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作 者:刘尚杰 郑洲 陆国永 乔杰 章跃陵 LIU Shang jie;ZHENG Zhou;LUO Guoyong;QIAO Jie;ZHANG Yueling(Department of Biology, College of Science, Shantou University, Shantou 515063, Guangdong, China)
机构地区:[1]汕头大学理学院生物学系广东省海洋生物技术重点实验室,广东汕头515063
出 处:《汕头大学学报(自然科学版)》2017年第4期3-9,共7页Journal of Shantou University:Natural Science Edition
基 金:国家自然科学基金项目(31672689);广东省自然科学基金重点项目(2017A030311032);广东省高等学校重大科研项目培育计划类项目(2014GKXM043)
摘 要:目前研究证实,人血红蛋白不仅具有输氧功能,而且具有酚氧化酶活性、抑菌活性等非特异性免疫学活性.本课题运用生物信息学技术对人血红蛋白与凝集素进行同源性分析,结果显示人血红蛋白α、β亚基与人、牛、大鼠、家鼠、非洲爪蟾、斑马鱼凝集素均存在同源区域,同源性大小为20%~46.7%.进而采用玻片凝集法与糖抑制实验探索人血红蛋白的凝集活性,结果表明人血红蛋白对副溶血弧菌等6种细菌均存在明显的凝集活性,其凝集比活为3.9~15.6 mg/L,且α-D-葡萄糖、麦芽糖、α-D-乳糖、D-半乳糖、D-山梨糖、D-木糖和N-乙酰神经氨酸可以部分或全部抑制人血红蛋白的细菌凝集活性.由此说明,人血红蛋白确实具有凝集活性,所获研究结果为进一步探索人血红蛋白的免疫学活性及其作用机理奠定了良好的基础.Hemoglobin is an important oxygen carrier in erythrocytes. However, recent reports have demonstrated that human hemoglobin has some nonspecific immunological functions including phenoloxidase and antimicrobial activity. In the present study, the homology between human hemoglobin and agglutinin was analyzed by bioinformatics. The results showed that the αand β chains of human hemoglobin possessed 20%~46.7% homology with lectin from Homo sapiens, Bos taurus, Rattus norvegicus, Mus musculus, Xenopus(Silurana)tropicalis and Danio rerio. When six bacteria including Vibrio parahaemolyticus, Vibrio alginolyticus, Vibrio fluvialis, Stphylococcus aureus, Escherichia coli K12 and beta streptococcus were reacted with human hemoglobin, the results showed that human hemoglobin could aggregate with all these bacteria, with agglutinative activities in the range 3.9~15.6 mg/L. Moreover, saccharide effect on human hemoglobin was further analyzed using nine saccharides includin g α-D-glucofuranose,Maltose, α-D-lactose, D-galactose, D-sorbin, D-xylose and N-acetylneuraminic acid. The results indicated that the agglutinative activity of human hemoglobin could be partly or completely inhibited by these monosaccharides or oligosaccharides. Taken together, these results suggested that human hemoglobin could also act as an agglutinin in nonspecific immune response, hence,these results will lay the foundation to further explore the immunological functions of human hemoglobin and its mechanism.
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