| pubmed-article:17766422 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0318329 | lld:lifeskim |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0872252 | lld:lifeskim |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0008551 | lld:lifeskim |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:17766422 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:17766422 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:17766422 | pubmed:dateCreated | 2007-10-18 | lld:pubmed |
| pubmed-article:17766422 | pubmed:abstractText | Anaplasma phagocytophilum is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of A. phagocytophilum 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 A. phagocytophilum are largely unknown. To identify the major surface proteins of A. phagocytophilum, 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 A. phagocytophilum 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 A. phagocytophilum infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family Anaplasmataceae. 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 A. phagocytophilum and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines. | lld:pubmed |
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| pubmed-article:17766422 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17766422 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17766422 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17766422 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17766422 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17766422 | pubmed:issn | 0021-9193 | lld:pubmed |
| pubmed-article:17766422 | pubmed:author | pubmed-author:RikihisaYasuk... | lld:pubmed |
| pubmed-article:17766422 | pubmed:author | pubmed-author:GeYanY | lld:pubmed |
| pubmed-article:17766422 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17766422 | pubmed:volume | 189 | lld:pubmed |
| pubmed-article:17766422 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17766422 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17766422 | pubmed:pagination | 7819-28 | lld:pubmed |
| pubmed-article:17766422 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17766422 | pubmed:meshHeading | pubmed-meshheading:17766422... | lld:pubmed |
| pubmed-article:17766422 | pubmed:meshHeading | pubmed-meshheading:17766422... | lld:pubmed |
| pubmed-article:17766422 | pubmed:meshHeading | pubmed-meshheading:17766422... | lld:pubmed |
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| pubmed-article:17766422 | pubmed:meshHeading | pubmed-meshheading:17766422... | lld:pubmed |
