دورية أكاديمية
Structural and biophysical characterization of the secreted, β-helical adhesin EtpA of enterotoxigenic Escherichia coli
| العنوان: | Structural and biophysical characterization of the secreted, β-helical adhesin EtpA of enterotoxigenic Escherichia coli |
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| المؤلفون: | Ntui, Clifford Manyo, Fleckenstein, James M, Schubert, Wolf-Dieter |
| المصدر: | 2020-Current year OA Pubs |
| بيانات النشر: | Digital Commons@Becker |
| سنة النشر: | 2023 |
| المجموعة: | Washington University School of Medicine: Digital Commons@Becker |
| مصطلحات موضوعية: | Child, Humans, Preschool, Enterotoxigenic Escherichia coli, Escherichia coli Proteins, Adhesins, Bacterial, Membrane Transport Proteins, Diarrhea, Membrane Glycoproteins, ICTS (Institute of Clinical and Translational Sciences), Medicine and Health Sciences |
| الوصف: | Enterotoxigenic Escherichia coli (ETEC) is a diarrhoeal pathogen associated with high morbidity and mortality especially among young children in developing countries. At present, there is no vaccine for ETEC. One candidate vaccine antigen, EtpA, is a conserved secreted adhesin that binds to the tips of flagellae to bridge ETEC to host intestinal glycans. EtpA is exported through a Gram-negative, two-partner secretion system (TPSS, type Vb) comprised of the secreted EtpA passenger (TpsA) protein and EtpB (TpsB) transporter that is integrated into the outer bacterial membrane. TpsA proteins share a conserved, N-terminal TPS domain followed by an extensive C-terminal domain with divergent sequence repeats. Two soluble, N-terminal constructs of EtpA were prepared and analysed respectively including residues 67 to 447 (EtpA67-447) and 1 to 606 (EtpA1-606). The crystal structure of EtpA67-447 solved at 1.76 Å resolution revealed a right-handed parallel β-helix with two extra-helical hairpins and an N-terminal β-strand cap. Analyses by circular dichroism spectroscopy confirmed the β-helical fold and indicated high resistance to chemical and thermal denaturation as well as rapid refolding. A theoretical AlphaFold model of full-length EtpA largely concurs with the crystal structure adding an extended β-helical C-terminal domain after an interdomain kink. We propose that robust folding of the TPS domain upon secretion provides a template to extend the N-terminal β-helix into the C-terminal domains of TpsA proteins. |
| نوع الوثيقة: | text |
| وصف الملف: | application/pdf |
| اللغة: | unknown |
| العلاقة: | https://digitalcommons.wustl.edu/oa_4/2185Test; https://digitalcommons.wustl.edu/context/oa_4/article/3180/viewcontent/Structural_and_biophysical_PLoS_One.pdfTest |
| DOI: | 10.1371/journal.pone.0287100 |
| الإتاحة: | https://doi.org/10.1371/journal.pone.0287100Test https://digitalcommons.wustl.edu/oa_4/2185Test https://digitalcommons.wustl.edu/context/oa_4/article/3180/viewcontent/Structural_and_biophysical_PLoS_One.pdfTest |
| رقم الانضمام: | edsbas.9BA1B0E9 |
| قاعدة البيانات: | BASE |
| DOI: | 10.1371/journal.pone.0287100 |
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