Abstract：
:Enveloped viruses enter cells by inducing fusion of viral and cellular membranes, a process catalyzed by a specialized membrane-fusion protein expressed on their surface. This review focuses on recent structural studies of viral fusion proteins with an emphasis on their metastable prefusion form and on interactions with neutralizing antibodies. The fusion glycoproteins have been difficult to study because they are present in a labile, metastable form at the surface of infectious virions. Such metastability is a functional requirement, allowing these proteins to refold into a lower energy conformation while transferring the difference in energy to catalyze the membrane fusion reaction. Structural studies have shown that stable immunogens presenting the same antigenic sites as the labile wild-type proteins efficiently elicit potently neutralizing antibodies, providing a framework with which to engineer the antigens for stability, as well as identifying key vulnerability sites that can be used in next-generation subunit vaccine design.
journal_name
Celljournal_title
Cellauthors
Rey FA,Lok SMdoi
10.1016/j.cell.2018.02.054subject
Has Abstractpub_date
2018-03-08 00:00:00pages
1319-1334issue
6eissn
0092-8674issn
1097-4172pii
S0092-8674(18)30231-9journal_volume
172pub_type
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