ArticleProceedings of the National Academy of Sciences of the United States of America2026
Spike destabilization attenuates Mink Cluster 5 SARS-CoV-2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors.
Funding
Abstract
Throughout the COVID-19 pandemic, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has shown the capacity to infect a wide range of nonhuman hosts, including farmed mink. In early 2020, a mink-associated variant, termed mink cluster 5 (MC5V), emerged in Denmark and spread to mink farmers and their household contacts but failed to cause a sustained outbreak and eventually disappeared. Here, we demonstrate that the spike protein (S) of MC5V is intrinsically unstable and impaired in processing, leading to markedly attenuated infectivity and fusogenicity. Remarkably, these defects are primarily driven by a single mutation, I692V, located in the S2 subunit of S, with additional contribution from the Y453F substitution in the receptor-binding domain. Structural analyses indicate that I692V induces conformational instability in S, promoting spontaneous S1 shedding and impairing spike incorporation into virions. These findings reveal that spike instability constrains viral fitness and emphasize the importance of monitoring zoonotic SARS-CoV-2 variants and other emerging viral pathogens.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.