Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/23116
Title: A novel protein from helicobacter pylori with a potential role in gastroduodenal diseases
Authors: XU FEISHAN
Keywords: Helicobacter pylori, mucin, mucin binding protein (MBP), peptidyl-arginine deiminase (PAD), gastric epithelium, gastroduodenal diseases,
Issue Date: 21-May-2007
Source: XU FEISHAN (2007-05-21). A novel protein from helicobacter pylori with a potential role in gastroduodenal diseases. ScholarBank@NUS Repository.
Abstract: Helicobacter pylori, the gastric pathogen, interacts with gastric mucus layer before colonizing the gastric epithelium. However, such interaction has not been well established. In this study, a novel H. pylori protein (HP0049) has been identified as a mucin binding protein (MBP) as it binds to bovine submaxillary and porcine gastric mucins. The corresponding mbp gene was cloned, expressed, recombinant protein (rMBP) purified and antibody raised. The mucin binding ability of rMBP was inhibited upon pretreatment with neuraminidase and Na-metaperiodate indicating that carbohydrates and sialic acid mediate in the binding of MBP to mucins. Transmission electron microscopy demonstrates that MBP localizes in the cytoplasm close to the cell membrane. Interestingly, sequence analysis revealed MBP to be a potential new member of peptidyl-arginine deiminase (PAD) family as rMBP also displayed PAD activity. ELISA results show significantly higher antibody level against rMBP in patients with non-ulcer dyspepsia than patients with peptic ulcer disease (p = 0.002). The findings show that MBP with distinctive PAD activity may play a potential role in H. pylori related gastroduodenal diseases.
URI: http://scholarbank.nus.edu.sg/handle/10635/23116
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