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Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics
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| Zeitschriftentitel: | Journal of Bacteriology |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Bacteriology, 189, 2007, 21, S. 7819-7828 |
| 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 |
|---|---|
| author |
Ge, Yan Rikihisa, Yasuko |
| spellingShingle |
Ge, Yan Rikihisa, Yasuko Journal of Bacteriology Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics Molecular Biology Microbiology |
| author_sort |
ge, yan |
| spelling |
Ge, Yan Rikihisa, Yasuko 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00866-07 <jats:title>ABSTRACT</jats:title><jats:p><jats:italic>Anaplasma phagocytophilum</jats:italic>is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of<jats:italic>A. phagocytophilum</jats:italic>plays a crucial role in subverting the hostile host cell environment. However, except for the P44/Msp2 outer membrane protein family, the surface components of<jats:italic>A. phagocytophilum</jats:italic>are largely unknown. To identify the major surface proteins of<jats:italic>A. phagocytophilum</jats:italic>, a membrane-impermeable, cleavable biotin reagent, sulfosuccinimidyl-2-[biotinamido]ethyl-1,3-dithiopropionate (Sulfo-NHS-SS-Biotin), was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin agarose affinity purification and then separated by electrophoresis, followed by capillary liquid chromatography-nanospray tandem mass spectrometry analysis. Among the major proteins captured by affinity purification were five<jats:italic>A. phagocytophilum</jats:italic>proteins, Omp85, hypothetical proteins APH_0404 (designated Asp62) and APH_0405 (designated Asp55), P44 family proteins, and Omp-1A. The surface exposure of Asp62 and Asp55 was verified by immunofluorescence microscopy. Recombinant Asp62 and Asp55 proteins were recognized by an HGA patient serum. Anti-Asp62 and anti-Asp55 peptide sera partially neutralized<jats:italic>A. phagocytophilum</jats:italic>infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family<jats:italic>Anaplasmataceae</jats:italic>. With the exception of P44-18, all of the proteins were newly revealed major surface-exposed proteins whose study should facilitate understanding the interaction between<jats:italic>A. phagocytophilum</jats:italic>and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines.</jats:p> Identification of Novel Surface Proteins of<i>Anaplasma phagocytophilum</i>by Affinity Purification and Proteomics Journal of Bacteriology |
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American Society for Microbiology, 2007 |
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American Society for Microbiology, 2007 |
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| title |
Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_unstemmed |
Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_full |
Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_fullStr |
Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_full_unstemmed |
Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_short |
Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_sort |
identification of novel surface proteins of<i>anaplasma phagocytophilum</i>by affinity purification and proteomics |
| topic |
Molecular Biology Microbiology |
| url |
http://dx.doi.org/10.1128/jb.00866-07 |
| publishDate |
2007 |
| physical |
7819-7828 |
| description |
<jats:title>ABSTRACT</jats:title><jats:p><jats:italic>Anaplasma phagocytophilum</jats:italic>is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of<jats:italic>A. phagocytophilum</jats:italic>plays a crucial role in subverting the hostile host cell environment. However, except for the P44/Msp2 outer membrane protein family, the surface components of<jats:italic>A. phagocytophilum</jats:italic>are largely unknown. To identify the major surface proteins of<jats:italic>A. phagocytophilum</jats:italic>, a membrane-impermeable, cleavable biotin reagent, sulfosuccinimidyl-2-[biotinamido]ethyl-1,3-dithiopropionate (Sulfo-NHS-SS-Biotin), was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin agarose affinity purification and then separated by electrophoresis, followed by capillary liquid chromatography-nanospray tandem mass spectrometry analysis. Among the major proteins captured by affinity purification were five<jats:italic>A. phagocytophilum</jats:italic>proteins, Omp85, hypothetical proteins APH_0404 (designated Asp62) and APH_0405 (designated Asp55), P44 family proteins, and Omp-1A. The surface exposure of Asp62 and Asp55 was verified by immunofluorescence microscopy. Recombinant Asp62 and Asp55 proteins were recognized by an HGA patient serum. Anti-Asp62 and anti-Asp55 peptide sera partially neutralized<jats:italic>A. phagocytophilum</jats:italic>infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family<jats:italic>Anaplasmataceae</jats:italic>. With the exception of P44-18, all of the proteins were newly revealed major surface-exposed proteins whose study should facilitate understanding the interaction between<jats:italic>A. phagocytophilum</jats:italic>and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines.</jats:p> |
