The risk of zoonotic spillover of coronaviruses poses a constant threat to humanity, as recently exemplified by SARS‑CoV-2. During the pandemic, the rapid emergence of immune escape mutations led to a loss of efficacy of both therapeutic and humoral anti‑...

Cryo-electron tomography (cryo-ET) is emerging as a transformative tool for structural biology. Unlike methods based on purified molecules, cryo-ET en…

Learn about the 2026 winners of ACS Publications' Biological and Medicinal Chemistry lectureships and awards.

Coronaviruses use spike proteins to enter cells. This study shows these spikes can change shape, helping the viruses adapt to new hosts, including whales and dolphins. Understanding this flexibility may help predict and prevent future cross-species infections.

Author summary Coronaviruses are well known for their ability to jump between species, a process driven mainly by the spike protein on their surface. In this study, we examined spike proteins from coronaviruses found in marine mammals (whales and dolphins) to better understand how these viruses evolve and interact with their hosts. Using structural biology and mass spectrometry, we discovered several unusual features of the cetacean spike proteins. These spikes contain an extra domain within their receptor-binding region that resembles cupin proteins, assemble into trimers in a novel way that hides the receptor-binding domains, and show clusters of sugars (O-linked glycans) near the sites thought to interact with host receptors. These distinctive features suggest that cetacean coronaviruses may use a different entry mechanism, in which the extra domain acts as a switch to reveal the hidden receptor-binding regions. Such a mechanism could affect which species these viruses can infect, how easily they cross species barriers, and how they evade the immune system. Our findings emphasize the structural diversity and modularity of coronavirus spike proteins, highlight the unique adaptations of coronaviruses in marine mammals, and provide insight into their potential to give rise to new diseases in other species.

<p>We are delighted to announce the 2026 EMBO Practice Course on “<a href="https://www.embl.org/about/info/course-and-conference-office/events/cry26-01/#vf-tabs__section-dtc24-01" target="_blank"…

Nature Reviews Molecular Cell Biology, Published online: 26 March 2026; doi:10.1038/s41580-026-00962-4Yang and Liu discuss strategies that help address particle orientation bias in cryogenic electron microscopy (cryo-EM), and offer practical advice to tackle it.

Join our team to contribute to the operation and innovation of state-of-the-art cryo-electron microscopes and empower groundbreaking research.

A major new national facility for electron microscopy, called EMPower, has been awarded to a consortium of Dutch universities and medical centers. EMPower aims to pave the way for major discoveries im...

SARS-CoV-2 variant booster vaccination broadens human B cell responses through the germinal center reaction.

Lövestam and Scheres present a cryo-EM structure of vault particles, found during tau filament extraction from progressive supranuclear palsy (PSP) brain tissue. They reveal a symmetry shift at the va...

Are you a creative postdoctoral-scientist keen to explore novel in-situ biology with cryogenic electron tomography? Do you have a background in imaging technologies and/or image processing?We are look...

In a groundbreaking advance that significantly deepens our understanding of viral replication machinery, researchers have unveiled high-resolution cryo-electron microscopy (cryo-EM) structures of the Nipah virus (NiV) polymerase complex. This detailed structural insight opens new avenues for the design of antiviral agents targeting a highly pathogenic zoonotic virus responsible for severe and often fatal human infections. Nipah virus, an emergent member of the Paramyxoviridae family, poses a persistent public health threat due to its zoonotic nature and the absence of approved therapeutics.

Chakraborty, Sandate, et al. report that chromatin-bound p53 interacts with deubiquitinating enzyme USP7 but not with the E3 ubiquitin ligase E6AP-E6, despite both co-factors being associated with the...

Vitellogenin (Vg) is the main yolk precursor lipoprotein in almost all egg-laying animals. In addition, along its evolutionary history, Vg has developed a range of new functions in different taxa. In the honey bee, Vg has functions related to immunity, antioxidant protection, social behavior and longevity. However, the molecular mechanisms underlying Vg functionalities are still poorly understood. Here, we report the cryo-EM structure of full-length honey bee Vg, one-step purified directly from hemolymph. The structure provides structural insights into the overall domain architecture, including the lipid binding cavity and the previously uncharacterized von Willebrand factor type D domain. A domain of unknown function has been identified as a C-terminal cystine knot domain based on structural homology. Information about post-translational modifications, cleavage products, metal and lipid binding allow an improved understanding of the mechanisms underlying the range of Vg functionalitie