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Functional studies of host-specific ephrin-B ligands as Henipavirus receptors

  1. Author:
    Bossart, K. N.
    Tachedjian, M.
    McEachern, J. A.
    Crameri, G.
    Zhu, Z. Y.
    Dimitrov, D. S.
    Broder, C. C.
    Wang, L. F.
  2. Author Address

    Bossart, Katharine N.; Tachedjian, Mary, McEachern, Jennifer A.; Wang, Lin-Fa] CSIRO, Australian Anim Hlth Lab, Geelong, Vic 3220, Australia. [Zhu, Zhongyu] NCI, SAIC Frederick Inc, BRP, Frederick, MD 21702 USA. [Zhu, Zhongyu, Dimitrov, Dimiter S.] NCI, CCR, CCRNP, Prot Interact Grp, Frederick, MD 21702 USA. [Broder, Christopher C.] Uniformed Serv Univ Hlth Sci, Bethesda, MD 20814 USA.
    1. Year: 2008
  1. Journal: Virology
    1. 372
    2. 2
    3. Pages: 357-371
  2. Type of Article: Article
  1. Abstract:

    Hendra virus (HeV) and Nipah virus (NiV) are closely related paramyxoviruses that infect and cause disease in a wide range of mammalian hosts. To determine whether host receptor molecules play a role in species-specific and/or virus-specific infection we have cloned and characterized ephrin-B2 and ephrin-B3 ligands from a range of species, including human, horse, pig, cat, dog, bats (Pteropus alecto and Pteropus vampyrus) and mouse. HeV and NiV were both able to infect cells expressing any of the ephrin-B2 and ephrin-B3 molecules. There did not appear to be significant differences in receptor function from different species or receptor usage by HeV and NiV Soluble ephrin ligands, their receptors and G-specific human monoclonal antibodies differentially blocked henipavirus infections suggesting different receptor affinities, overlapping receptor binding domains of the henipavirus attachment glycoprotein (G) and that the functional domains of the ephrin ligands may be important for henipavirus binding. (c) 2007 Elsevier Inc. All rights reserved.

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External Sources

  1. PMID: 18054977

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