中性粒细胞激活蛋白介导幽门螺杆菌与高分子量唾液粘蛋白上硫酸化碳水化合物的黏附。
Neutrophil-activating protein mediates adhesion of Helicobacter pylori to sulfated carbohydrates on high-molecular-weight salivary mucin.
作者信息
Namavar F, Sparrius M, Veerman E C, Appelmelk B J, Vandenbroucke-Grauls C M
机构信息
Department of Medical Microbiology, Medical School, Vrije Universiteit, Amsterdam, The Netherlands.
出版信息
Infect Immun. 1998 Feb;66(2):444-7. doi: 10.1128/IAI.66.2.444-447.1998.
Abstract
The in vitro binding of surface-exposed material and outer membrane proteins of Helicobacter pylori to high-molecular-weight salivary mucin was studied. We identified a 16-kDa surface protein which adhered to high-molecular-weight salivary mucin. This protein binds specifically to sulfated oligosaccharide structures such as sulfo-Lewis a, sulfogalactose and sulfo-N-acetyl-glucosamine on mucin. Sequence analysis of the protein proved that it was identical to the N-terminal amino acid sequence of neutrophil-activating protein. Moreover, this adhesin was able to bind to Lewis x blood group antigen.
摘要
研究了幽门螺杆菌表面暴露物质和外膜蛋白与高分子量唾液粘蛋白的体外结合。我们鉴定出一种16 kDa的表面蛋白，它能粘附于高分子量唾液粘蛋白。该蛋白特异性结合粘蛋白上的硫酸化寡糖结构，如硫酸化路易斯a、硫酸半乳糖和硫酸N - 乙酰葡糖胺。该蛋白的序列分析证明它与中性粒细胞活化蛋白的N端氨基酸序列相同。此外，这种粘附素能够结合Lewis x血型抗原。
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