Evolving antibody evasion and receptor affinity of the Omicron BA.2.75 sublineage of SARS-CoV-2

SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly CH.1.1 and BN.1. Here, we investigated the viral receptor affinities and neutralization evasion properties of major BA.2.75 subvariants actively...

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Published iniScience Vol. 26; no. 11; p. 108254
Main Authors Wang, Qian, Li, Zhiteng, Guo, Yicheng, Mellis, Ian A., Iketani, Sho, Liu, Michael, Yu, Jian, Valdez, Riccardo, Lauring, Adam S., Sheng, Zizhang, Gordon, Aubree, Liu, Lihong, Ho, David D.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 17.11.2023
Elsevier
Subjects
antibody evasion
BA.2.75 subvariants
convergent evolution
evolutionary trajectories
mRNA vaccine
neutralizing monoclonal antibody
receptor-binding affinity
SARS-CoV-2
BA.2.75 subvariants
SARS-CoV-2
convergent evolution
neutralizing monoclonal antibody
antibody evasion
evolutionary trajectories
receptor-binding affinity
mRNA vaccine
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Abstract SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly CH.1.1 and BN.1. Here, we investigated the viral receptor affinities and neutralization evasion properties of major BA.2.75 subvariants actively circulating in different regions worldwide. We found two distinct evolutionary pathways and three newly identified mutations that shaped the virological features of these subvariants. One phenotypic group exhibited a discernible decrease in viral receptor affinities, but a noteworthy increase in resistance to antibody neutralization, as exemplified by CH.1.1, which is apparently as resistant as XBB.1.5. In contrast, a second group demonstrated a substantial increase in viral receptor affinity but only a moderate increase in antibody evasion, as exemplified by BN.1. We also observed that all prevalent SARS-CoV-2 variants in the circulation presently, except for BN.1, exhibit profound levels of antibody evasion, suggesting this is the dominant determinant of virus transmissibility today. [Display omitted] •BA.2.75 continues to evolve into multiple subvariants, including CH.1.1 and BN.1•CH.1.1 exhibits a level of antibody evasion comparable to that of XBB.1.5•Among BA.2.75 sublineages, BN.1 has the highest viral receptor-binding affinity•BA.2.75 subvariants either increase receptor affinity or heighten antibody evasion
AbstractList SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly CH.1.1 and BN.1. Here, we investigated the viral receptor affinities and neutralization evasion properties of major BA.2.75 subvariants actively circulating in different regions worldwide. We found two distinct evolutionary pathways and three newly identified mutations that shaped the virological features of these subvariants. One phenotypic group exhibited a discernible decrease in viral receptor affinities, but a noteworthy increase in resistance to antibody neutralization, as exemplified by CH.1.1, which is apparently as resistant as XBB.1.5. In contrast, a second group demonstrated a substantial increase in viral receptor affinity but only a moderate increase in antibody evasion, as exemplified by BN.1. We also observed that all prevalent SARS-CoV-2 variants in the circulation presently, except for BN.1, exhibit profound levels of antibody evasion, suggesting this is the dominant determinant of virus transmissibility today.SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly CH.1.1 and BN.1. Here, we investigated the viral receptor affinities and neutralization evasion properties of major BA.2.75 subvariants actively circulating in different regions worldwide. We found two distinct evolutionary pathways and three newly identified mutations that shaped the virological features of these subvariants. One phenotypic group exhibited a discernible decrease in viral receptor affinities, but a noteworthy increase in resistance to antibody neutralization, as exemplified by CH.1.1, which is apparently as resistant as XBB.1.5. In contrast, a second group demonstrated a substantial increase in viral receptor affinity but only a moderate increase in antibody evasion, as exemplified by BN.1. We also observed that all prevalent SARS-CoV-2 variants in the circulation presently, except for BN.1, exhibit profound levels of antibody evasion, suggesting this is the dominant determinant of virus transmissibility today.
SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly CH.1.1 and BN.1. Here, we investigated the viral receptor affinities and neutralization evasion properties of major BA.2.75 subvariants actively circulating in different regions worldwide. We found two distinct evolutionary pathways and three newly identified mutations that shaped the virological features of these subvariants. One phenotypic group exhibited a discernible decrease in viral receptor affinities, but a noteworthy increase in resistance to antibody neutralization, as exemplified by CH.1.1, which is apparently as resistant as XBB.1.5. In contrast, a second group demonstrated a substantial increase in viral receptor affinity but only a moderate increase in antibody evasion, as exemplified by BN.1. We also observed that all prevalent SARS-CoV-2 variants in the circulation presently, except for BN.1, exhibit profound levels of antibody evasion, suggesting this is the dominant determinant of virus transmissibility today.
SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly CH.1.1 and BN.1. Here, we investigated the viral receptor affinities and neutralization evasion properties of major BA.2.75 subvariants actively circulating in different regions worldwide. We found two distinct evolutionary pathways and three newly identified mutations that shaped the virological features of these subvariants. One phenotypic group exhibited a discernible decrease in viral receptor affinities, but a noteworthy increase in resistance to antibody neutralization, as exemplified by CH.1.1, which is apparently as resistant as XBB.1.5. In contrast, a second group demonstrated a substantial increase in viral receptor affinity but only a moderate increase in antibody evasion, as exemplified by BN.1. We also observed that all prevalent SARS-CoV-2 variants in the circulation presently, except for BN.1, exhibit profound levels of antibody evasion, suggesting this is the dominant determinant of virus transmissibility today. [Display omitted] •BA.2.75 continues to evolve into multiple subvariants, including CH.1.1 and BN.1•CH.1.1 exhibits a level of antibody evasion comparable to that of XBB.1.5•Among BA.2.75 sublineages, BN.1 has the highest viral receptor-binding affinity•BA.2.75 subvariants either increase receptor affinity or heighten antibody evasion
ArticleNumber 108254
Author Yu, Jian
Liu, Lihong
Li, Zhiteng
Lauring, Adam S.
Mellis, Ian A.
Liu, Michael
Guo, Yicheng
Sheng, Zizhang
Gordon, Aubree
Wang, Qian
Iketani, Sho
Ho, David D.
Valdez, Riccardo
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Issue 11
Keywords BA.2.75 subvariants
SARS-CoV-2
convergent evolution
neutralizing monoclonal antibody
antibody evasion
evolutionary trajectories
receptor-binding affinity
mRNA vaccine
Language English
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Snippet SARS-CoV-2 Omicron BA.2.75 has diversified into multiple subvariants with additional spike mutations and several are expanding in prevalence, particularly...
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StartPage 108254
SubjectTerms antibody evasion
BA.2.75 subvariants
convergent evolution
evolutionary trajectories
mRNA vaccine
neutralizing monoclonal antibody
receptor-binding affinity
SARS-CoV-2
Title Evolving antibody evasion and receptor affinity of the Omicron BA.2.75 sublineage of SARS-CoV-2
URI https://dx.doi.org/10.1016/j.isci.2023.108254
https://www.ncbi.nlm.nih.gov/pubmed/38026207
https://www.proquest.com/docview/2895699717
https://doaj.org/article/7f2b73f89dda43fc8f43fd1452cf7be6
Volume 26
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