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Cryo-EM structures of Trypanosoma brucei gambiense ISG65 with human complement C3 and C3b and their roles in alternative pathway restriction.

التفاصيل البيبلوغرافية
العنوان: Cryo-EM structures of Trypanosoma brucei gambiense ISG65 with human complement C3 and C3b and their roles in alternative pathway restriction.
المؤلفون: Sülzen H; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic.; Faculty of Science, Charles University, Albertov 6, 12800, Prague 2, Czech Republic., Began J; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic.; Department of Immunobiology, University of Lausanne, Chemin des Boveresses 155, 1066, Epalinges, Switzerland., Dhillon A; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic., Kereïche S; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic.; First Faculty of Medicine, Charles University, Albertov 4, 12800, Prague, Czech Republic., Pompach P; Institute of Biotechnology of the Czech Academy of Sciences, 25250, Vestec, Czech Republic., Votrubova J; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic., Zahedifard F; Department of Parasitology, Faculty of Science, Charles University Prague, Biocev, 25250, Vestec, Czech Republic., Šubrtova A; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic., Šafner M; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic., Hubalek M; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic., Thompson M; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic.; University of Antwerp, Antwerp, Belgium.; Agidens, Industrial Machinery Manufacturing, Zwijndrecht, Antwerp, Belgium., Zoltner M; Department of Parasitology, Faculty of Science, Charles University Prague, Biocev, 25250, Vestec, Czech Republic., Zoll S; Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences, Flemingovo namesti 542/2, 16000, Prague, Czech Republic. sebastian.zoll@uochb.cas.cz.
المصدر: Nature communications [Nat Commun] 2023 Apr 27; Vol. 14 (1), pp. 2403. Date of Electronic Publication: 2023 Apr 27.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Complement C3*/metabolism , Trypanosoma brucei gambiense*/metabolism, Humans ; Complement Activation ; Complement C3-C5 Convertases/metabolism ; Complement C5/metabolism ; Complement Pathway, Alternative ; Cryoelectron Microscopy ; Protein Binding
مستخلص: African Trypanosomes have developed elaborate mechanisms to escape the adaptive immune response, but little is known about complement evasion particularly at the early stage of infection. Here we show that ISG65 of the human-infective parasite Trypanosoma brucei gambiense is a receptor for human complement factor C3 and its activation fragments and that it takes over a role in selective inhibition of the alternative pathway C5 convertase and thus abrogation of the terminal pathway. No deposition of C4b, as part of the classical and lectin pathway convertases, was detected on trypanosomes. We present the cryo-electron microscopy (EM) structures of native C3 and C3b in complex with ISG65 which reveal a set of modes of complement interaction. Based on these findings, we propose a model for receptor-ligand interactions as they occur at the plasma membrane of blood-stage trypanosomes and may facilitate innate immune escape of the parasite.
(© 2023. The Author(s).)
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المشرفين على المادة: 0 (Complement C3)
EC 3.4.21.- (Complement C3-C5 Convertases)
0 (Complement C5)
0 (C3 protein, human)
تواريخ الأحداث: Date Created: 20230427 Date Completed: 20230508 Latest Revision: 20230508
رمز التحديث: 20230509
مُعرف محوري في PubMed: PMC10140031
DOI: 10.1038/s41467-023-37988-7
PMID: 37105991
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-023-37988-7