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Prepublished online as a Blood First Edition Paper on July 17, 2003; DOI 10.1182/blood-2003-02-0621. This Article Full Text (PDF) All Versions of this Article: 2003-02-0621v1 102/9/3387    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Carlyon, J. A Articles by Fikrig, E. Search for Related Content PubMed PubMed Citation Articles by Carlyon, J. A Articles by Fikrig, E. Social Bookmarking                   What's this? Submitted February 26, 2003 Accepted June 18, 2003 Murine neutrophils require 1,3-fucosylation but not PSGL-1 for productive infection with Anaplasma phagocytophilum Jason A Carlyon, Mustafa Akkoyunlu, Lijun Xia, Tadayuki Yago, Tian Wang, Richard D Cummings, Rodger P McEver, and Erol Fikrig* Section of Rheumatology, Department of Internal Medicine, Yale University, New Haven, CT, USA Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, Oklahoma City, OK, USA Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK, USA * Corresponding author; email: erol.fikrig{at}yale.edu. Anaplasma phagocytophilum causes human granulocytic ehrlichiosis, the second most-common tick-borne disease in the United States. Mice are natural reservoirs for this bacterium, and man is an inadvertent host. A. phagocytophilum's tropism for human neutrophils is linked to neutrophil expression of P-selectin glycoprotein ligand-1 (PSGL-1), as well as sialylated and 1,3-fucosylated glycans. To determine whether A. phagocytophilum utilizes similar molecular features to infect murine neutrophils, we assessed in vitro bacterial binding to neutrophils from and infection in wild-type mice, mice lacking 1,3-fucosyltransferases Fuc-TIV and Fuc-TVII, or mice lacking PSGL-1. Binding to Fuc-TIV-/-/Fuc-TVII-/- neutrophils and infection of Fuc-TIV-/-/Fuc-TVII-/- mice were significantly reduced relative to wild-type mice. A. phagocytophilum binding to PSGL-1-/- neutrophils was modestly reduced, whereas sialidase treatment significantly decreased binding to both wild-type and PSGL-1-/- neutrophils. A. phagocytophilum similarly infected PSGL-1-/- and wild-type mice in vivo. A. phagocytophilum induced comparable levels of chemokines from wild-type and PSGL-1-/- neutrophils in vitro, while those induced from Fuc-TIV-/-/Fuc-TVII-/- neutrophils were appreciably reduced. Therefore, A. phagocytophilum infection in mice, as in humans, requires sialylation and 1,3-fucosylation of neutrophils. However, murine infection does not require neutrophil expression of PSGL-1, which has important implications for understanding how A. phagocytophilum binds to and infects neutrophils. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: M. J. Troese and J. A. Carlyon Anaplasma phagocytophilum Dense-Cored Organisms Mediate Cellular Adherence through Recognition of Human P-Selectin Glycoprotein Ligand 1 Infect. Immun., September 1, 2009; 77(9): 4018 - 4027. [Abstract] [Full Text] [PDF] M. J. Troese, M. Sarkar, N. L. Galloway, R. J. Thomas, S. A. Kearns, D. V. Reneer, T. Yang, and J. A. 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