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Hadas Cohen-Dvashi¹, Itay Kilimnik¹, Ron Diskin²

¹Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.

Nature Microbiology

|August 29, 2018

Summary

This summary is machine-generated.

Lujo virus (LUJV), a fatal pathogen, uses the cellular receptor neuropilin-2 (NRP2) for cell entry. Structural analysis reveals LUJV

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Area of Science:

Virology
Structural Biology
Molecular Biology

Background:

Lujo virus (LUJV) is a highly fatal pathogen within the Arenaviridae family.
LUJV utilizes neuropilin-2 (NRP2) as a cellular receptor, distinct from canonical arenavirus receptors.
The unique cellular entry mechanism of LUJV raises questions about its evolutionary adaptation and molecular recognition.

Purpose of the Study:

To elucidate the structural mechanism by which LUJV's GP1 protein binds to NRP2.
To understand the molecular basis for LUJV's unprecedented receptor usage.
To provide insights for developing strategies against LUJV and similar emerging viral threats.

Main Methods:

X-ray crystallography was employed to determine the structure of the LUJV GP1 receptor-binding domain in complex with NRP2.
Structural analysis was combined with experimental validation to confirm key findings.
Comparative structural analysis was performed with known Old and New World arenaviruses.

Main Results:

The structure reveals that LUJV GP1 is more similar to Old World arenaviruses than New World arenaviruses.
NRP2 recognition by LUJV GP1 is dependent on metal ions.
The complete binding site for NRP2 is formed within the context of the trimeric viral spike protein.

Conclusions:

The study provides a detailed structural mechanism for LUJV cell attachment via NRP2.
Findings highlight the evolutionary flexibility of arenaviruses in adopting new cellular receptors.
This research offers critical information for the development of countermeasures against Lujo virus.