کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
3415530 1224966 2007 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Human gastric glycosphingolipids recognized by Helicobacter pylori vacuolating cytotoxin VacA
موضوعات مرتبط
علوم زیستی و بیوفناوری ایمنی شناسی و میکروب شناسی ایمونولوژی
پیش نمایش صفحه اول مقاله
Human gastric glycosphingolipids recognized by Helicobacter pylori vacuolating cytotoxin VacA
چکیده انگلیسی

Many bacterial toxins utilize cell surface glycoconjugate receptors for attachment to target cells. In the present study the potential carbohydrate binding of Helicobacter pylori vacuolating cytotoxin VacA was investigated by binding to human gastric glycosphingolipids on thin-layer chromatograms. Thereby a distinct binding of the toxin to two compounds in the non-acid glycosphingolipid fraction was detected. The VacA-binding glycosphingolipids were isolated and characterized by mass spectrometry and proton NMR as galactosylceramide (Galβ1Cer) and galabiosylceramide (Galα4Galβ1Cer). Comparison of the binding preferences of the protein to reference glycosphingolipids from other sources showed an additional recognition of glucosylceramide (Glcβ1Cer), lactosylceramide (Galβ4Glcβ1Cer) and globotriaosylceramide (Galα4Galβ4Glcβ1Cer). No binding to the glycosphingolipids recognized by the VacA holotoxin was obtained with a mutant toxin with deletion of the 37 kDa fragment of VacA (P58 molecule). Collectively our data show that the VacA cytotoxin is a glycosphingolipid binding protein, where the 37 kDa moiety is required for carbohydrate recognition. The ability to bind to short chain glycosphingolipids will position the toxin close to the cell membrane, which may facilitate toxin internalization.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Microbes and Infection - Volume 9, Issue 5, April 2007, Pages 605–614
نویسندگان
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