دورية أكاديمية
Structural and Biochemical Requirements for Secretory Component Interactions with Dimeric IgA.
| العنوان: | Structural and Biochemical Requirements for Secretory Component Interactions with Dimeric IgA. |
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| المؤلفون: | Kumar Bharathkar S; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL., Stadtmueller BM; Department of Biochemistry, University of Illinois Urbana-Champaign, Urbana, IL.; Department of Biomedical and Translational Sciences, Carle Illinois College of Medicine, University of Illinois Urbana-Champaign, Urbana, IL.; Carl R. Woese Institute of Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL. |
| المصدر: | Journal of immunology (Baltimore, Md. : 1950) [J Immunol] 2024 Jul 15; Vol. 213 (2), pp. 226-234. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, N.I.H., Extramural |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Association of Immunologists Country of Publication: United States NLM ID: 2985117R Publication Model: Print Cited Medium: Internet ISSN: 1550-6606 (Electronic) Linking ISSN: 00221767 NLM ISO Abbreviation: J Immunol Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Bethesda, MD : American Association of Immunologists Original Publication: Baltimore : Williams & Wilkins, c1950- |
| مواضيع طبية MeSH: | Immunoglobulin A, Secretory*/immunology , Immunoglobulin A, Secretory*/metabolism , Secretory Component*/metabolism , Secretory Component*/immunology , Receptors, Polymeric Immunoglobulin*/metabolism , Receptors, Polymeric Immunoglobulin*/immunology , Receptors, Polymeric Immunoglobulin*/genetics, Animals ; Mice ; Protein Binding ; Protein Multimerization ; Humans ; Immunoglobulin A/immunology ; Immunoglobulin A/metabolism ; Protein Conformation |
| مستخلص: | Secretory (S) IgA is the predominant mucosal Ab that protects host epithelial barriers and promotes microbial homeostasis. SIgA production occurs when plasma cells assemble two copies of monomeric IgA and one joining chain (JC) to form dimeric (d) IgA, which is bound by the polymeric Ig receptor (pIgR) on the basolateral surface of epithelial cells and transcytosed to the apical surface. There, pIgR is proteolytically cleaved, releasing SIgA, a complex of the dIgA and the pIgR ectodomain, called the secretory component (SC). The pIgR's five Ig-like domains (D1-D5) undergo a conformational change upon binding dIgA, ultimately contacting four IgA H chains and the JC in SIgA. In this study, we report structure-based mutational analysis combined with surface plasmon resonance binding assays that identify key residues in mouse SC D1 and D3 that mediate SC binding to dIgA. Residues in D1 CDR3 are likely to initiate binding, whereas residues that stabilize the D1-D3 interface are likely to promote the conformational change and stabilize the final SIgA structure. Additionally, we find that the JC's three C-terminal residues play a limited role in dIgA assembly but a significant role in pIgR/SC binding to dIgA. Together, these results inform models for the intricate mechanisms underlying IgA transport across epithelia and functions in the mucosa. (Copyright © 2024 by The American Association of Immunologists, Inc.) |
| التعليقات: | Update of: bioRxiv. 2024 Apr 17:2023.11.09.566401. doi: 10.1101/2023.11.09.566401. (PMID: 38014291) |
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| معلومات مُعتمدة: | R01 AI165570 United States AI NIAID NIH HHS; R01AI165570 HHS | NIH | NIAID | Division of Intramural Research (DIR, NIAID) |
| المشرفين على المادة: | 0 (Immunoglobulin A, Secretory) 0 (Secretory Component) 0 (Receptors, Polymeric Immunoglobulin) 0 (Immunoglobulin A) |
| تواريخ الأحداث: | Date Created: 20240529 Date Completed: 20240701 Latest Revision: 20240711 |
| رمز التحديث: | 20240711 |
| مُعرف محوري في PubMed: | PMC11233122 |
| DOI: | 10.4049/jimmunol.2300717 |
| PMID: | 38809110 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1550-6606 |
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| DOI: | 10.4049/jimmunol.2300717 |