| Characterization of a sialic acid- and P-selectin glycoprotein ligand-1-independent adhesin activity in the granulocytotropic bacterium Anaplasma phagocytophilum. | |
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MedLine Citation:
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PMID: 16869829 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Anaplasma phagocytophilum, the aetiologic agent of human granulocytic anaplasmosis, is an obligate intracellular bacterium that colonizes neutrophils and neutrophil precursors. The granulocytotropic bacterium uses multiple adhesins that cooperatively bind to the N-terminal region of P-selectin glycoprotein ligand-1 (PSGL-1) and to sialyl Lewis x (sLe(x)) expressed on myeloid cell surfaces. Recognition of sLe(x) occurs through interactions with alpha2,3-sialic acid and alpha1,3-fucose. It is unknown whether other bacteria-host cell interactions are involved. In this study, we have enriched for A. phagocytophilum organisms that do not rely on sialic acid for cellular adhesion and entry by maintaining strain NCH-1 in HL-60 cells that are severely undersialylated. The selected bacteria, termed NCH-1A, also exhibit lessened dependencies on PSGL-1 and alpha1,3-fucose. Optimal adhesion and invasion by NCH-1A require interactions with the known determinants (sialic acid, PSGL-1 and alpha1,3-fucose), but none of them is absolutely necessary. NCH-1A binding to sLe(x)-modified PSGL-1 requires recognition of the known determinants in the same manners as other A. phagocytophilum strains. These data suggest that A. phagocytophilum expresses a separate adhesin from those targeting sialic acid, alpha1,3-fucose and the N-terminal region of PSGL-1. We propose that NCH-1A upregulates expression of this adhesin. |
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Authors:
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Dexter V Reneer; Sarah A Kearns; Tadayuki Yago; Jonathan Sims; Richard D Cummings; Rodger P McEver; Jason A Carlyon |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2006-07-26 |
Journal Detail:
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Title: Cellular microbiology Volume: 8 ISSN: 1462-5814 ISO Abbreviation: Cell. Microbiol. Publication Date: 2006 Dec |
Date Detail:
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Created Date: 2006-11-09 Completed Date: 2007-01-25 Revised Date: 2007-12-03 |
Medline Journal Info:
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Nlm Unique ID: 100883691 Medline TA: Cell Microbiol Country: England |
Other Details:
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Languages: eng Pagination: 1972-84 Citation Subset: IM |
Affiliation:
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Department of Microbiology, Immunology and Molecular Genetics, University of Kentucky College of Medicine, Lexington, KY, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adhesins, Bacterial
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chemistry,
metabolism* Anaplasma phagocytophilum / metabolism*, pathogenicity Bacterial Adhesion* Fucose / metabolism HL-60 Cells Humans Membrane Glycoproteins / metabolism N-Acetylneuraminic Acid / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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AI065631/AI/NIAID NIH HHS; AI48075/AI/NIAID NIH HHS; DK065039/DK/NIDDK NIH HHS; HL65631/HL/NHLBI NIH HHS; P20 RR020171/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Adhesins, Bacterial; 0/Membrane Glycoproteins; 0/P-selectin ligand protein; 131-48-6/N-Acetylneuraminic Acid; 3713-31-3/Fucose |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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