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Virus entry. Lassa virus entry requires a trigger-induced receptor switch.

Lucas T Jae1, Matthijs Raaben2, Andrew S Herbert3

  • 1Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, Netherlands.

Science (New York, N.Y.)
|June 28, 2014
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Summary
This summary is machine-generated.

Lassa virus infects humans via rodents, causing hemorrhagic fever. A specific protein switch in susceptible species, absent in birds, explains why chickens resist Lassa virus infection.

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Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • Lassa virus (LASV) is a zoonotic pathogen causing severe hemorrhagic fever in humans.
  • Avian cells have historically shown resistance to LASV infection, despite the virus's broad cellular tropism.
  • Understanding LASV entry mechanisms is crucial for developing antiviral strategies.

Purpose of the Study:

  • To elucidate the molecular mechanisms underlying Lassa virus entry into susceptible host cells.
  • To identify host factors and viral interactions that determine species-specific susceptibility to Lassa virus.
  • To investigate the role of cellular receptors and post-translational modifications in Lassa virus infection.

Main Methods:

  • Utilized haploid genetic screens to identify host factors essential for Lassa virus infection.
  • Investigated virus-receptor interactions using cell-based assays and biochemical analyses.
  • Analyzed the role of specific glycosylation sites on host cell receptors and viral glycoproteins.
  • Employed Lamp1-deficient mouse models to assess in vivo relevance.

Main Results:

  • Lassa virus engages α-dystroglycan in avian cells but requires a pH-dependent switch to LAMP1 for entry into susceptible cells.
  • The sialyltransferase ST3GAL4 is critical for the interaction between the Lassa virus glycoprotein and LAMP1.
  • A single glycosylated residue on LAMP1, absent in birds, is essential for Lassa virus envelope protein binding and subsequent infection.
  • Lamp1-deficient mice exhibit resistance to Lassa virus, confirming the in vivo importance of this receptor.

Conclusions:

  • Lassa virus entry relies on a species-specific receptor switch from α-dystroglycan to LAMP1, mediated by ST3GAL4.
  • A specific glycosylation site on LAMP1 is a key determinant of Lassa virus susceptibility.
  • This findings reveal a novel mechanism of viral entry and host tropism, offering potential targets for therapeutic intervention against Lassa virus.