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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: |
| Zusammenfassung: | <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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| Umfang: | 3833-3841 |
| ISSN: |
0019-9567
1098-5522 |
| DOI: | 10.1128/iai.00188-07 |