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The structure of the Lujo virus spike complex

Author

Listed:
  • Maayan Eilon-Ashkenazy

    (Weizmann Institute of Science)

  • Hadas Cohen-Dvashi

    (Weizmann Institute of Science)

  • Sarah Borni

    (Weizmann Institute of Science)

  • Ron Shaked

    (Weizmann Institute of Science)

  • Rivka Calinsky

    (Weizmann Institute of Science)

  • Yaakov Levy

    (Weizmann Institute of Science)

  • Ron Diskin

    (Weizmann Institute of Science)

Abstract

Lujo virus (LUJV) is a human pathogen that was the cause of a deadly hemorrhagic fever outbreak in Africa. LUJV is a divergent member of the Arenaviridae with some similarities to both the “Old World” and “New World” serogroups, but it uses a cell-entry receptor, neuropilin-2 (NRP2), that is distinct from the receptors of OW and NW viruses. Though the receptor binding domain of LUJV has been characterized structurally, the overall organization of the trimeric spike complex and how NRP2 is recognized in this context were unknown. Here, we present the structure of the membrane-embedded LUJV spike complex determined by cryo-electron microscopy. Analysis of the structure suggested that a single NRP2 molecule is bound at the apex of the trimeric spike and that multiple subunits of the trimer contact the receptor. The binding of NRP2 involves an intriguing arginine-methionine interaction, which we analyzed using quantum mechanical modeling methods. We compare the LUJV spike structure with the only other available structure of a complete arenaviral spike, which is the Lassa virus. The similarities and differences between them shed light on Arenavirus evolution, inform vaccine design, and provide information that will be useful in combating future Arenavirus outbreaks.

Suggested Citation

  • Maayan Eilon-Ashkenazy & Hadas Cohen-Dvashi & Sarah Borni & Ron Shaked & Rivka Calinsky & Yaakov Levy & Ron Diskin, 2024. "The structure of the Lujo virus spike complex," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51606-0
    DOI: 10.1038/s41467-024-51606-0
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    References listed on IDEAS

    as
    1. Sheli R. Radoshitzky & Jonathan Abraham & Christina F. Spiropoulou & Jens H. Kuhn & Dan Nguyen & Wenhui Li & Jane Nagel & Paul J. Schmidt & Jack H. Nunberg & Nancy C. Andrews & Michael Farzan & Hyeryu, 2007. "Transferrin receptor 1 is a cellular receptor for New World haemorrhagic fever arenaviruses," Nature, Nature, vol. 446(7131), pages 92-96, March.
    2. Michael Katz & Jonathan Weinstein & Maayan Eilon-Ashkenazy & Katrin Gehring & Hadas Cohen-Dvashi & Nadav Elad & Sarel J. Fleishman & Ron Diskin, 2022. "Structure and receptor recognition by the Lassa virus spike complex," Nature, Nature, vol. 603(7899), pages 174-179, March.
    3. Hadas Cohen-Dvashi & Ron Amon & Krystle N. Agans & Robert W. Cross & Aliza Borenstein-Katz & Mathieu Mateo & Sylvain Baize & Vered Padler-Karavani & Thomas W. Geisbert & Ron Diskin, 2020. "Rational design of universal immunotherapy for TfR1-tropic arenaviruses," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    4. Wei Shi & Yongfei Cai & Haisun Zhu & Hanqin Peng & Jewel Voyer & Sophia Rits-Volloch & Hong Cao & Megan L. Mayer & Kangkang Song & Chen Xu & Jianming Lu & Jun Zhang & Bing Chen, 2023. "Cryo-EM structure of SARS-CoV-2 postfusion spike in membrane," Nature, Nature, vol. 619(7969), pages 403-409, July.
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