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Atomic force microscopy reveals microtubule defects at submolecular resolution

In a study recently published in the journal Nano Letters, researchers from Nano Life Science Institute (WPI-NanoLSI), Kanazawa University, Kanazawa, Japan, used frequency-modulated atomic force microscopy to reveal the submolecular structure of microtubule (MT) inner surface and visualize structural defects in the MT lattice, providing valuable insights into the complex dynamic processes that regulate microtubule function.

Microtubules (MTs), a key component of the cytoskeleton in , serve as scaffolds and play vital roles in cellular processes such as , cell migration, intracellular transport, and trafficking. MTs are composed of α-tubulin and β-tubulin proteins, which polymerize into dimers and assemble into linear protofilaments that form a cylindrical lattice.

Traditional methods like X-ray crystallography and cryo– have provided structural insights into MTs but involve complex sample preparation and data analysis. There remains a need for techniques that can examine MT structural features, assembly dynamics, and lattice defects at submolecular resolution under physiological conditions.

WordPress Hunk Companion Plugin Flaw Exploited to Silently Install Vulnerable Plugins

“The chain of exploitation underscores the importance of securing every component of a WordPress site, especially third‑party themes and plugins, which can become critical points of entry for attackers.”

The development comes as Wordfence disclosed a high-severity flaw in the WPForms plugin (CVE-2024–11205, CVSS score: 8.5) that makes it possible for authenticated attackers, with Subscriber-level access and above, to refund Stripe payments and cancel subscriptions.

The vulnerability, which affects versions 1.8.4 up to, and including, 1.9.2.1, has been resolved in versions 1.9.2.2 or later. The plugin is installed on over 6 million WordPress sites.

A new class of antivirals could help prevent future pandemics

The arrival of Paxlovid in December 2021 marked another turning point in the COVID-19 pandemic—an effective antiviral that has since successfully treated millions. But like many antivirals before it, scientists know that at some point, Paxlovid is likely to lose some efficacy due to drug resistance. Researchers working to stay ahead of such emerging threats have now identified a wholly new way to treat SARS-CoV-2 infections—work that may have even broader implications.

In fact, a new study by the Tuschl laboratory introduces a proof-of-concept for a novel class of antivirals that would target a type of enzyme essential not just to SARS, but also many RNA viruses, including Ebola and dengue, as well as cytosolic-replicating DNA viruses, including Pox viruses. The findings may pave the way for a faster and more robust response to future pandemics.

“Nobody has found a way to inhibit this enzyme before,” says Thomas Tuschl, the F. M. Al Akl and Margaret Al Akl professor at Rockefeller. “Our work establishes cap methyl transferase enzymes as therapeutic targets and opens the door to many more antiviral developments against pathogens that until now we’ve had only limited tools to fight.”

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