# Mount Sinai Identifies Single Mutation Altering Andes Virus Protein Dynamics in Vitro

- Published: 2026-11-07 01:49 UTC
- Section: Life & Health › Biology & biochemistry
- Tags: Andes virus protein dynamics, Mount Sinai hantavirus research, glycoprotein cleavage domain, virus like particles, Science Advances study
- URL: https://realtech.media/news/rt-acb1294b114e338018eb892e_mount_sinai_identifies/

**Researchers found that one amino acid difference in the Andes virus glycoprotein alters its transport in human cells and accelerates particle release in vitro.**

![Mount Sinai Identifies Single Mutation Altering Andes Virus Protein Dynamics in Vitro](https://realtech.media/media/2026/11/605d07815a6a5247.jpg)
*newswise.com*

On November 6, 2026, researchers from the Icahn School of Medicine at Mount Sinai published a study in *Science Advances* identifying a single amino acid difference between rodent- and human-derived isolates of the Andes virus that alters how a key glycoprotein behaves inside human cells, according to newswise.com. Andes virus is an RNA virus capable of causing hantavirus pulmonary syndrome and is notable for its ability to transmit between humans [1].

## Isolates Comparison and Screening

The team evaluated a rodent-derived isolate alongside a human-derived isolate collected during the 2018–2019 outbreak in Epuyén, Argentina, which involved human-to-human transmission and caused 11 deaths [1]. Genomic analysis revealed 25 amino acid variations between the two isolates. The authors focused on a substitution located adjacent to the glycoprotein cleavage domain due to its role in viral processing and assembly [1]. While the rodent-derived isolate grew faster, both reached equivalent final titers without differences in RNA production.

## Intracellular Dynamics and Particle Assembly

To observe the mechanics of the glycoprotein, researchers engineered the human-derived isolate's sequence to include the rodent-derived amino acid substitution using non-infectious molecular expression systems and virus-like particles [1]. The single substitution reduced the retention time of the glycoprotein in the Golgi apparatus and accelerated the release of virus-like particles [1].

The investigators noted that this in vitro work does not prove the mutation causes human adaptation or transmission in a complete infectious virus. However, the identified mechanism provides a baseline for evaluating sequences from other events, including the fatal 2026 outbreak aboard the cruise ship Hondius, where alterations in the transmembrane domain were identified [1].

## Sources

1. [newswise.com](https://www.newswise.com/articles/mount-sinai-study-identifies-single-amino-acid-change-that-alters-andes-virus-protein-behavior-in-human-cells)

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Source: RealTech, realtech.media — https://realtech.media/news/rt-acb1294b114e338018eb892e_mount_sinai_identifies/