Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins
Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
The human metapneumovirus (hMPV) fusion (F) protein is essential for viral entry and is a key target of neutralizing antibodies and vaccine development. The prefusion conformation is thought to be the optimal vaccine antigen, but previously described prefusion F proteins expressed poorly and were not well stabilized. Here, we use structures of hMPV...
Alternative Titles
Full title
Structure-based design of prefusion-stabilized human metapneumovirus fusion proteins
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_1881314158b644b685989d8847d72882
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_1881314158b644b685989d8847d72882
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-022-28931-3
