26 oktober 2022: Bron: NRC en Science Direct

De NRC schreef een uitstekend artikel over deze studie (abstract onderaan dit artikel): 

Imprinted antibody responses against SARS-CoV-2 Omicron sublineage

Hier het artikel in de NRC:

Brede afweer na Omikron-infectie


Een doorbraakinfectie na een volledige vaccinatie roept een sterke afweer op. Dat is ook goed nieuws voor het combinatievaccin.

Bij volledig gevaccineerde mensen die daarbovenop een infectie met de Omikron subvariant BA.1 kregen, ontstaan breed werkende antistoffen tegen zowel het oorspronkelijke coronavirus uit Wuhan als tegen allerlei subvarianten van Omikron, waaronder BA.4/5. Die laatste is nu in Nederland dominant. De antistoffen neutraliseren die subvariant BA.4/5 wel iets minder goed dan andere subvarianten, zoals BA.1 en BA.2, maar ze kunnen hem wel onschadelijk maken. Dat schrijft een groep internationale onderzoekers in een publicatie die vorige week in het wetenschappelijke tijdschrift Science verscheen. De vinding is goed nieuws: het bevestigt de verwachting dat de nieuwe vaccins tegen Omikron BA.1 ook beschermen tegen nieuwe subvarianten.

Een grote zorg van wetenschappers is dat het afweersysteem te rigide wordt. Kan het immuunsysteem, eenmaal getraind door een infectie met het originele virus uit Wuhan, of door een vaccinatieserie tegen dat oorspronkelijke virus, het afweergeschut nog wel omvormen tegen andere varianten? Die zorg groeit met de opkomst van een ‘variantensoep’; de talrijke subvarianten van Omikron die nu de corona-infecties veroorzaken en die aan de afweer weten te ontsnappen (Denemarken telde er recent zo’n 120).

De studie in Science laat zien dat het de eerste infectie of vaccinatie inderdaad een diepe stempel heeft gedrukt op het immuunsysteem.>>>>>>>>lees verder

Imprinted antibody responses against SARS-CoV-2 Omicron sublineages

20 Oct 2022
First Release


Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron sublineages carry distinct spike mutations and represent an antigenic shift resulting in escape from antibodies induced by previous infection or vaccination. We show that hybrid immunity or vaccine boosters elicit plasma neutralizing activity against Omicron BA.1, BA.2, BA.2.12.1 and BA.4/5 and that breakthrough infections, but not vaccination-only, induce neutralizing activity in the nasal mucosa. Consistent with immunological imprinting, most antibodies derived from memory B cells or plasma cells of Omicron breakthrough cases cross-react with the Wuhan-Hu-1, BA.1, BA.2, and BA.4/5 receptor-binding domains whereas Omicron primary infections elicit B cells of narrow specificity up to 6 months post infection. Although most clinical antibodies have reduced neutralization of Omicron, we identified an ultrapotent pan-variant neutralizing antibody, that is a strong candidate for clinical development.
The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron at the end of 2021 caused worldwide COVID-19 case surges. The Omicron BA.1 and BA.1.1 lineages swept the world followed by the BA.2 lineage (1). Although BA.1 and BA.2 share a large number of spike (S) mutations, they are each characterized by unique sets of amino acid changes, which are associated with different antigenic properties (24). The BA.2.12.1 sublineage emerged in the United States, peaking at the beginning of June and is characterized by the presence of the S1 L452Q receptor-binding domain (RBD) and S704L S2 subunit mutations in addition to the BA.2-defining mutations (4). The BA.2.75 sublineage is spreading in multiple countries and carries unique mutations (added to the BA.2 background) in the N-terminal domain (NTD), along with D339H, G446S and N460K mutations and the R493Q reversion in the RBD (5). The BA.3 S glycoprotein comprises a combination of mutations found in BA.1 S and BA.2 S (6), whereas BA.4 S and BA.5 S are identical to each other and comprise a deletion of residues 69-70, the L452R and F486V substitutions along with the R493Q reversion compared to BA.2 S (7). We characterized the emergence of Omicron (BA.1) as a major antigenic shift due to the unprecedented magnitude of immune evasion associated with this variant of concern (3812). Mutations in the BA.1 S glycoprotein NTD and RBD, which are the main targets of neutralizing antibodies (381318), explain the markedly reduced plasma neutralizing activity of previously infected or vaccinated subjects, especially those that have not received booster doses, and the escape from most monoclonal antibodies (mAbs) used in the clinic. As a result, an increasing number of reinfections or breakthrough infections are occurring (1922), even though these cases tend to be milder than infections of immunologically naive individuals.


