DC-SIGN and DC-SIGNR Bind Ebola Glycoproteins and Enhance Infection of Macrophages and Endothelial Cells

Ebola virus exhibits a broad cellular tropism in vitro. In humans and animal models, virus is found in most tissues and organs during the latter stages of infection. In contrast, a more restricted cell and tissue tropism is exhibited early in infection where macrophages, liver, lymph node, and splee...

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Published in:	Virology (New York, N.Y.) Vol. 305; no. 1; pp. 115 - 123
Main Authors:	Simmons, Graham, Reeves, Jacqueline D., Grogan, Case C., Vandenberghe, Luk H., Baribaud, Frédéric, Whitbeck, J.Charles, Burke, Emily, Buchmeier, Michael J., Soilleux, Elizabeth J., Riley, James L., Doms, Robert W., Bates, Paul, Pöhlmann, Stefan
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 05.01.2003
Subjects:	Cell Adhesion Molecules - physiology Ebolavirus - physiology Endothelium, Vascular - cytology Endothelium, Vascular - virology Humans Lectins, C-Type - physiology Macrophages - virology Membrane Glycoproteins - physiology Receptors, Cell Surface - physiology Transduction, Genetic Viral Matrix Proteins - physiology
ISSN:	0042-6822, 1096-0341
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Abstract	Ebola virus exhibits a broad cellular tropism in vitro. In humans and animal models, virus is found in most tissues and organs during the latter stages of infection. In contrast, a more restricted cell and tissue tropism is exhibited early in infection where macrophages, liver, lymph node, and spleen are major initial targets. This indicates that cellular factors other than the broadly expressed virus receptor(s) modulate Ebola virus tropism. Here we demonstrate that the C-type lectins DC-SIGN and DC-SIGNR avidly bind Ebola glycoproteins and greatly enhance transduction of primary cells by Ebola virus pseudotypes and infection by replication-competent Ebola virus. DC-SIGN and DC-SIGNR are expressed in several early targets for Ebola virus infection, including dendritic cells, alveolar macrophages, and sinusoidal endothelial cells in the liver and lymph node. While DC-SIGN and DC-SIGNR do not directly mediate Ebola virus entry, their pattern of expression in vivo and their ability to efficiently capture virus and to enhance infection indicate that these attachment factors can play an important role in Ebola transmission, tissue tropism, and pathogenesis.
AbstractList	Ebola virus exhibits a broad cellular tropism in vitro. In humans and animal models, virus is found in most tissues and organs during the latter stages of infection. In contrast, a more restricted cell and tissue tropism is exhibited early in infection where macrophages, liver, lymph node, and spleen are major initial targets. This indicates that cellular factors other than the broadly expressed virus receptor(s) modulate Ebola virus tropism. Here we demonstrate that the C-type lectins DC-SIGN and DC-SIGNR avidly bind Ebola glycoproteins and greatly enhance transduction of primary cells by Ebola virus pseudotypes and infection by replication-competent Ebola virus. DC-SIGN and DC-SIGNR are expressed in several early targets for Ebola virus infection, including dendritic cells, alveolar macrophages, and sinusoidal endothelial cells in the liver and lymph node. While DC-SIGN and DC-SIGNR do not directly mediate Ebola virus entry, their pattern of expression in vivo and their ability to efficiently capture virus and to enhance infection indicate that these attachment factors can play an important role in Ebola transmission, tissue tropism, and pathogenesis. Ebola virus exhibits a broad cellular tropism in vitro. In humans and animal models, virus is found in most tissues and organs during the latter stages of infection. In contrast, a more restricted cell and tissue tropism is exhibited early in infection where macrophages, liver, lymph node, and spleen are major initial targets. This indicates that cellular factors other than the broadly expressed virus receptor(s) modulate Ebola virus tropism. Here we demonstrate that the C-type lectins DC-SIGN and DC-SIGNR avidly bind Ebola glycoproteins and greatly enhance transduction of primary cells by Ebola virus pseudotypes and infection by replication-competent Ebola virus. DC-SIGN and DC-SIGNR are expressed in several early targets for Ebola virus infection, including dendritic cells, alveolar macrophages, and sinusoidal endothelial cells in the liver and lymph node. While DC-SIGN and DC-SIGNR do not directly mediate Ebola virus