دورية أكاديمية

Shiga toxin 1 and ricin A chain bind to human polymorphonuclear leukocytes through a common receptor

التفاصيل البيبلوغرافية
العنوان: Shiga toxin 1 and ricin A chain bind to human polymorphonuclear leukocytes through a common receptor
المؤلفون: Arfilli, Valentina, Carnicelli, Domenica, Rocchi, Laura, Ricci, Francesca, Pagliaro, Pasqualepaolo, Tazzari, Pier Luigi, Brigotti, Maurizio
المساهمون: Alma Mater Studiorum Università di Bologna = University of Bologna (UNIBO)
المصدر: ISSN: 0264-6021.
بيانات النشر: HAL CCSD
Portland Press
سنة النشر: 2010
المجموعة: Archive ouverte HAL (Hyper Article en Ligne, CCSD - Centre pour la Communication Scientifique Directe)
مصطلحات موضوعية: Life Sciences
الوصف: International audience ; The main cause of acute renal failure in children is HUS (hemolytic uremic syndrome), a consequence of intestinal infections with Escherichia coli strains producing Stx (Shiga toxins). Stx released in the gut by the non-invasive bacteria reach the blood stream and are targeted to cerebral and renal endothelium triggering HUS. PMN (polymorphonuclear leukocytes) seem involved in Stx delivery through an unidentified membrane receptor (Kd = 10-8 M; 2 x 105 binding sites) which does not allow internalization. Some experts in the field have defined the interaction Stx/PMN as non-specific and of little biological significance. Here, we show that the A chain of ricin, the well known plant RIP (ribosome-inactivating protein), interacts with PMN (Kd = 10-9 M; 2 x 105 binding sites) competing for the same receptor that recognizes Stx, whereas diphtheria toxin and several agonists of Toll-like receptors or the mannose-receptor were ineffective. No toxic effects of ricin A chain on PMN were observed, as assessed by measuring protein synthesis and the rate of spontaneous apoptosis of leukocytes. Moreover, two single-chain RIPs (gelonin, saporin S6) showed the same competing effect. Thus, RIPs and Stx1 share structural similarities, the same enzymatic activity and a common receptor on PMN. These observations reveal that the Stx/PMN interaction is specific confirming that PMN recognize molecular patterns common to different foreign molecules.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: hal-00529103; https://hal.science/hal-00529103Test; https://hal.science/hal-00529103/documentTest; https://hal.science/hal-00529103/file/PEER_stage2_10.1042%252FBJ20100455.pdfTest
DOI: 10.1042/BJ20100455
الإتاحة: https://doi.org/10.1042/BJ20100455Test
https://hal.science/hal-00529103Test
https://hal.science/hal-00529103/documentTest
https://hal.science/hal-00529103/file/PEER_stage2_10.1042%252FBJ20100455.pdfTest
حقوق: info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.EA7ADABD
قاعدة البيانات: BASE