دورية أكاديمية
أعرض في EDS

Alpha hemolysin of E. coli induces hemolysis of human erythrocytes independently of toxin interaction with membrane proteins.

التفاصيل البيبلوغرافية
العنوان: Alpha hemolysin of E. coli induces hemolysis of human erythrocytes independently of toxin interaction with membrane proteins.
المؤلفون: Cané L; Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CCT- La Plata, CONICET. Facultad de Ciencias Médicas. Universidad Nacional de La Plata, Argentina., Saffioti NA; Instituto de Química y Fisico-Química Biológicas (IQUIFIB) 'Prof. Alejandro C. Paladini', Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina; Instituto de Nanosistemas, Universidad de General San Martín, Avenida 25 de Mayo 1021, San Martín, Buenos Aires, Argentina., Genetet S; Université Paris Cité and Université des Antilles, INSERM, BIGR, F-75015, Paris, France., Daza Millone MA; Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas (INIFTA), CCT- La Plata, CONICET. Universidad Nacional de La Plata, Sucursal 4 Casilla de Correo 16, 1900, La Plata, Argentina., Ostuni MA; Université Paris Cité and Université des Antilles, INSERM, BIGR, F-75015, Paris, France., Schwarzbaum PJ; Instituto de Química y Fisico-Química Biológicas (IQUIFIB) 'Prof. Alejandro C. Paladini', Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, Buenos Aires, Argentina., Mouro-Chanteloup I; Université Paris Cité and Université des Antilles, INSERM, BIGR, F-75015, Paris, France., Herlax V; Instituto de Investigaciones Bioquímicas de La Plata (INIBIOLP), CCT- La Plata, CONICET. Facultad de Ciencias Médicas. Universidad Nacional de La Plata, Argentina. Electronic address: vherlax@med.unlp.edu.ar.
المصدر: Biochimie [Biochimie] 2024 Jan; Vol. 216, pp. 3-13. Date of Electronic Publication: 2023 Oct 13.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Editions Scientifiques Elsevier Country of Publication: France NLM ID: 1264604 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1638-6183 (Electronic) Linking ISSN: 03009084 NLM ISO Abbreviation: Biochimie Subsets: MEDLINE
أسماء مطبوعة: Publication: Paris : Editions Scientifiques Elsevier
Original Publication: Paris.
مواضيع طبية MeSH: Escherichia coli Proteins*/metabolism , Toxins, Biological*/metabolism, Humans ; Escherichia coli/metabolism ; Hemolysin Proteins/pharmacology ; Hemolysin Proteins/chemistry ; Hemolysin Proteins/metabolism ; Membrane Proteins/metabolism ; Glycophorins/metabolism ; Glycophorins/pharmacology ; Hemolysis ; Erythrocytes/metabolism
مستخلص: Alpha hemolysin (HlyA) is a hemolytic and cytotoxic protein secreted by uropathogenic strains of E. coli. The role of glycophorins (GPs) as putative receptors for HlyA binding to red blood cells (RBCs) has been debated. Experiments using anti-GPA/GPB antibodies and a GPA-specific epitope nanobody to block HlyA-GP binding on hRBCs, showed no effect on hemolytic activity. Similarly, the hemolysis induced by HlyA remained unaffected when hRBCs from a GPA null /GPB null variant were used. Surface Plasmon Resonance experiments revealed similar values of the dissociation constant between GPA and either HlyA, ProHlyA (inactive protoxin), HlyAΔ914-936 (mutant of HlyA lacking the binding domain to GPA) or human serum albumin, indicating that the binding between the proteins and GPA is not specific. Although far Western blot followed by mass spectroscopy analyses suggested that HlyA interacts with Band 3 and spectrins, hemolytic experiments on spectrin-depleted hRBCs and spherocytes, indicated these proteins do not mediate the hemolytic process. Our results unequivocally demonstrate that neither glycophorins, nor Band 3 and spectrins mediate the cytotoxic activity of HlyA on hRBCs, thereby challenging the HlyA-receptor hypothesis. This finding holds significant relevance for the design of anti-toxin therapeutic strategies, particularly in light of the growing antibiotic resistance exhibited by bacteria.
Competing Interests: Declaration of competing interest The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
(Copyright © 2023 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)
فهرسة مساهمة: Keywords: Band 3; GPA(null)/GPB(null); Glycophorins; RTX toxins; Spectrins; UPEC
المشرفين على المادة: 0 (Escherichia coli Proteins)
0 (Hemolysin Proteins)
0 (Membrane Proteins)
0 (Glycophorins)
0 (Toxins, Biological)
تواريخ الأحداث: Date Created: 20231011 Date Completed: 20240101 Latest Revision: 20240101
رمز التحديث: 20240102
DOI: 10.1016/j.biochi.2023.10.008
PMID: 37820991
قاعدة البيانات: MEDLINE
الوصف
تدمد:1638-6183
DOI:10.1016/j.biochi.2023.10.008