Dataset Information

Role of IgM and IgA Antibodies in the Neutralization of SARS-CoV-2.

ABSTRACT:

Background

SARS-CoV-2 has infected millions of people globally. Virus infection requires the receptor-binding domain (RBD) of the spike protein. Although studies have demonstrated anti-spike and - RBD antibodies to be protective in animal models, and convalescent plasma as a promising therapeutic option, little is known about immunoglobulin (Ig) isotypes capable of blocking infection.

Methods

We studied spike- and RBD-specific Ig isotypes in convalescent and acute plasma/sera using a multiplex bead assay. We also determined virus neutralization activities in plasma, sera, and purified Ig fractions using a VSV pseudovirus assay.

Results

Spike- and RBD-specific IgM, IgG1, and IgA1 were produced by all or nearly all subjects at variable levels and detected early after infection. All samples displayed neutralizing activity. Regression analyses revealed that IgM and IgG1 contributed most to neutralization, consistent with IgM and IgG fractions' neutralization potency. IgA also exhibited neutralizing activity, but with lower potency.

Conclusion

IgG, IgM and IgA are critical components of convalescent plasma used for COVID-19 treatment.

SUBMITTER: Klingler J

PROVIDER: S-EPMC7654883 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Publications

Role of IgM and IgA Antibodies in the Neutralization of SARS-CoV-2.

Klingler Jéromine J Weiss Svenja S Itri Vincenza V Liu Xiaomei X Oguntuyo Kasopefoluwa Y KY Stevens Christian C Ikegame Satoshi S Hung Chuan-Tien CT Enyindah-Asonye Gospel G Amanat Fatima F Baine Ian I Arinsburg Suzanne S Bandres Juan C JC Kojic Erna Milunka EM Stoever Jonathan J Jurczyszak Denise D Bermudez-Gonzalez Maria M Nádas Arthur A Liu Sean S Lee Benhur B Zolla-Pazner Susan S Hioe Catarina E CE

medRxiv : the preprint server for health sciences 20201221

<h4>Background</h4>SARS-CoV-2 has infected millions of people globally. Virus infection requires the receptor-binding domain (RBD) of the spike protein. Although studies have demonstrated anti-spike and - RBD antibodies to be protective in animal models, and convalescent plasma as a promising therapeutic option, little is known about immunoglobulin (Ig) isotypes capable of blocking infection.<h4>Methods</h4>We studied spike- and RBD-specific Ig isotypes in convalescent and acute plasma/sera usin ...[more]

PMID: 33173891

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Project description:Zoonotic spillover of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) to humans in December 2019 caused the coronavirus disease 2019 (COVID-19) pandemic. Serological monitoring is critical for detailed understanding of individual immune responses to infection and protection to guide clinical therapeutic and vaccine strategies. We developed a high throughput multiplexed SARS-CoV-2 antigen microarray incorporating spike (S) and nucleocapsid protein (NP) and fragments expressed in various hosts which allowed simultaneous assessment of serum IgG, IgA, and IgM responses. Antigen glycosylation influenced antibody binding, with S glycosylation generally increasing and NP glycosylation decreasing binding. Purified antibody isotypes demonstrated a binding pattern and intensity different from the same isotype in whole serum, probably due to competition from the other isotypes present. Using purified antibody isotypes from naïve Irish COVID-19 patients, we correlated antibody isotype binding to different panels of antigens with disease severity, with binding to the S region S1 expressed in insect cells (S1 Sf21) significant for IgG, IgA, and IgM. Assessing longitudinal response for constant concentrations of purified antibody isotypes for a patient subset demonstrated that the relative proportion of antigen-specific IgGs decreased over time for severe disease, but the relative proportion of antigen-specific IgA binding remained at the same magnitude at 5 and 9 months post-first symptom onset. Further, the relative proportion of IgM binding decreased for S antigens but remained the same for NP antigens. This may support antigen-specific serum IgA and IgM playing a role in maintaining longer-term protection, important for developing and assessing vaccine strategies. Overall, these data demonstrate the multiplexed platform as a sensitive and useful platform for expanded humoral immunity studies, allowing detailed elucidation of antibody isotypes response against multiple antigens. This approach will be useful for monoclonal antibody therapeutic studies and screening of donor polyclonal antibodies for patient infusions.

Dataset Information

Role of IgM and IgA Antibodies in the Neutralization of SARS-CoV-2.

Background

Methods

Results

Conclusion

Publications

Role of IgM and IgA Antibodies in the Neutralization of SARS-CoV-2.

Similar Datasets

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