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. 2021 Nov;18(11):2557-2559.
doi: 10.1038/s41423-021-00772-y. Epub 2021 Oct 11.

Delta variant (B.1.617.2) sublineages do not show increased neutralization resistance

Prerna Arora  1   2 , Amy Kempf  1   2 , Inga Nehlmeier  1 , Luise Graichen  1   2 , Anzhalika Sidarovich  1   2 , Martin S Winkler  3 , Sebastian Schulz  4 , Hans-Martin Jäck  4 , Metodi V Stankov  5 , Georg M N Behrens  5 , Stefan Pöhlmann  6   7 , Markus Hoffmann  8   9
Affiliations

Delta variant (B.1.617.2) sublineages do not show increased neutralization resistance

Prerna Arora et al. Cell Mol Immunol. 2021 Nov.
No abstract available

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Conflict of interest statement

The authors declare no competing interests.

Figures

Fig. 1
Fig. 1
Sublineages of the Delta variant do not show increased host cell entry or resistance to neutralization by antibodies from infected or vaccinated individuals. A Schematic illustration of the SARS-CoV-2 S protein. Mutations associated with the Delta variant (B.1.617.2) are highlighted in red. Mutation K417N, specific for variant Delta Plus, is marked in purple; mutations identical to those found in the Alpha variant (B.1.1.7) are labeled in green (RBD, receptor-binding domain; TD, transmembrane domain). B A summary of S protein variants under study and their respective mutations is given below the S protein scheme (NTD, N-terminal domain). C Particles pseudotyped with the indicated S proteins were inoculated onto four different cell lines, and transduction efficiency was quantified by measuring virus-encoded luciferase activity in cell lysates at 16–18 h post transduction. Presented are average (mean) data from six biological replicates (each conducted with technical quadruplicates) for which transduction was normalized against wild-type (WT) SARS-CoV-2 S (=1). Error bars indicate the standard error of the mean (SEM). D Particles pseudotyped with WT (green), Delta (B.1.617.2) variant (yellow) or Delta Plus variant (purple) S proteins were incubated for 30 min at 37 °C in the presence of the indicated monoclonal antibodies before being inoculated onto Vero cells. Transduction efficiency was quantified as described above. For normalization, WT S protein-driven entry in the absence of monoclonal antibody was set as 0% inhibition. The average of four technical replicates is shown. Error bars indicate the standard deviation (SD). E, F Particles bearing the indicated S proteins were incubated for 30 min at 37 °C in the presence of different dilutions of convalescent plasma (E) or vaccinee serum (F) before being inoculated onto Vero cells. Transduction efficiency was quantified as stated above and used to calculate the plasma/serum dilution factor that leads to a 50% reduction in transduction (neutralizing titer 50, NT50). Data for nine convalescent plasma samples and fourteen vaccination serum samples are presented. Black lines indicate the median, and numbers in brackets represent the fold change in NT50 compared to WT SARS-CoV-2 S (dashed line = detection limit). Statistical significance was analyzed by two-tailed Student’s t test (nsp > 0.05; *p ≤ 0.05; **p ≤ 0.01; ***p ≤ 0.001)
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