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目的 HpaA是幽门螺杆菌(Helicobacter pylori)的主要粘附因子,参与幽门螺杆菌在人胃黏膜上的定植过程。特异性阻断HpaA与人胃上皮细胞的粘附,可能成为阻断Hp感染的新方法,从而弥补常规治疗中出现的毒副作用大、耐药性等问题。方法以人工合成的HpaA主要结构域KRTIQKKRTIQK多肽为靶标,应用噬菌体随机十二肽库进行筛选,经过3轮淘选,提取阳性噬菌体克隆ssDNA,测序并进行序列分析。通过相应的分析软件对亲和肽进行分析比对。结果通过多次筛选与富集,获得了与HpaA相互作用的功能分子ASPH、EGR2。运用软件模拟发现ASPH、EGR2均能与HpaA分子高度吻合。结论通过噬菌体肽库技术筛选出与幽门螺杆菌主要粘附分子HpaA相互作用的2个功能分子,可能参与幽门螺杆菌的定植与致病过程,为进一步研究幽门螺杆菌在人胃内致病的机制和多肽治疗方法提供了依据。
Objective HpaA is the main adhesion factor of Helicobacter pylori and participates in the colonization of human gastric mucosa by Helicobacter pylori. Specific blocking of HpaA adhesion to human gastric epithelial cells may become a new way to block Hp infection and thus make up for the conventional treatment of toxic side effects, resistance and other issues. Methods Targeting KRTIQKKTIRQQ peptide, a major synthetic domain of HpaA, was screened by phage display randomized 12-mer peptide library. After 3 rounds of panning, positive phage cloned ssDNA was extracted, sequenced and sequenced. Affinity peptides were analyzed and aligned by the corresponding analysis software. Results After screening and enriching for many times, functional molecules ASPH and EGR2 interacting with HpaA were obtained. Using software simulation found that ASPH, EGR2 and HpaA molecules are highly consistent. Conclusion Two functional molecules interacting with HpaA, a major adhesion molecule of Helicobacter pylori, are screened by phage peptide library technology, which may be involved in the colonization and pathogenicity of Helicobacter pylori. In order to further study the pathogenicity of Helicobacter pylori in human stomach Mechanism and peptide treatment provided the basis.