Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.

Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.
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DOI:
10.1016/j.virol.2015.02.037
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发表时间:
2015-05
期刊:
影响因子:
3.7
通讯作者:
Lamb, Robert A.
Lamb, Robert A.
中科院分区:
医学3区
文献类型:
--
作者:
Bose, Sayantan;Jardetzky, Theodore S.;Lamb, Robert A.

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The Paramyxoviridae include some of the great and ubiquitous disease-causing viruses of humans and animals. In most paramyxoviruses, two viral membrane glycoproteins, fusion protein (F) and receptor binding protein (HN, H or G) mediate a concerted process of recognition of host cell surface molecules followed by fusion of viral and cellular membranes, resulting in viral nucleocapsid entry into the cytoplasm. The interactions between the F and HN, H or G viral glycoproteins and host molecules are critical in determining host range, virulence and spread of these viruses. Recently, atomic structures, together with biochemical and biophysical studies, have provided major insights into how these two viral glycoproteins successfully interact with host receptors on cellular membranes and initiate the membrane fusion process to gain entry into cells. These studies highlight the conserved core mechanisms of paramyxovirus entry that provide the fundamental basis for rational anti-viral drug design and vaccine development. New structural and functional insights into paramyxovirus entry mechanisms. Current data on paramyxovirus glycoproteins suggest a core conserved entry mechanism. Diverse mechanisms preventing premature fusion activation exist in these viruses. Precise spacio-temporal interplay between paramyxovirus glycoproteins initiate entry.
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