E-resources
Peer reviewed
Open access
-
Nutalai, Rungtiwa; Zhou, Daming; Tuekprakhon, Aekkachai; Ginn, Helen M.; Supasa, Piyada; Liu, Chang; Huo, Jiandong; Mentzer, Alexander J.; Duyvesteyn, Helen M.E.; Dijokaite-Guraliuc, Aiste; Skelly, Donal; Ritter, Thomas G.; Amini, Ali; Bibi, Sagida; Adele, Sandra; Johnson, Sile Ann; Constantinides, Bede; Webster, Hermione; Temperton, Nigel; Klenerman, Paul; Barnes, Eleanor; Dunachie, Susanna J.; Crook, Derrick; Pollard, Andrew J.; Lambe, Teresa; Goulder, Philip; Paterson, Neil G.; Williams, Mark A.; Hall, David R.; Mongkolsapaya, Juthathip; Fry, Elizabeth E.; Dejnirattisai, Wanwisa; Ren, Jingshan; Stuart, David I.; Screaton, Gavin R.
Cell, 06/2022, Volume: 185, Issue: 12Journal Article
Highly transmissible Omicron variants of SARS-CoV-2 currently dominate globally. Here, we compare neutralization of Omicron BA.1, BA.1.1, and BA.2. BA.2 RBD has slightly higher ACE2 affinity than BA.1 and slightly reduced neutralization by vaccine serum, possibly associated with its increased transmissibility. Neutralization differences between sub-lineages for mAbs (including therapeutics) mostly arise from variation in residues bordering the ACE2 binding site; however, more distant mutations S371F (BA.2) and R346K (BA.1.1) markedly reduce neutralization by therapeutic antibody Vir-S309. In-depth structure-and-function analyses of 27 potent RBD-binding mAbs isolated from vaccinated volunteers following breakthrough Omicron-BA.1 infection reveals that they are focused in two main clusters within the RBD, with potent right-shoulder antibodies showing increased prevalence. Selection and somatic maturation have optimized antibody potency in less-mutated epitopes and recovered potency in highly mutated epitopes. All 27 mAbs potently neutralize early pandemic strains, and many show broad reactivity with variants of concern. Display omitted •Potent RBD antibodies from Omicron breakthrough vaccinees broadly neutralize VoC•These, possible recall antibodies, are focused in two main clusters•Somatic maturation adapts public antibodies to recover potency•BA.2 > BA.1 ACE2 affinity. BA.2 < BA.1 neutralization by vaccine serum and Vir-S309 Analysis of antibodies from SARS-CoV-2 Omicron breakthrough infections reveals their structural and functional properties as well as ability to neutralize different pandemic strains.
Author
![loading ... loading ...](themes/default/img/ajax-loading.gif)
Shelf entry
Permalink
- URL:
Impact factor
Access to the JCR database is permitted only to users from Slovenia. Your current IP address is not on the list of IP addresses with access permission, and authentication with the relevant AAI accout is required.
Year | Impact factor | Edition | Category | Classification | ||||
---|---|---|---|---|---|---|---|---|
JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
Select the library membership card:
If the library membership card is not in the list,
add a new one.
DRS, in which the journal is indexed
Database name | Field | Year |
---|
Links to authors' personal bibliographies | Links to information on researchers in the SICRIS system |
---|
Source: Personal bibliographies
and: SICRIS
The material is available in full text. If you wish to order the material anyway, click the Continue button.