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| author | Ge, Yan, Rikihisa, Yasuko |
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| description | <jats:title>ABSTRACT</jats:title><jats:p><jats:italic>Anaplasma phagocytophilum</jats:italic>is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of<jats:italic>A. phagocytophilum</jats:italic>plays a crucial role in subverting the hostile host cell environment. However, except for the P44/Msp2 outer membrane protein family, the surface components of<jats:italic>A. phagocytophilum</jats:italic>are largely unknown. To identify the major surface proteins of<jats:italic>A. phagocytophilum</jats:italic>, a membrane-impermeable, cleavable biotin reagent, sulfosuccinimidyl-2-[biotinamido]ethyl-1,3-dithiopropionate (Sulfo-NHS-SS-Biotin), was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin agarose affinity purification and then separated by electrophoresis, followed by capillary liquid chromatography-nanospray tandem mass spectrometry analysis. Among the major proteins captured by affinity purification were five<jats:italic>A. phagocytophilum</jats:italic>proteins, Omp85, hypothetical proteins APH_0404 (designated Asp62) and APH_0405 (designated Asp55), P44 family proteins, and Omp-1A. The surface exposure of Asp62 and Asp55 was verified by immunofluorescence microscopy. Recombinant Asp62 and Asp55 proteins were recognized by an HGA patient serum. Anti-Asp62 and anti-Asp55 peptide sera partially neutralized<jats:italic>A. phagocytophilum</jats:italic>infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family<jats:italic>Anaplasmataceae</jats:italic>. With the exception of P44-18, all of the proteins were newly revealed major surface-exposed proteins whose study should facilitate understanding the interaction between<jats:italic>A. phagocytophilum</jats:italic>and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines.</jats:p> |
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| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
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| physical | 7819-7828 |
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| series | Journal of Bacteriology |
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| spelling | Ge, Yan Rikihisa, Yasuko 0021-9193 1098-5530 American Society for Microbiology Molecular Biology Microbiology http://dx.doi.org/10.1128/jb.00866-07 <jats:title>ABSTRACT</jats:title><jats:p><jats:italic>Anaplasma phagocytophilum</jats:italic>is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of<jats:italic>A. phagocytophilum</jats:italic>plays a crucial role in subverting the hostile host cell environment. However, except for the P44/Msp2 outer membrane protein family, the surface components of<jats:italic>A. phagocytophilum</jats:italic>are largely unknown. To identify the major surface proteins of<jats:italic>A. phagocytophilum</jats:italic>, a membrane-impermeable, cleavable biotin reagent, sulfosuccinimidyl-2-[biotinamido]ethyl-1,3-dithiopropionate (Sulfo-NHS-SS-Biotin), was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin agarose affinity purification and then separated by electrophoresis, followed by capillary liquid chromatography-nanospray tandem mass spectrometry analysis. Among the major proteins captured by affinity purification were five<jats:italic>A. phagocytophilum</jats:italic>proteins, Omp85, hypothetical proteins APH_0404 (designated Asp62) and APH_0405 (designated Asp55), P44 family proteins, and Omp-1A. The surface exposure of Asp62 and Asp55 was verified by immunofluorescence microscopy. Recombinant Asp62 and Asp55 proteins were recognized by an HGA patient serum. Anti-Asp62 and anti-Asp55 peptide sera partially neutralized<jats:italic>A. phagocytophilum</jats:italic>infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family<jats:italic>Anaplasmataceae</jats:italic>. With the exception of P44-18, all of the proteins were newly revealed major surface-exposed proteins whose study should facilitate understanding the interaction between<jats:italic>A. phagocytophilum</jats:italic>and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines.</jats:p> Identification of Novel Surface Proteins of<i>Anaplasma phagocytophilum</i>by Affinity Purification and Proteomics Journal of Bacteriology |
| spellingShingle | Ge, Yan, Rikihisa, Yasuko, Journal of Bacteriology, Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics, Molecular Biology, Microbiology |
| title | Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_full | Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_fullStr | Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_full_unstemmed | Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_short | Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| title_sort | identification of novel surface proteins of<i>anaplasma phagocytophilum</i>by affinity purification and proteomics |
| title_unstemmed | Identification of Novel Surface Proteins ofAnaplasma phagocytophilumby Affinity Purification and Proteomics |
| topic | Molecular Biology, Microbiology |
| url | http://dx.doi.org/10.1128/jb.00866-07 |