Asset Details
Do you wish to reserve the book?
Functional refolding of the penetration protein on a non-enveloped virus
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
Functional refolding of the penetration protein on a non-enveloped virus
Do you wish to request the book?
Functional refolding of the penetration protein on a non-enveloped virus
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
Functional refolding of the penetration protein on a non-enveloped virus
2021
Overview
A non-enveloped virus requires a membrane lesion to deliver its genome into a target cell
1
. For rotaviruses, membrane perforation is a principal function of the viral outer-layer protein, VP4
2
,
3
. 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.
Electron cryomicroscopy and cryotomography studies reveal that rotaviruses attach to a target cell through the outer-layer protein VP4, which—following cleavage—rearranges to enable perforation of the membrane and delivery of the viral genome into the host cell.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ Animals
/ Antigens, Viral - metabolism
/ Capsid Proteins - metabolism
/ Capsid Proteins - ultrastructure
/ Cell Membrane - ultrastructure
/ Genomes
/ Humanities and Social Sciences
/ Lectins
/ Lipids
/ Mutant Proteins - metabolism
/ Mutant Proteins - ultrastructure
/ Mutation
/ Proteins
/ RNA-Binding Proteins - metabolism
/ Science
/ Viral Nonstructural Proteins - metabolism
/ Virions
/ Viruses
