Long COVID can upend the lives of those who have it—when you’re a student, it can be even harder

(MedPage Today) -- Note that some links may require registration or subscription. Several California counties will require healthcare workers, and in some cases patients, to mask up during the upcoming respiratory virus season. (San Francisco... Source link

SARS-CoV-2 infection is associated with elevated risks of HPV-related carcinoma in situ and cancer, irrespective of age or race. The findings underscore the importance of understanding the interplay b...

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), responsible for the COVID-19 pandemic, utilizes membrane-bound, angiotensin-converting enzyme II (ACE2) for internalization and infection. We describe the development of a biologic that takes advantage of the proximity of the N-terminus of bound ACE2 to the three-fold symmetry axis of the spike protein to create an ultrapotent, trivalent ACE2 entry antagonist. Distinct disulfide bonds were added to enhance serum stability and a single point mutation was introduced to eliminate enzymatic activity. Through surface plasmon resonance, pseudovirus neutralization assays, and single-particle cryo-electron microscopy, we show this antagonist binds to and inhibits SARS-CoV-2 variants.   We further show the antagonist binds to and inhibits a 2003 SARS-CoV-1 strain. Collectively, structural insight has allowed us to design a universal trivalent antagonist against all variants of SARS-CoV-2 tested, suggesting it will be active against the emergence of future mutants. Structure-guided engineering of a trimeric ACE2 viral decoy reveals high affinity for spike protein, viral inhibition, and serum stability, offering a universal therapeutic strategy against SARS-CoV-2 variants and SARS-CoV-1 through symmetry-matched avidity.   Published in Communications Biology (Oct. 6, 2025): https://doi.org/10.1038/s42003-025-08819-w