A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy.
Many SARS-CoV-2 variants have mutations at key sites targeted by antibodies. However, it is unknown if antibodies elicited by infection with these variants target the same or different regions of the viral spike as antibodies elicited by earlier viral isolates. Here we compare the specificities of p...
| Main Authors: | , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2022-02-01
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| Series: | PLoS Pathogens |
| Online Access: | https://doi.org/10.1371/journal.ppat.1010248 |
| _version_ | 1819118859337072640 |
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| author | Allison J Greaney Tyler N Starr Rachel T Eguia Andrea N Loes Khadija Khan Farina Karim Sandile Cele John E Bowen Jennifer K Logue Davide Corti David Veesler Helen Y Chu Alex Sigal Jesse D Bloom |
| author_facet | Allison J Greaney Tyler N Starr Rachel T Eguia Andrea N Loes Khadija Khan Farina Karim Sandile Cele John E Bowen Jennifer K Logue Davide Corti David Veesler Helen Y Chu Alex Sigal Jesse D Bloom |
| author_sort | Allison J Greaney |
| collection | DOAJ |
| description | Many SARS-CoV-2 variants have mutations at key sites targeted by antibodies. However, it is unknown if antibodies elicited by infection with these variants target the same or different regions of the viral spike as antibodies elicited by earlier viral isolates. Here we compare the specificities of polyclonal antibodies produced by humans infected with early 2020 isolates versus the B.1.351 variant of concern (also known as Beta or 20H/501Y.V2), which contains mutations in multiple key spike epitopes. The serum neutralizing activity of antibodies elicited by infection with both early 2020 viruses and B.1.351 is heavily focused on the spike receptor-binding domain (RBD). However, within the RBD, B.1.351-elicited antibodies are more focused on the "class 3" epitope spanning sites 443 to 452, and neutralization by these antibodies is notably less affected by mutations at residue 484. Our results show that SARS-CoV-2 variants can elicit polyclonal antibodies with different immunodominance hierarchies. |
| first_indexed | 2024-12-22T05:55:34Z |
| format | Article |
| id | doaj.art-47294b3432084a629a2f2e376fdff936 |
| institution | Directory Open Access Journal |
| issn | 1553-7366 1553-7374 |
| language | English |
| last_indexed | 2024-12-22T05:55:34Z |
| publishDate | 2022-02-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj.art-47294b3432084a629a2f2e376fdff9362022-12-21T18:36:43ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742022-02-01182e101024810.1371/journal.ppat.1010248A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy.Allison J GreaneyTyler N StarrRachel T EguiaAndrea N LoesKhadija KhanFarina KarimSandile CeleJohn E BowenJennifer K LogueDavide CortiDavid VeeslerHelen Y ChuAlex SigalJesse D BloomMany SARS-CoV-2 variants have mutations at key sites targeted by antibodies. However, it is unknown if antibodies elicited by infection with these variants target the same or different regions of the viral spike as antibodies elicited by earlier viral isolates. Here we compare the specificities of polyclonal antibodies produced by humans infected with early 2020 isolates versus the B.1.351 variant of concern (also known as Beta or 20H/501Y.V2), which contains mutations in multiple key spike epitopes. The serum neutralizing activity of antibodies elicited by infection with both early 2020 viruses and B.1.351 is heavily focused on the spike receptor-binding domain (RBD). However, within the RBD, B.1.351-elicited antibodies are more focused on the "class 3" epitope spanning sites 443 to 452, and neutralization by these antibodies is notably less affected by mutations at residue 484. Our results show that SARS-CoV-2 variants can elicit polyclonal antibodies with different immunodominance hierarchies.https://doi.org/10.1371/journal.ppat.1010248 |
| spellingShingle | Allison J Greaney Tyler N Starr Rachel T Eguia Andrea N Loes Khadija Khan Farina Karim Sandile Cele John E Bowen Jennifer K Logue Davide Corti David Veesler Helen Y Chu Alex Sigal Jesse D Bloom A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy. PLoS Pathogens |
| title | A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy. |
| title_full | A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy. |
| title_fullStr | A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy. |
| title_full_unstemmed | A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy. |
| title_short | A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy. |
| title_sort | sars cov 2 variant elicits an antibody response with a shifted immunodominance hierarchy |
| url | https://doi.org/10.1371/journal.ppat.1010248 |
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