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EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus

Author

Listed:
  • Oscar A. Negrete

    (Department of Microbiology, Immunology and Molecular Genetics)

  • Ernest L. Levroney

    (Department of Microbiology, Immunology and Molecular Genetics)

  • Hector C. Aguilar

    (Department of Microbiology, Immunology and Molecular Genetics)

  • Andrea Bertolotti-Ciarlet

    (University of Pennsylvania)

  • Ronen Nazarian

    (Department of Microbiology, Immunology and Molecular Genetics)

  • Sara Tajyar

    (Department of Microbiology, Immunology and Molecular Genetics)

  • Benhur Lee

    (Department of Microbiology, Immunology and Molecular Genetics
    Department of Pathology and Laboratory Medicine
    UCLA AIDS Institute, David Geffen School of Medicine, UCLA)

Abstract

Nipah virus receptor Nipah virus, first recognized in 1999, is an emerging disease that causes fatal encephalitis in humans. Its natural host is thought to be the fruit bat but it is also found in pigs and other animals. It could pose a serious threat to the pig-farming industry and there is recent evidence of human-to-human transmission. A crucial receptor that the virus relies on to infect human cells has now been identified, suggesting ways that the infection might be countered by vaccines or drugs. The virus's attachment protein binds to the ephrinB2 receptor. This receptor is critical for normal vascular developmental processes and is present in tissues targeted by Nipah virus. The enzyme EphB4 can block the entry of the virus into the cell.

Suggested Citation

  • Oscar A. Negrete & Ernest L. Levroney & Hector C. Aguilar & Andrea Bertolotti-Ciarlet & Ronen Nazarian & Sara Tajyar & Benhur Lee, 2005. "EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus," Nature, Nature, vol. 436(7049), pages 401-405, July.
    • Handle: RePEc:nat:nature:v:436:y:2005:i:7049:d:10.1038_nature03838
    DOI: 10.1038/nature03838
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    Cited by:

    1. Ge Yang & Dong Wang & Bin Liu, 2024. "Structure of the Nipah virus polymerase phosphoprotein complex," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Yingying Guo & Songyue Wu & Wenting Li & Haonan Yang & Tianhao Shi & Bin Ju & Zheng Zhang & Renhong Yan, 2024. "The cryo-EM structure of homotetrameric attachment glycoprotein from langya henipavirus," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Li Chen & Mengmeng Sun & Huajun Zhang & Xinghai Zhang & Yanfeng Yao & Ming Li & Kangyin Li & Pengfei Fan & Haiwei Zhang & Ye Qin & Zhe Zhang & Entao Li & Zhen Chen & Wuxiang Guan & Shanshan Li & Chang, 2024. "Potent human neutralizing antibodies against Nipah virus derived from two ancestral antibody heavy chains," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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