New world bats harbor diverse influenza A viruses.

New world bats harbor diverse influenza A viruses.
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DOI:
10.1371/journal.ppat.1003657
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发表时间:
2013
期刊:
影响因子:
6.7
通讯作者:
Donis RO
Donis RO
中科院分区:
医学1区
文献类型:
--
作者:
Tong S;Zhu X;Li Y;Shi M;Zhang J;Bourgeois M;Yang H;Chen X;Recuenco S;Gomez J;Chen LM;Johnson A;Tao Y;Dreyfus C;Yu W;McBride R;Carney PJ;Gilbert AT;Chang J;Guo Z;Davis CT;Paulson JC;Stevens J;Rupprecht CE;Holmes EC;Wilson IA;Donis RO

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水禽携带不同的甲型流感病毒,是自然界中的主要病毒库。最近在中美洲果蝠身上发现了一种新的H17N10亚型流感病毒,这表明其他新大陆物种可能同样携带不同的流感病毒。利用共识简并RT-PCR方法,在秘鲁的平面果蝠(Artibeus Planirostris)体内分离到一种新的甲型流感病毒,命名为H18N11。重组H18蛋白的血清学研究表明,几种秘鲁蝙蝠都感染了这种病毒。系统发育分析表明,在某些基因片段中,新世界蝙蝠的流感病毒遗传多样性比所有其他哺乳动物和鸟类的总和还要多,这表明宿主与病毒之间存在着长期的联系。血凝素和神经氨酸酶的结构和功能分析表明,唾液酸既不是病毒附着的配体,也不是释放的底物,提示甲型流感病毒附着和激活膜融合进入宿主细胞的独特模式。综上所述,这些发现表明,蝙蝠是一个潜在的重要和可能的古老的储存库,为不同的流感病毒库。此前的研究表明,一种新的甲型流感病毒(H17N10)正在危地马拉(中美洲)的果蝠中传播。在这里,我们调查了南美洲的蝙蝠物种中是否存在类似的病毒。对从秘鲁亚马逊雨林地区采集的蝙蝠的直肠拭子进行的分析发现,另一种来自蝙蝠的新甲型流感病毒在系统发育上与危地马拉发现的病毒不同。编码平面果蝠新病毒表面蛋白的基因被命名为新亚型H18N11。对几种秘鲁蝙蝠的血液样本进行的血清学测试表明,表面蛋白抗体的流行率很高。系统发育分析表明,来自中美洲和南美洲的蝙蝠种群在某些基因片段上保持着与所有其他哺乳动物和鸟类的总和一样多的流感病毒遗传多样性。血凝素和神经氨酸酶蛋白的晶体结构表明,唾液酸既不是病毒附着的受体,也不是释放的底物,这可能是甲型流感病毒附着和激活膜融合进入宿主细胞的新机制。总而言之,我们的发现表明,蝙蝠是流感病毒的潜在重要宿主。
Aquatic birds harbor diverse influenza A viruses and are a major viral reservoir in nature. The recent discovery of influenza viruses of a new H17N10 subtype in Central American fruit bats suggests that other New World species may similarly carry divergent influenza viruses. Using consensus degenerate RT-PCR, we identified a novel influenza A virus, designated as H18N11, in a flat-faced fruit bat (Artibeus planirostris) from Peru. Serologic studies with the recombinant H18 protein indicated that several Peruvian bat species were infected by this virus. Phylogenetic analyses demonstrate that, in some gene segments, New World bats harbor more influenza virus genetic diversity than all other mammalian and avian species combined, indicative of a long-standing host-virus association. Structural and functional analyses of the hemagglutinin and neuraminidase indicate that sialic acid is not a ligand for virus attachment nor a substrate for release, suggesting a unique mode of influenza A virus attachment and activation of membrane fusion for entry into host cells. Taken together, these findings indicate that bats constitute a potentially important and likely ancient reservoir for a diverse pool of influenza viruses. Previous studies indicated that a novel influenza A virus (H17N10) was circulating in fruit bats from Guatemala (Central America). Herein, we investigated whether similar viruses are present in bat species from South America. Analysis of rectal swabs from bats sampled in the Amazon rainforest region of Peru identified another new influenza A virus from bats that is phylogenetically distinct from the one identified in Guatemala. The genes that encode the surface proteins of the new virus from the flat-faced fruit bat were designated as new subtype H18N11. Serologic testing of blood samples from several species of Peruvian bats indicated a high prevalence of antibodies to the surface proteins. Phylogenetic analyses demonstrate that bat populations from Central and South America maintain as much influenza virus genetic diversity in some gene segments as all other mammalian and avian species combined. The crystal structures of the hemagglutinin and neuraminidase proteins indicate that sialic acid is not a receptor for virus attachment nor a substrate for release, suggesting a novel mechanism of influenza A virus attachment and activation of membrane fusion for entry into host cells. In summary, our findings indicate that bats constitute a potentially important reservoir for influenza viruses.
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