author_facet Ge, Yan
Rikihisa, Yasuko
Ge, Yan
Rikihisa, Yasuko
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
facet_avail Online
Free
finc_class_facet Medizin
Biologie
format ElectronicArticle
fullrecord blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9pYWkuMDAxODgtMDc
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9pYWkuMDAxODgtMDc
institution DE-Zwi2
DE-D161
DE-Gla1
DE-Zi4
DE-15
DE-Pl11
DE-Rs1
DE-105
DE-14
FID-BBI-DE-23
DE-Ch1
DE-L229
DE-D275
DE-Bn3
DE-Brt1
imprint American Society for Microbiology, 2007
imprint_str_mv American Society for Microbiology, 2007
issn 0019-9567
1098-5522
issn_str_mv 0019-9567
1098-5522
language English
mega_collection American Society for Microbiology (CrossRef)
match_str ge2007surfaceexposedproteinsofehrlichiachaffeensis
publishDateSort 2007
publisher American Society for Microbiology
recordtype ai
record_format ai
series Infection and Immunity
source_id 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>
container_issue 8
container_start_page 3833
container_title Infection and Immunity
container_volume 75
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
_version_ 1792332837340315659
geogr_code not assigned
last_indexed 2024-03-01T14:03:13.309Z
geogr_code_person not assigned
openURL url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Surface-Exposed+Proteins+ofEhrlichia+chaffeensis&rft.date=2007-08-01&genre=article&issn=1098-5522&volume=75&issue=8&spage=3833&epage=3841&pages=3833-3841&jtitle=Infection+and+Immunity&atitle=Surface-Exposed+Proteins+of%3Ci%3EEhrlichia+chaffeensis%3C%2Fi%3E&aulast=Rikihisa&aufirst=Yasuko&rft_id=info%3Adoi%2F10.1128%2Fiai.00188-07&rft.language%5B0%5D=eng
SOLR
_version_ 1792332837340315659
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>
doi_str_mv 10.1128/iai.00188-07
facet_avail Online, Free
finc_class_facet Medizin, Biologie
format ElectronicArticle
format_de105 Article, E-Article
format_de14 Article, E-Article
format_de15 Article, E-Article
format_de520 Article, E-Article
format_de540 Article, E-Article
format_dech1 Article, E-Article
format_ded117 Article, E-Article
format_degla1 E-Article
format_del152 Buch
format_del189 Article, E-Article
format_dezi4 Article
format_dezwi2 Article, E-Article
format_finc Article, E-Article
format_nrw Article, E-Article
geogr_code not assigned
geogr_code_person not assigned
id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9pYWkuMDAxODgtMDc
imprint American Society for Microbiology, 2007
imprint_str_mv American Society for Microbiology, 2007
institution DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, FID-BBI-DE-23, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1
issn 0019-9567, 1098-5522
issn_str_mv 0019-9567, 1098-5522
language English
last_indexed 2024-03-01T14:03:13.309Z
match_str ge2007surfaceexposedproteinsofehrlichiachaffeensis
mega_collection American Society for Microbiology (CrossRef)
physical 3833-3841
publishDate 2007
publishDateSort 2007
publisher American Society for Microbiology
record_format ai
recordtype ai
series Infection and Immunity
source_id 49
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