entry, their pattern of expression in vivo and their ability to efficiently capture virus and to enhance infection indicate that these attachment factors can play an important role in Ebola transmission, tissue tropism, and pathogenesis.Ebola virus exhibits a broad cellular tropism in vitro. In humans and animal models, virus is found in most tissues and organs during the latter stages of infection. In contrast, a more restricted cell and tissue tropism is exhibited early in infection where macrophages, liver, lymph node, and spleen are major initial targets. This indicates that cellular factors other than the broadly expressed virus receptor(s) modulate Ebola virus tropism. Here we demonstrate that the C-type lectins DC-SIGN and DC-SIGNR avidly bind Ebola glycoproteins and greatly enhance transduction of primary cells by Ebola virus pseudotypes and infection by replication-competent Ebola virus. DC-SIGN and DC-SIGNR are expressed in several early targets for Ebola virus infection, including dendritic cells, alveolar macrophages, and sinusoidal endothelial cells in the liver and lymph node. While DC-SIGN and DC-SIGNR do not directly mediate Ebola virus entry, their pattern of expression in vivo and their ability to efficiently capture virus and to enhance infection indicate that these attachment factors can play an important role in Ebola transmission, tissue tropism, and pathogenesis.
Author	Riley, James L. Simmons, Graham Burke, Emily Reeves, Jacqueline D. Grogan, Case C. Buchmeier, Michael J. Baribaud, Frédéric Soilleux, Elizabeth J. Vandenberghe, Luk H. Bates, Paul Doms, Robert W. Whitbeck, J.Charles Pöhlmann, Stefan
Author_xml	– sequence: 1 givenname: Graham surname: Simmons fullname: Simmons, Graham organization: Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 2 givenname: Jacqueline D. surname: Reeves fullname: Reeves, Jacqueline D. organization: Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 3 givenname: Case C. surname: Grogan fullname: Grogan, Case C. organization: USAMRIID, Ft. Detrick, Frederick, Maryland, 21702 – sequence: 4 givenname: Luk H. surname: Vandenberghe fullname: Vandenberghe, Luk H. organization: Abramson Family Cancer Research Institute, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 5 givenname: Frédéric surname: Baribaud fullname: Baribaud, Frédéric organization: Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 6 givenname: J.Charles surname: Whitbeck fullname: Whitbeck, J.Charles organization: School of Dental Medicine, Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 7 givenname: Emily surname: Burke fullname: Burke, Emily organization: Division of Virology, Scripps Research Institute, La Jolla, California, 92037 – sequence: 8 givenname: Michael J. surname: Buchmeier fullname: Buchmeier, Michael J. organization: Division of Virology, Scripps Research Institute, La Jolla, California, 92037 – sequence: 9 givenname: Elizabeth J. surname: Soilleux fullname: Soilleux, Elizabeth J. organization: Department of Molecular Histopathology, University of Cambridge, Cambridge, CB2 1QP, United Kingdom – sequence: 10 givenname: James L. surname: Riley fullname: Riley, James L. organization: Abramson Family Cancer Research Institute, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 11 givenname: Robert W. surname: Doms fullname: Doms, Robert W. organization: Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 12 givenname: Paul surname: Bates fullname: Bates, Paul organization: Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104 – sequence: 13 givenname: Stefan surname: Pöhlmann fullname: Pöhlmann, Stefan organization: Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania, 19104
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/12504546$$D View this record in MEDLINE/PubMed
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Snippet	Ebola virus exhibits a broad cellular tropism in vitro. In humans and animal models, virus is found in most tissues and organs during the latter stages of...
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SubjectTerms	Cell Adhesion Molecules - physiology Ebolavirus - physiology Endothelium, Vascular - cytology Endothelium, Vascular - virology Humans Lectins, C-Type - physiology Macrophages - virology Membrane Glycoproteins - physiology Receptors, Cell Surface - physiology Transduction, Genetic Viral Matrix Proteins - physiology
Title	DC-SIGN and DC-SIGNR Bind Ebola Glycoproteins and Enhance Infection of Macrophages and Endothelial Cells
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