AI Chat Paper
Note: Please note that the following content is generated by AMiner AI. SciOpen does not take any responsibility related to this content.
{{lang === 'zh_CN' ? '文章概述' : 'Summary'}}
{{lang === 'en_US' ? '中' : 'Eng'}}
Chat more with AI
Powered by AMiner. Clicking this button will take you away from SciOpen.
Home Genes & Diseases Article
PDF (2.7 MB)
Cite
EndNote(RIS) BibTeX
Collect
Submit Manuscript AI Chat Paper
Show Outline
Outline
Show full outline
Hide outline
Outline
Show full outline
Hide outline
Full Length Article | Open Access

Reduced neutralization of SARS-CoV-2 B.1.617 variant by convalescent and vaccinated sera

Jie Hua,1, Xiao-yu Weib,1, Jin Xianga,1, Pai Penga, Feng-li Xua, Kang Wua, Fei-yang Luoc, Ai-shun Jinc, Liang Fangb, Bei-zhong Liub( ), Kai Wanga( ), Ni Tanga( ), Ai-Long Huanga( )
Key Laboratory of Molecular Biology for Infectious Diseases (Ministry of Education), Institute for Viral Hepatitis, Department of Infectious Diseases, The Second Affiliated Hospital, Chongqing Medical University, Chongqing 400010, PR China
Yong-Chuan Hospital, Chongqing Medical University, Chongqing 402177, PR China
Department of Immunology, College of Basic Medicine, Chongqing Medical University, Chongqing 400016, PR China

Peer review under responsibility of Chongqing Medical University.

Show Author Information

Abstract

Coronavirus disease 2019 (COVID-19) is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The Spike protein that mediates coronavirus entry into host cells is a major target for COVID-19 vaccines and antibody therapeutics. However, multiple variants of SARS-CoV-2 have emerged, which may potentially compromise vaccine effectiveness. Using a pseudovirus-based assay, we evaluated SARS-CoV-2 cell entry mediated by the viral Spike B.1.617 and B.1.1.7 variants. We also compared the neutralization ability of monoclonal antibodies from convalescent sera and neutralizing antibodies (NAbs) elicited by CoronaVac (inactivated vaccine) and ZF2001 (RBD-subunit vaccine) against B.1.617 and B.1.1.7 variants. Our results showed that, compared to D614G and B.1.1.7 variants, B.1.617 shows enhanced viral entry and membrane fusion, as well as more resistant to antibody neutralization. These findings have important implications for understanding viral infectivity and for immunization policy against SARS-CoV-2 variants.

Keywords

MutationVaccineCoronavirusSARS-CoV-2Neutralizing antibodiesImmune escapeViral entry

References

1

V'kovski P, Kratzel A, Steiner S, Stalder H, Thiel V. Coronavirus biology and replication: implications for SARS-CoV-2. Nat Rev Microbiol. 2021;19(3): 155-170.
Crossref Google Scholar
2

Korber B, Fischer WM, Gnanakaran S, et al. Tracking changes in SARS-CoV-2 spike: evidence that D614G increases infectivity of the COVID-19 virus. Cell. 2020;182(4): 812-827.
Crossref Google Scholar
3

Stamatatos L, Czartoski J, Wan YH, et al. mRNA vaccination boosts cross-variant neutralizing antibodies elicited by SARS-CoV-2 infection. Science. 2021;372(6549): 1413-1418.
Crossref Google Scholar
4

Robbiani DF, Gaebler C, Muecksch F, et al. Convergent antibody responses to SARS-CoV-2 in convalescent individuals. Nature. 2020;584(7821): 437-442.
Crossref Google Scholar
5

Piccoli L, Park YJ, Tortorici MA, et al. Mapping neutralizing and immunodominant sites on the SARS-CoV-2 spike receptor-binding domain by structure-guided high-resolution serology. Cell. 2020;183(4): 1024-1042.
Crossref Google Scholar
6

