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The Structures of Secretory and Dimeric Immunoglobulin A

Sonya Kumar Bharathkar, Benjamin W. Parker, Andrey G. Malyutin, Nandan Haloi, Kathryn E. Huey-Tubman, Emad Tajkhorshid, Beth M. Stadtmueller
doi: https://doi.org/10.1101/2020.02.16.951780
Sonya Kumar Bharathkar
1Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois 61801 USA
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Benjamin W. Parker
1Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois 61801 USA
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Andrey G. Malyutin
2Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125 USA
3Beckman Institute, California Institute of Technology, Pasadena, CA 91125 USA
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Nandan Haloi
4Center for Biophysics and Quantitative Biology, University of Illinois at Urbana–Champaign, Urbana, 61801
5NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, Urbana, 61801
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Kathryn E. Huey-Tubman
2Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125 USA
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Emad Tajkhorshid
1Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois 61801 USA
4Center for Biophysics and Quantitative Biology, University of Illinois at Urbana–Champaign, Urbana, 61801
5NIH Center for Macromolecular Modeling and Bioinformatics, Beckman Institute for Advanced Science and Technology, Urbana, 61801
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Beth M. Stadtmueller
1Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, Illinois 61801 USA
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  • For correspondence: bethms@illinois.edu
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Abstract

Secretory (S) Immunoglobulin (I) A is the predominant mucosal antibody, which binds pathogens and commensal microbes. SIgA is a polymeric antibody, typically containing two copies of IgA that assemble with one joining-chain (JC) to form dimeric (d) IgA that is bound by the polymeric Ig-receptor ectodomain, called secretory component (SC). Here we report the cryo-electron microscopy structures of murine SIgA and dIgA. Structures reveal two IgAs conjoined through four heavy-chain tailpieces and the JC that together form a β-sandwich-like fold. The two IgAs are bent and tilted with respect to each other, forming distinct concave and convex surfaces. In SIgA, SC is bound to one face, asymmetrically contacting both IgAs and JC. The bent and tilted arrangement of complex components limits the possible positions of both sets of antigen binding fragments (Fabs) and preserves steric accessibility to receptor binding sites, likely influencing antigen binding and effector functions.

Competing Interest Statement

The authors have declared no competing interest.

Footnotes

  • The text and figures of this manuscript have been revised to better communicate results to a broad audience; no new data or analysis has been added.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-ND 4.0 International license.
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Posted October 15, 2020.
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The Structures of Secretory and Dimeric Immunoglobulin A
Sonya Kumar Bharathkar, Benjamin W. Parker, Andrey G. Malyutin, Nandan Haloi, Kathryn E. Huey-Tubman, Emad Tajkhorshid, Beth M. Stadtmueller
bioRxiv 2020.02.16.951780; doi: https://doi.org/10.1101/2020.02.16.951780
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The Structures of Secretory and Dimeric Immunoglobulin A
Sonya Kumar Bharathkar, Benjamin W. Parker, Andrey G. Malyutin, Nandan Haloi, Kathryn E. Huey-Tubman, Emad Tajkhorshid, Beth M. Stadtmueller
bioRxiv 2020.02.16.951780; doi: https://doi.org/10.1101/2020.02.16.951780

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