TY - JOUR
T1 - Infection- and vaccine-induced antibody binding and neutralization of the B.1.351 SARS-CoV-2 variant
AU - Edara, Venkata Viswanadh
AU - Norwood, Carson
AU - Floyd, Katharine
AU - Lai, Lilin
AU - Davis-Gardner, Meredith E.
AU - Hudson, William H.
AU - Mantus, Grace
AU - Nyhoff, Lindsay E.
AU - Adelman, Max W.
AU - Fineman, Rebecca
AU - Patel, Shivan
AU - Byram, Rebecca
AU - Gomes, Dumingu Nipuni
AU - Michael, Garett
AU - Abdullahi, Hayatu
AU - Beydoun, Nour
AU - Panganiban, Bernadine
AU - McNair, Nina
AU - Hellmeister, Kieffer
AU - Pitts, Jamila
AU - Winters, Joy
AU - Kleinhenz, Jennifer
AU - Usher, Jacob
AU - O'Keefe, James B.
AU - Piantadosi, Anne
AU - Waggoner, Jesse J.
AU - Babiker, Ahmed
AU - Stephens, David S.
AU - Anderson, Evan J.
AU - Edupuganti, Srilatha
AU - Rouphael, Nadine
AU - Ahmed, Rafi
AU - Wrammert, Jens
AU - Suthar, Mehul S.
N1 - Funding Information:
This work was supported in part by grants (P51 OD011132, 3U19AI057266-17S1 CCHI Immune Memory Supplement, U19AI090023, R01AI127799, R01AI148378, K99AI153736, 1UM1AI148576-01, 5R38AI140299-03, and UM1AI148684 to Emory University) from the National Institute of Allergy and Infectious Diseases (NIAID), the National Institutes of Health (NIH), The Oliver S. and Jennie R. Donaldson Charitable Trust, the Emory Executive Vice President for Health Affairs Synergy Fund award, the Pediatric Research Alliance Center for Childhood Infections and Vaccines and Children's Healthcare of Atlanta, COVID-Catalyst-I3 Funds from the Woodruff Health Sciences Center and Emory School of Medicine, a Woodruff Health Sciences Center 2020 COVID-19 CURE Award, and the Vital Projects/Proteus funds. We thank Jim Wilbur (Mesoscale Discovery) for providing reagents to perform the RBD-binding assays. The graphical abstract was created with Biorender.com. The following reagent was obtained through BEI Resources, NIAID, NIH: SARS-Related Coronavirus 2, Isolate hCoV-19/South Africa/KRISP-K005325/2020, NR-54009, contributed by Alex Sigal and Tulio de Oliveira. We thank Natalie Thornburg, Clinton Paden, and Suxiang Tong for sequencing and analysis of the B.1.351 variant (CDC, Atlanta, GA). V.E. M.S. C.N. K.F. L.L. and M.D.G. contributed to the acquisition, analysis and interpretation of the data. W.H.H. G.M. L.E.N. M.W.A. R.F. S.P. R.B. D.N.G. G.M. H.A. N.B. B.P. N.M. K.H. J.P. J.W. J.K. J.U. J.B.O. A.P. J.J.W. and A.B. contributed to the acquisition, analysis, and interpretation of the data. S.E. served as the principal investigator of the clinical protocol for acquisition of patient samples and contributed to interpretation of the data. E.J.A. and N.R. contributed to the acquisition, analysis, and interpretation of the data. R.A. J.W. V.E. and M.S. contributed to the acquisition, analysis, and interpretation of the data as well as the conception and design of the work and writing of the manuscript. The authors declare no competing interests.
Publisher Copyright:
© 2021 Elsevier Inc.
PY - 2021/4/14
Y1 - 2021/4/14
N2 - The emergence of SARS-CoV-2 variants with mutations in the spike protein is raising concerns about the efficacy of infection- or vaccine-induced antibodies. We compared antibody binding and live virus neutralization of sera from naturally infected and Moderna-vaccinated individuals against two SARS-CoV-2 variants: B.1 containing the spike mutation D614G and the emerging B.1.351 variant containing additional spike mutations and deletions. Sera from acutely infected and convalescent COVID-19 patients exhibited a 3-fold reduction in binding antibody titers to the B.1.351 variant receptor-binding domain of the spike protein and a 3.5-fold reduction in neutralizing antibody titers against SARS-CoV-2 B.1.351 variant compared to the B.1 variant. Similar results were seen with sera from Moderna-vaccinated individuals. Despite reduced antibody titers against the B.1.351 variant, sera from infected and vaccinated individuals containing polyclonal antibodies to the spike protein could still neutralize SARS-CoV-2 B.1.351, suggesting that protective humoral immunity may be retained against this variant.
AB - The emergence of SARS-CoV-2 variants with mutations in the spike protein is raising concerns about the efficacy of infection- or vaccine-induced antibodies. We compared antibody binding and live virus neutralization of sera from naturally infected and Moderna-vaccinated individuals against two SARS-CoV-2 variants: B.1 containing the spike mutation D614G and the emerging B.1.351 variant containing additional spike mutations and deletions. Sera from acutely infected and convalescent COVID-19 patients exhibited a 3-fold reduction in binding antibody titers to the B.1.351 variant receptor-binding domain of the spike protein and a 3.5-fold reduction in neutralizing antibody titers against SARS-CoV-2 B.1.351 variant compared to the B.1 variant. Similar results were seen with sera from Moderna-vaccinated individuals. Despite reduced antibody titers against the B.1.351 variant, sera from infected and vaccinated individuals containing polyclonal antibodies to the spike protein could still neutralize SARS-CoV-2 B.1.351, suggesting that protective humoral immunity may be retained against this variant.
KW - SARS-CoV-2
KW - emerging variants
KW - humoral immunity
KW - receptor-binding domain
KW - vaccine
KW - viral neutralization
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U2 - 10.1016/j.chom.2021.03.009
DO - 10.1016/j.chom.2021.03.009
M3 - Article
C2 - 33798491
AN - SCOPUS:85103563984
VL - 29
SP - 516-521.e3
JO - Cell Host and Microbe
JF - Cell Host and Microbe
SN - 1931-3128
IS - 4
ER -