Hu J, Peng P, Wang K, et al. Emerging SARS-CoV-2 variants reduce neutralization sensitivity to convalescent sera and monoclonal antibodies. Cell Mol Immunol. 2021;18(4): 1061-1063.
Crossref Google Scholar
7

Hu J, He CL, Gao QZ, et al. D614G mutation of SARS-CoV-2 spike protein enhances viral infectivity. BioRxiv. 2020.
Crossref Google Scholar
8

Sheikh A, McMenamin J, Taylor B, Robertson C. Public Health Scotland and the EAVE Ⅱ Collaborators. SARS-CoV-2 Delta VOC in Scotland: demographics, risk of hospital admission, and vaccine effectiveness. Lancet. 2021;397(10293): 2461-2462.
Crossref Google Scholar
9

Kustin T, Harel N, Finkel U, et al. Evidence for increased breakthrough rates of SARS-CoV-2 variants of concern in BNT162b2-mRNA-vaccinated individuals. Nat Med. 2021;27(8): 1379-1384.
Crossref Google Scholar
10

Hacisuleyman E, Hale C, Saito Y, et al. Vaccine breakthrough infections with SARS-CoV-2 variants. N Engl J Med. 2021;384(23): 2212-2218.
Crossref Google Scholar
11

Peng P, Hu J, Deng HJ, et al. Changes in the humoral immunity response in SARS-CoV-2 convalescent patients over 8 months. Cell Mol Immunol. 2021;18(2): 490-491.
Crossref Google Scholar
12

Long QX, Liu BZ, Deng HJ, et al. Antibody responses to SARS-CoV-2 in patients with COVID-19. Nat Med. 2020;26(6): 845-848.
Crossref Google Scholar
13

Connor RI, Chen BK, Choe S, Landau NR. Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes. Virology. 1995;206(2): 935-944.
Crossref Google Scholar
14

Han X, Wang Y, Li S, et al. A rapid and efficient screening system for neutralizing antibodies and its application for SARS-CoV-2. Front Immunol. 2021;12: 653189.
Crossref Google Scholar
15

Ou X, Liu Y, Lei X, et al. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV. Nat Commun. 2020;11(1): 1620.
Crossref Google Scholar
16

Hu J, Gao Q, He C, Huang A, Tang N, Wang K. Development of cell-based Pseudovirus entry assay to identify potential viral entry inhibitors and neutralizing antibodies against SARS-CoV-2. Genes Dis. 2020;7(4): 551-557.
Crossref Google Scholar
17

Geraerts M, Willems S, Baekelandt V, Debyser Z, Gijsbers R. Comparison of lentiviral vector titration methods. BMC Biotechnol. 2006;6: 34.
Crossref Google Scholar
18

Shang J, Wan Y, Luo C, et al. Cell entry mechanisms of SARS-CoV-2. Proc Natl Acad Sci U S A. 2020;117(21): 11727-11734.
Crossref Google Scholar
19

Yi C, Sun X, Ye J, et al. Key residues of the receptor binding motif in the spike protein of SARS-CoV-2 that interact with ACE2 and neutralizing antibodies. Cell Mol Immunol. 2020;17(6): 621-630.
Crossref Google Scholar
20

Hoffmann M, Hofmann-Winkler H, Krüger N, et al. SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination. Cell Rep. 2021;36(3): 109415.
Crossref Google Scholar
21

Motozono C, Toyoda M, Zahradnik J, et al. SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity. Cell Host Microbe. 2021;29(7): 1124-1136.
Crossref Google Scholar
22

Saito A, Nasser H, Uriu K, et al. Enhanced fusogenicity and pathogenicity of SARS-CoV-2 Delta P681R mutation. Nature. 2022;602(7896): 300-306.
Crossref Google Scholar
23

Wall EC, Wu M, Harvey R, et al. Neutralising antibody activity against SARS-CoV-2 VOCs B.1.617.2 and B.1.351 by BNT162b2 vaccination. Lancet. 2021;397(10292): 2331-2333.
Crossref Google Scholar
24

