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High-Resolution Map of Hantavirus Protein Advances Vaccine Research

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Andes Virus Blueprint Unveiled: A Critical Step Towards Vaccines and Therapies

Researchers have published new findings in the journal Cell regarding the Andes virus, a hantavirus. This research represents a significant step toward developing vaccines and antibody therapies for hantaviruses.

A team led by The University of Texas at Austin produced a detailed, high-resolution blueprint of a protein complex that the Andes virus uses to infect host cells. This structural information, a 3D map of the molecules, is crucial for vaccine development and antibody therapy creation. The detailed structure enabled researchers to develop a vaccine candidate that induced neutralizing antibodies against the Andes virus when injected into mice.

"Having a clearer blueprint of the virus enables the design of effective vaccines and antibody therapies for hantaviruses."
— Jason McLellan, Professor of Molecular Biosciences at UT Austin and Lead Researcher

The Hantavirus Threat

Hantaviruses are known to be transmitted from rodents to humans, have a death rate approaching 40%, and currently lack approved vaccines or treatments.

In 2024, the National Institutes of Health (NIH) identified hantaviruses as pathogens of high concern for future pandemics, initiating grants through the ReVAMPP program to study these viruses and develop countermeasures. This particular study was enabled by a grant establishing the Provident consortium.

Unveiling the Virus's Infection Mechanism

The team mapped the Andes virus's surface protein complex, a mushroom-shaped Gn-Gc tetramer, using cryo-electron microscopy. They analyzed virus-like particles (non-infectious mimics of the virus) and reconstructed the 3D structures of the tetramers on their surface.

A specialized method was used to isolate and analyze specific orientations of the tetramers, achieving an exceptionally high resolution of 2.3 angstroms, which is a substantial improvement over previous models.

Paving the Way for Future Countermeasures

These structures illustrate the Gn-Gc tetramer in its pre-infection state. For vaccines and antibody therapies to be most effective, they must target these surface proteins at this critical stage.

Future research aims to identify stabilizing mutations, potentially using artificial intelligence, to lock these viral protein complexes in the optimal pre-infection configuration.

Collaborative Effort

Collaborators on this study included Kartik Chandran from Albert Einstein College of Medicine, researchers from Texas A&M University, The University of Texas Southwestern Medical Center, and HDT Bio in Seattle.