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TitleFunctional refolding of the penetration protein on a non-enveloped virus.
Journal, issue, pagesNature, Vol. 590, Issue 7847, Page 666-670, Year 2021
Publish dateJan 13, 2021
AuthorsTobias Herrmann / Raúl Torres / Eric N Salgado / Cristina Berciu / Daniel Stoddard / Daniela Nicastro / Simon Jenni / Stephen C Harrison /
PubMed AbstractA non-enveloped virus requires a membrane lesion to deliver its genome into a target cell. For rotaviruses, membrane perforation is a principal function of the viral outer-layer protein, VP4. Here we ...A non-enveloped virus requires a membrane lesion to deliver its genome into a target cell. For rotaviruses, membrane perforation is a principal function of the viral outer-layer protein, VP4. Here we describe the use of electron cryomicroscopy to determine how VP4 performs this function and show that when activated by cleavage to VP8* and VP5*, VP4 can rearrange on the virion surface from an 'upright' to a 'reversed' conformation. The reversed structure projects a previously buried 'foot' domain outwards into the membrane of the host cell to which the virion has attached. Electron cryotomograms of virus particles entering cells are consistent with this picture. Using a disulfide mutant of VP4, we have also stabilized a probable intermediate in the transition between the two conformations. Our results define molecular mechanisms for the first steps of the penetration of rotaviruses into the membranes of target cells and suggest similarities with mechanisms postulated for other viruses.
External linksNature / PubMed:33442061 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 4.3 Å
Structure data

21955

6wxe

EMDB-21955, PDB-6wxe:
Cryo-EM reconstruction of VP5*/VP8* assembly from rhesus rotavirus particles - Upright conformation
Method: EM (single particle) / Resolution: 3.4 Å

21956

6wxf

EMDB-21956, PDB-6wxf:
Cryo-EM reconstruction of VP5*/VP8* assembly from rhesus rotavirus particles - Intermediate conformation
Method: EM (single particle) / Resolution: 4.3 Å

21957

6wxg

EMDB-21957, PDB-6wxg:
Cryo-EM reconstruction of VP5*/VP8* assembly from rhesus rotavirus particles - Reversed conformation
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-CA:
Unknown entry

Source
  • rotavirus a (strain rva/monkey/united states/rrv/1975/g3p5b[3])
KeywordsVIRAL PROTEIN / Complex / non-enveloped virus / viral particle / entry / membrane-penetration / rotavirus / VP4 / VP5* / VP8* / intermediate

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