High-Resolution Molecular Blueprint of Andes Virus Surface Protein Opens Path for First Hantavirus Vaccines

UT Austin researchers reveal a high-resolution 3D map of the Andes virus protein complex. This breakthrough helps design the first vaccines for hantaviruses.

By: AXL Media

Published: Feb 27, 2026, 1:09 PM EST

Source: The information in this article was sourced from University of Texas at Austin

Mapping a Pathogen of Pandemic Potential

Hantaviruses, which are primarily transmitted from rodents to humans, represent a significant global health threat with a mortality rate approaching 40%. Despite their lethal nature and worldwide prevalence, there are currently no approved vaccines or targeted therapies available. The urgency for medical intervention was highlighted by high-profile fatalities last year, prompting the National Institutes of Health (NIH) to categorize hantaviruses as pathogens of the highest concern for future pandemics. Now, a breakthrough study published in the journal Cell provides a foundational tool for changing this trajectory through structural biology.

A 3D Blueprint for Viral Neutralization

A research team led by Jason McLellan, a professor of molecular biosciences at UT Austin, has successfully constructed a 2.3-angstrom resolution map of the Andes virus Gn-Gc tetramer. This mushroom-shaped protein complex sits on the surface of the virus and acts as the "key" that allows the pathogen to unlock and enter host cells. By capturing details at the scale of individual atoms, the team has created a 3D blueprint that allows scientists to see exactly where the virus is vulnerable to antibodies. This level of detail is a prerequisite for the rational design of vaccines and therapeutic proteins.

Innovative Imaging Techniques at the Nanoscale

To achieve this unprecedented clarity, the team utilized cryo-electron microscopy (cryo-EM) on virus-like particles that mimic the structure of the Andes virus without being infectious. The breakthrough came from a novel reconstruction method where researchers isolated only the "shadows" of protein complexes oriented sideways to the electron beam. This selective processing corrected major inaccuracies found in previous 12-angstrom models, providing a transformational improvement in structural accuracy. McLellan predicts that this refined imaging method will soon be applied to the study of various other high-risk viral families.