Bolze A, Cirulli ET, Luo S, et al. Rapid displacement of SARS-CoV-2 variant B.1.1.7 by B.1.617.2 and P.1 in the United States. MedRxiv. 2021.
Google Scholar
25

Liu C, Ginn HM, Dejnirattisai W, et al. Reduced neutralization of SARS-CoV-2 B.1.617 by vaccine and convalescent serum. Cell. 2021;184(16): 4220-4236.
Crossref Google Scholar
26

Liu J, Liu Y, Xia H, et al. BNT162b2-elicited neutralization of B.1.617 and other SARS-CoV-2 variants. Nature. 2021;596(7871): 273-275.
Crossref Google Scholar
27

Edara VV, Pinsky BA, Suthar MS, et al. Infection and vaccine-induced neutralizing-antibody responses to the SARS-CoV-2 B.1.617 variants. N Engl J Med. 2021;385(7): 664-666.
Crossref Google Scholar
28

Caniels TG, Bontjer I, van der Straten K, et al. Emerging SARS-CoV-2 variants of concern evade humoral immune responses from infection and vaccination. Sci Adv. 2021;7(36): eabj5365.
Crossref Google Scholar
29

Collier DA, De Marco A, Ferreira IATM, et al. Sensitivity of SARS-CoV-2 B.1.1.7 to mRNA vaccine-elicited antibodies. Nature. 2021;593(7857): 136-141.
Crossref Google Scholar
30

Wu K, Werner AP, Koch M, et al. Serum neutralizing activity elicited by mRNA-1273 vaccine. N Engl J Med. 2021;384(15): 1468-1470.
Crossref Google Scholar
31

Greaney AJ, Starr TN, Gilchuk P, et al. Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition. Cell Host Microbe. 2021;29(1): 44-57.
Crossref Google Scholar
32

Wang P, Nair MS, Liu L, et al. Antibody resistance of SARS-CoV-2 variants B.1.351 and B.1.1.7. Nature. 2021;593(7857): 130-135.
Crossref Google Scholar
33

Hoffmann M, Arora P, Groß R, et al. SARS-CoV-2 variants B.1.351 and P.1 escape from neutralizing antibodies. Cell. 2021;184(9): 2384-2393.
Crossref Google Scholar
34

Li Q, Nie J, Wu J, et al. SARS-CoV-2 501Y. V2 variants lack higher infectivity but do have immune escape. Cell. 2021;184(9): 2362-2371.
Crossref Google Scholar
35

Liu Q, Xiong Q, Mei F, et al. Antibody neutralization to SARS-CoV-2 and variants after 1 year in Wuhan, China. Innovation (Camb). 2022;3(1): 100181.
Crossref Google Scholar
36

McCallum M, Bassi J, De Marco A, et al. SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern. Science. 2021;373(6555): 648-654.
Crossref Google Scholar
37

Deng X, Garcia-Knight MA, Khalid MM, et al. Transmission, infectivity, and neutralization of a spike L452R SARS-CoV-2 variant. Cell. 2021;184(13): 3426-3437.
Crossref Google Scholar
Genes & Diseases
Volume 9 Issue 5,
September 2022
Pages 1290-1300
DOI: 10.1016/j.gendis.2021.11.007
Cite this article:
Hu J, Wei X-y, Xiang J, et al. Reduced neutralization of SARS-CoV-2 B.1.617 variant by convalescent and vaccinated sera. Genes & Diseases, 2022, 9(5): 1290-1300. https://doi.org/10.1016/j.gendis.2021.11.007

389

Views

5

Downloads

11

Crossref

12

Web of Science

12

Scopus

0

CSCD

Altmetrics
Received: 11 July 2021
Revised: 26 September 2021
Accepted: 05 November 2021
Published: 03 December 2021
© 2021, Chongqing Medical University.

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

Return