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STUDY ON RECEPTOR SPECIFICITY OF ANIMAL INFLUENZA VIRUSES

动物流感病毒受体特异性的研究

基本信息

批准号：
06660368
负责人：
ITO Toshihiro
金额：
$ 1.34万
依托单位：
HOKKAIDO UNIVERSITY
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1994
资助国家：
日本
起止时间：
1994 至 1995
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-06660368/
关键词：
Influenza virus Receptor specificity Sialic acid Host range Tissue tropism Hemagglutinin Interspecies transmission Inhibitor レセプター

项目摘要

The receptor specificity of the HA differs amongsinfluenza viruses : most avian influenza viruses preferentially bind the sialic acid-alpha-2,3-galactose (SAalpha2-3Gal) linkage, while human influenza viruses preferentially bind the SAalpha2,6Gal linkage on cell surface sialyloligosaccharides. To understand the molecular basis of host range restriction, we examined the distribution of sialyloligosaccharides at the replication site of influenza virus in nonhuman animals. Using linkage-specific lectins, we found that epitherial cells lining duck intestine and horse trachea contain SAalpha2,3Gal but not SAalpha2,6Gal linkages, whereas those lining pig trachea contain both. We next examined why the mutant human HA,which preferentially reconizes SAalpha2,3Gal, does not support virus replication in duck intestine. The analysis of the receptor specificity of duck and mutant human viruses suggested that the recognition of N-glycolyl sialic acid (NeuGc) is iportant for intestinal replication of … More virus in ducks. NeuGcalpha2,3 was immunologically detected in epitherial cells in duck uintestine. These findings show that the presence of the receptors in the replication site of animals corresponds tothe receptor specificity of viruses isolated from such animals.To test whether agglutination of erythrocytes from different animal species could be used to assess the receptor specificity of influenza A viruses, we determined the agglutinating activities of a range of virus strains. All equine and avian viruses agglutinated erythrocytes from all of the animal ; species tested (chickens, ducks, guinea pigs, humans, sheep, forses and cows), The human viruses agglutinated all but the horse. and cow erythrocytes. Fluorescene-activated cell sorting analysis of erythrocytes using linkage-specific lectins showed that both cow and horse crythrocytes contain a large amount of SAalpha2,3Gal- but virtually no SAalpha2,6Gal-specific lectin-reactive oligosaccharides on the cell surface, while human and chicken erythrocytes contain both types of oligosaccharides. These findings show that agglutinating assays with erythrocytes from different animal species would be useful in characterizing the receptor specificity of influenza A viruses. Less

HA的受体特异性与流感病毒不同：大多数禽流感病毒优先结合唾液酸-α-2，3-半乳糖（SA α 2 -3Gal）键，而人流感病毒优先结合细胞表面唾液酸寡糖上的SA α 2，6 Gal键。为了了解宿主范围限制的分子基础，我们研究了唾液酸寡糖在非人动物流感病毒复制位点的分布。使用连接特异性凝集素，我们发现，上皮细胞内衬鸭肠和马气管含有SA α 2，3Gal，但没有SA α 2，6 Gal连接，而内衬猪气管含有两者。我们接下来研究了为什么优先识别SA α 2，3Gal的突变型人HA不支持病毒在鸭肠中复制。对鸭病毒和突变体人病毒受体特异性的分析表明，N-羟乙酰唾液酸（NeuGc）的识别对肠复制至关重要， ...更多信息鸭体内的病毒NeuG α 2，3在鸭小肠上皮细胞中有免疫学表达。这些发现表明，在动物的复制位点的受体的存在对应于从这样的动物分离的病毒的受体特异性。为了测试是否凝集从不同的动物物种的红细胞可以用来评估甲型流感病毒的受体特异性，我们确定了一系列的病毒株的凝集活性。所有马和禽病毒均凝集所有动物的红细胞;供试种属（鸡、鸭、豚鼠、人、绵羊、牛和牛），人病毒凝集除马外的所有动物。和牛红细胞使用连接特异性凝集素对红细胞进行的双烯激活细胞分选分析表明，牛和马红细胞均含有大量的SA α 2，3Gal-，但细胞表面上几乎没有SA α 2，6 Gal-特异性凝集素反应性寡糖，而人和鸡红细胞含有两种类型的寡糖。这些发现表明，来自不同动物种属的红细胞凝集试验将有助于表征甲型流感病毒的受体特异性。少