Journal
CELL REPORTS MEDICINE
Volume 2, Issue 1, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.xcrm.2020.100189
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Funding
- National Institute of Allergy and Infectious Diseases of the National Institutes of Health [U24AI152172, U24AI152172-01S1]
- National Institute on Minority Health and Health Disparities of the National Institutes of Health [U54MD012388]
- State of Arizona Technology and Research Initiative Fund (TRIF)
- Hooper Undergraduate Research Award
- Jean Shuler Research Mini-Grant
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The study used a highly multiplexed peptide assay to investigate antibody responses across all human coronaviruses in COVID-19 convalescent and negative donors. The results show that antibodies elicited by SARS-CoV-2 can cross-recognize specific epitopes of pandemic and endemic coronavirus antigens, with a preference for binding endemic homologs.
The SARS-CoV-2 proteome shares regions of conservation with endemic human coronaviruses (CoVs), but it remains unknown to what extent these may be cross-recognized by the antibody response. Here, we study cross-reactivity using a highly multiplexed peptide assay (PepSeq) to generate an epitope- resolved view of IgG reactivity across all human CoVs in both COVID-19 convalescent and negative donors. PepSeq resolves epitopes across the SARS-CoV-2 Spike and Nucleocapsid proteins that are commonly targeted in convalescent donors, including several sites also recognized in some uninfected controls. By comparing patterns of homologous reactivity between CoVs and using targeted antibody-depletion experiments, we demonstrate that SARS-CoV-2 elicits antibodies that cross-recognize pandemic and endemic CoV antigens at two Spike S2 subunit epitopes. We further show that these cross-reactive antibodies preferentially bind endemic homologs. Our findings highlight sites at which the SARS-CoV-2 response appears to be shaped by previous CoV exposures and which have the potential to raise broadly neutralizing responses.
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