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Sera from unvaccinated, vaccinated, and previously infected and vaccinated individuals show reduced neutralizing and spike protein-binding activity towards the Omicron (B.1.1.529) variant of SARS-CoV-2 compared to other variants.
The production of blood cells, including some immune cells, relies heavily on the bone-marrow microenvironment. Cardiovascular diseases are now found to corrupt this niche, leading to imbalances in blood-cell production.
An investigation into the nature of genetic connections between individuals interred in the same chambers of an ancient tomb in Britain about 5,700 years ago sheds light on kinship in an early society.
A high-throughput yeast display platform is used to analyse the profiles of mutations in the SARS-CoV-2 receptor-binding domain (RBD) that enable escape from antibodies, and suggests that most anti-RBD antibodies can be escaped by the Omicron variant.
The B.1.1.529/Omicron variant of SARS-CoV-2 is resistant to neutralization by serum not only from patients who recovered from COVID-19, but also from individuals vaccinated with one of the four widely used COVID-19 vaccines.
The SARS-CoV-2 Alpha variant suppresses innate immune responses more effectively than isolates of first-wave SARS-CoV-2, and this is a result of mutations outside of the spike coding region that lead to upregulation of viral innate immune antagonists.
Pseudovirus assays and surface plasmon resonance show that the Omicron receptor-binding domain binds to human ACE2 with increased affinity relative to the ancestral virus, and that most neutralizing antibodies are considerably less potent against Omicron.
An isolate of the Omicron variant of SARS-COV-2 was completely or partially resistant to neutralization by all nine clinically approved monoclonal antibodies tested.
Plasma from individuals vaccinated with BNT162b2 exhibits 22-fold less neutralization capacity against Omicron (B.1.1.529) than against an ancestral SARS-CoV-2 strain but residual neutralization is maintained in those with high levels of neutralization of ancestral virus.
A distinct class of broadly neutralizing antibodies to the influenza virus target a membrane-proximal anchor epitope of the haemagglutinin stalk domain.
Disturbances in the radiocarbon record anchor a precisely dated archaeological stratigraphy of a medieval trading emporium in Denmark in time, revealing that the Viking expansion was associated with competition for trade routes rather than with raids.