Sheila F Lumley

TL;DR: In this paper, a structure-function analysis of B.1.351 was performed using a large cohort of convalescent and vaccinee serum samples, and it was shown that the receptor-binding domain mutations provide tighter ACE2 binding and widespread escape from monoclonal antibody neutralization largely driven by E484K, although K417N and N501Y act together against some important antibody classes.

TL;DR: The relationship between the presence of antibodies to severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) and the risk of subsequent reinfection remains unclear as discussed by the authors.

TL;DR: In this article, the authors examined the ability of B.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination, and found that B. 1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light chain contacts with residue 501.

TL;DR: Four commercial, widely available assays and a scalable 384-well ELISA can be used for SARS-CoV-2 serological testing to achieve sensitivity and specificity of at least 98%.

TL;DR: Risks were heterogenous across the hospital, with higher rates in acute medicine, and sporadic outbreaks in areas with few or no Covid-19 patients.