We thank Abigail E. Powell and Nadine Czudnochowski for assistance with protein production.
Funding: This study was supported by the National Institute of Allergy and Infectious Diseases (DP1AI158186 and HHSN272201700059C to D.V.), a Pew Biomedical Scholars Award (D.V.), an Investigators in the Pathogenesis of Infectious Disease Awards from the Burroughs Wellcome Fund (D.V.), Fast Grants (D.V.), the University of Washington Arnold and Mabel Beckman cryoEM center and the National Institute of Health grant S10OD032290 (to D.V.). S.P.J.W. supported be NIH grant AI163019. D.V. is an Investigator of the Howard Hughes Medical Institute. O.G. is funded by the Swiss Kidney Foundation.
Author contributions: A.C.W., A.L., D.P., D.C., M.S.P. and D.V. designed the experiments; A.C.W., A.D.M., D.P., C.S., W.R., K.R.S. F.Z., H.V.D., M.G., G.Sc. and F.A.L. isolated mAb and performed binding, neutralization assays, biolayer interferometry and surface plasmon resonance binding measurements; A.R., J.Z., N.F., M.M.R., J.N. performed neutralization assays using authentic virus. H.K. confirmed the Spike mutations of authentic virus by Sanger sequencing. A.D.M. and D.P. performed ACE2 binding inhibition and S1 shedding assays; B.G. and M.A.S. evaluated effector functions; C.S.F., J.B. and L.P performed memory B cell repertoire analysis. O.G., A.C. and P.F. contributed to the recruitment of donors and collection of plasma samples. J.d.I., L.S. and A.T. performed bioinformatic and epidemiology analyses. Z.L. and S.P.J.W. performed mutant selection and fitness assays; R.A., J.J., F.B., P.M., J.N., G.D.d.M., L.K. and H.B. performed hamster model experiments and data analysis; Y.J.P. carried out cryoEM specimen preparation, data collection and processing. Y.J.P. and D.V. built and refined the atomic models. J.E.B., C.S. purified recombinant glycoproteins. A.L., D.P., Y.J.P., A.D.M., Z.L., D.P., D.C., M.S.P. and D.V. analyzed the data; A.C.W., D.P., D.C., M.S.P. and D.V. wrote the manuscript with input from all authors; F.B., G.S., J.N., S.P.J.W., H.W.V, M.S.P., D.C., and D.V. supervised the project.
Competing interests: D.P., Ad.M., F.Z., M.G., C.S.F., J.B., C.S., H.V.D., K.H., W.R., M.A.S., G.Sc., B.G., F.B., J.d.I., A.R., J.Z., N.F., H.K., M.M.R, J.N., F.A.L., G.S., L.P., A.T., H.W.V., A.L., M.S.P. and D.C. are employees of Vir Biotechnology Inc. and may hold shares in Vir Biotechnology Inc. L.A.P. is a former employee and shareholder in Regeneron Pharmaceuticals. Regeneron provided no funding for this work. H.W.V. is a founder and holds shares in PierianDx and Casma Therapeutics. Neither company provided resources. D.C. is currently listed as an inventor on multiple patent applications, which disclose the subject matter described in this manuscript. The Veesler laboratory has received a sponsored research agreement from Vir Biotechnology Inc. S.P.J.W. has licensing agreements with Vir Biotechnology and Merck and is a consultant for Thylacine Bio. The remaining authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.
Data and materials availability: The cryoEM map and coordinates have been deposited to the Electron Microscopy Databank and Protein Data Bank with accession numbers listed in table S5. Materials generated in this study will be made available on request, but may require a completed materials transfer agreement signed with Vir Biotechnology Inc. or the University of Washington.
License information: This article is subject to HHMI’s Open Access to Publications policy. HHMI lab heads have previously granted a nonexclusive CC BY 4.0 license to the public and a sublicensable license to HHMI in their research articles. Pursuant to those licenses, the author-accepted manuscript of this article can be made freely available under a CC BY 4.0 license immediately upon publication.

Supplementary Materials

This PDF file includes:

Materials and Methods
Figs. S1 to S18
Tables S1 to S9
References (95126)

Other Supplementary Material for this manuscript includes the following:

MDAR Reproducibility Checklist
Data S1

References and Notes

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