology |
url |
http://dx.doi.org/10.1128/iai.00188-07 |
publishDate |
2007 |
physical |
3833-3841 |
description |
<jats:title>ABSTRACT</jats:title><jats:p>The surface proteins of<jats:italic>Ehrlichia chaffeensis</jats:italic>provide an important interface for pathogen-host interactions. To investigate the surface proteins of<jats:italic>E. chaffeensis</jats:italic>, membrane-impermeable, cleavable Sulfo-NHS-SS-Biotin was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin-agarose affinity purification. The affinity-captured proteins were separated by electrophoresis, and five relatively abundant protein bands containing immunoreactive proteins were subjected to capillary-liquid chromatography-nanospray tandem mass spectrometry analysis. Nineteen out of 22 OMP-1/P28 family proteins, including P28 (which previously was shown to be surface exposed), were detected in<jats:italic>E. chaffeensis</jats:italic>cultured in human monocytic leukemia THP-1 cells. For the first time, with the exception of P28 and P28-1, 17 OMP-1/P28 family proteins were demonstrated to be expressed at the protein level. The surface exposure of OMP-1A and OMP-1N was verified by immunofluorescence microscopy. OMP-1B was undetectable either by surface biotinylation or by Western blotting of the whole bacterial lysate, suggesting that it is not expressed by<jats:italic>E. chaffeensis</jats:italic>cultured in THP-1 cells. Additional<jats:italic>E. chaffeensis</jats:italic>surface proteins detected were OMP85, hypothetical protein ECH_0525 (here named Esp73), immunodominant surface protein gp47, and 11 other proteins. The identification of<jats:italic>E. chaffeensis</jats:italic>surface-exposed proteins provides novel insights into the<jats:italic>E. chaffeensis</jats:italic>surface and lays the foundation for rational studies on pathogen-host interactions and vaccine development.</jats:p> |
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author | Ge, Yan, Rikihisa, Yasuko |
author_facet | Ge, Yan, Rikihisa, Yasuko, Ge, Yan, Rikihisa, Yasuko |
author_sort | ge, yan |
container_issue | 8 |
container_start_page | 3833 |
container_title | Infection and Immunity |
container_volume | 75 |
description | <jats:title>ABSTRACT</jats:title><jats:p>The surface proteins of<jats:italic>Ehrlichia chaffeensis</jats:italic>provide an important interface for pathogen-host interactions. To investigate the surface proteins of<jats:italic>E. chaffeensis</jats:italic>, membrane-impermeable, cleavable Sulfo-NHS-SS-Biotin was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin-agarose affinity purification. The affinity-captured proteins were separated by electrophoresis, and five relatively abundant protein bands containing immunoreactive proteins were subjected to capillary-liquid chromatography-nanospray tandem mass spectrometry analysis. Nineteen out of 22 OMP-1/P28 family proteins, including P28 (which previously was shown to be surface exposed), were detected in<jats:italic>E. chaffeensis</jats:italic>cultured in human monocytic leukemia THP-1 cells. For the first time, with the exception of P28 and P28-1, 17 OMP-1/P28 family proteins were demonstrated to be expressed at the protein level. The surface exposure of OMP-1A and OMP-1N was verified by immunofluorescence microscopy. OMP-1B was undetectable either by surface biotinylation or by Western blotting of the whole bacterial lysate, suggesting that it is not expressed by<jats:italic>E. chaffeensis</jats:italic>cultured in THP-1 cells. Additional<jats:italic>E. chaffeensis</jats:italic>surface proteins detected were OMP85, hypothetical protein ECH_0525 (here named Esp73), immunodominant surface protein gp47, and 11 other proteins. The identification of<jats:italic>E. chaffeensis</jats:italic>surface-exposed proteins provides novel insights into the<jats:italic>E. chaffeensis</jats:italic>surface and lays the foundation for rational studies on pathogen-host interactions and vaccine development.</jats:p> |
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spelling | Ge, Yan Rikihisa, Yasuko 0019-9567 1098-5522 American Society for Microbiology Infectious Diseases Immunology Microbiology Parasitology http://dx.doi.org/10.1128/iai.00188-07 <jats:title>ABSTRACT</jats:title><jats:p>The surface proteins of<jats:italic>Ehrlichia chaffeensis</jats:italic>provide an important interface for pathogen-host interactions. To investigate the surface proteins of<jats:italic>E. chaffeensis</jats:italic>, membrane-impermeable, cleavable Sulfo-NHS-SS-Biotin was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin-agarose affinity purification. The affinity-captured proteins were separated by electrophoresis, and five relatively abundant protein bands containing immunoreactive proteins were subjected to capillary-liquid chromatography-nanospray tandem mass spectrometry analysis. Nineteen out of 22 OMP-1/P28 family proteins, including P28 (which previously was shown to be surface exposed), were detected in<jats:italic>E. chaffeensis</jats:italic>cultured in human monocytic leukemia THP-1 cells. For the first time, with the exception of P28 and P28-1, 17 OMP-1/P28 family proteins were demonstrated to be expressed at the protein level. The surface exposure of OMP-1A and OMP-1N was verified by immunofluorescence microscopy. OMP-1B was undetectable either by surface biotinylation or by Western blotting of the whole bacterial lysate, suggesting that it is not expressed by<jats:italic>E. chaffeensis</jats:italic>cultured in THP-1 cells. Additional<jats:italic>E. chaffeensis</jats:italic>surface proteins detected were OMP85, hypothetical protein ECH_0525 (here named Esp73), immunodominant surface protein gp47, and 11 other proteins. The identification of<jats:italic>E. chaffeensis</jats:italic>surface-exposed proteins provides novel insights into the<jats:italic>E. chaffeensis</jats:italic>surface and lays the foundation for rational studies on pathogen-host interactions and vaccine development.</jats:p> Surface-Exposed Proteins of<i>Ehrlichia chaffeensis</i> Infection and Immunity |
spellingShingle | Ge, Yan, Rikihisa, Yasuko, Infection and Immunity, Surface-Exposed Proteins ofEhrlichia chaffeensis, Infectious Diseases, Immunology, Microbiology, Parasitology |
title | Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_full | Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_fullStr | Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_full_unstemmed | Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_short | Surface-Exposed Proteins ofEhrlichia chaffeensis |
title_sort | surface-exposed proteins of<i>ehrlichia chaffeensis</i> |
title_unstemmed | Surface-Exposed Proteins ofEhrlichia chaffeensis |
topic | Infectious Diseases, Immunology, Microbiology, Parasitology |
url | http://dx.doi.org/10.1128/iai.00188-07 |