Biological properties of mengovirus: characterization of avirulent, hemagglutination-defective mutants.

Biological properties of mengovirus: characterization of avirulent, hemagglutination-defective mutants.
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DOI:
10.1007/bf01313892
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发表时间:
1987
影响因子:
2.7
通讯作者:
Bond CW
Bond CW
中科院分区:
医学4区
文献类型:
--
作者:
Anderson K;Bond CW

文献摘要

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将两种孟戈病毒突变体 205 和 280 的生物学特性与野生型病毒进行了比较。这些突变体在小鼠体内表现出斑块形态、血凝和毒力的改变,但对温度不敏感。孟戈病毒对人红细胞的凝集依赖于红细胞表面唾液酸的存在;然而,游离唾液酸未能抑制血凝。血型糖蛋白是人红细胞膜的主要唾液酸糖蛋白,对野生型病毒表现出受体特异性,但对突变体 205 或 280 不具有受体特异性。交联研究表明,血型糖蛋白对 α (1 D) 结构蛋白表现出结合特异性。在颅内 (IC) 和腹膜内 (IP) 感染的小鼠中,野生型孟戈病毒的 LD50 滴度分别为 7 和 1500 噬斑形成单位 (PFU)。然而,用106或107 PFU的突变体205或280感染IC或IP的小鼠没有表现出表明病毒感染的症状。从感染突变体 205 的小鼠大脑中分离出回复体,但未从感染突变体 280 的小鼠脑中分离出回复体。回复体的生物学特征表明血凝和毒力可能是表型相关的特征。
Biological properties of two mengovirus mutants, 205 and 280, were compared to those of wild-type virus. The mutants exhibited alterations in plaque morphology, hemagglutination, and virulence in mice, but were not temperature-sensitive. Agglutination of human erythrocytes by mengovirus was dependent on the presence of sialic acid on the erythrocyte surface; however, free sialic acid failed to inhibit hemagglutination. Glycophorin, the major sialoglycoprotein of human erythrocyte membranes, exhibited receptor specificity for wild-type virus, but not for mutants 205 or 280. Cross-linking studies indicated that glycophorin exhibited binding specificity for the alpha (1 D) structural protein. The LD50 titers for wild-type mengovirus were 7 and 1500 plaque forming units (PFU) in mice infected intracranially (IC) and intraperitoneally (IP), respectively. However, mice infected IC or IP with 106 or 107 PFU of mutant 205 or 280 did not exhibit symptoms indicative of virus infection. Revertants were isolated from the brains of mice infected with mutant 205, but not from the brains of mice infected with mutant 280. The biological characterization of the revertants indicated that hemagglutination and virulence may be phenotypically-linked traits.