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A SARS-CoV-2 variant elicits an antibody response with a shifted immunodominance hierarchy.
Greaney, Allison J; Starr, Tyler N; Eguia, Rachel T; Loes, Andrea N; Khan, Khadija; Karim, Farina; Cele, Sandile; Bowen, John E; Logue, Jennifer K; Corti, Davide; Veesler, David; Chu, Helen Y; Sigal, Alex; Bloom, Jesse D.
  • Greaney AJ; Basic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America.
  • Starr TN; Department of Genome Sciences & Medical Scientist Training Program, University of Washington, Seattle, Washington, United States of America.
  • Eguia RT; Basic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America.
  • Loes AN; Howard Hughes Medical Institute, Chevy Chase, Maryland, United States of America.
  • Khan K; Basic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America.
  • Karim F; Basic Sciences Division and Computational Biology Program, Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America.
  • Cele S; Howard Hughes Medical Institute, Chevy Chase, Maryland, United States of America.
  • Bowen JE; Africa Health Research Institute, Durban, South Africa.
  • Logue JK; School of Laboratory Medicine and Medical Sciences, University of KwaZulu-Natal, Durban, South Africa.
  • Corti D; Africa Health Research Institute, Durban, South Africa.
  • Veesler D; School of Laboratory Medicine and Medical Sciences, University of KwaZulu-Natal, Durban, South Africa.
  • Chu HY; Africa Health Research Institute, Durban, South Africa.
  • Sigal A; School of Laboratory Medicine and Medical Sciences, University of KwaZulu-Natal, Durban, South Africa.
  • Bloom JD; Department of Biochemistry, University of Washington, Seattle, Washington, United States of America.
PLoS Pathog ; 18(2): e1010248, 2022 02.
Article in English | MEDLINE | ID: covidwho-1674026
Preprint
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ABSTRACT
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral / Antibody Formation Topics: Variants Limits: Humans Language: English Journal: PLoS Pathog Year: 2022 Document Type: Article Affiliation country: Journal.ppat.1010248

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Full text: Available Collection: International databases Database: MEDLINE Main subject: SARS-CoV-2 / COVID-19 / Antibodies, Viral / Antibody Formation Topics: Variants Limits: Humans Language: English Journal: PLoS Pathog Year: 2022 Document Type: Article Affiliation country: Journal.ppat.1010248