Rhabdovirus matrix protein structures reveal a novel mode of self-association.
The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from La...
Saved in:
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2008-12-01
|
| Series: | PLoS Pathogens |
| Online Access: | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000251&type=printable |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850240557364805632 |
|---|---|
| author | Stephen C Graham René Assenberg Olivier Delmas Anil Verma Alireza Gholami Chiraz Talbi Raymond J Owens David I Stuart Jonathan M Grimes Hervé Bourhy |
| author_facet | Stephen C Graham René Assenberg Olivier Delmas Anil Verma Alireza Gholami Chiraz Talbi Raymond J Owens David I Stuart Jonathan M Grimes Hervé Bourhy |
| author_sort | Stephen C Graham |
| collection | DOAJ |
| description | The matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins. |
| format | Article |
| id | doaj-art-3ddadddc001147da98069bdb71b8804a |
| institution | OA Journals |
| issn | 1553-7366 1553-7374 |
| language | English |
| publishDate | 2008-12-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Pathogens |
| spelling | doaj-art-3ddadddc001147da98069bdb71b8804a2025-08-20T02:00:50ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742008-12-01412e100025110.1371/journal.ppat.1000251Rhabdovirus matrix protein structures reveal a novel mode of self-association.Stephen C GrahamRené AssenbergOlivier DelmasAnil VermaAlireza GholamiChiraz TalbiRaymond J OwensDavid I StuartJonathan M GrimesHervé BourhyThe matrix (M) proteins of rhabdoviruses are multifunctional proteins essential for virus maturation and budding that also regulate the expression of viral and host proteins. We have solved the structures of M from the vesicular stomatitis virus serotype New Jersey (genus: Vesiculovirus) and from Lagos bat virus (genus: Lyssavirus), revealing that both share a common fold despite sharing no identifiable sequence homology. Strikingly, in both structures a stretch of residues from the otherwise-disordered N terminus of a crystallographically adjacent molecule is observed binding to a hydrophobic cavity on the surface of the protein, thereby forming non-covalent linear polymers of M in the crystals. While the overall topology of the interaction is conserved between the two structures, the molecular details of the interactions are completely different. The observed interactions provide a compelling model for the flexible self-assembly of the matrix protein during virion morphogenesis and may also modulate interactions with host proteins.https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000251&type=printable |
| spellingShingle | Stephen C Graham René Assenberg Olivier Delmas Anil Verma Alireza Gholami Chiraz Talbi Raymond J Owens David I Stuart Jonathan M Grimes Hervé Bourhy Rhabdovirus matrix protein structures reveal a novel mode of self-association. PLoS Pathogens |
| title | Rhabdovirus matrix protein structures reveal a novel mode of self-association. |
| title_full | Rhabdovirus matrix protein structures reveal a novel mode of self-association. |
| title_fullStr | Rhabdovirus matrix protein structures reveal a novel mode of self-association. |
| title_full_unstemmed | Rhabdovirus matrix protein structures reveal a novel mode of self-association. |
| title_short | Rhabdovirus matrix protein structures reveal a novel mode of self-association. |
| title_sort | rhabdovirus matrix protein structures reveal a novel mode of self association |
| url | https://journals.plos.org/plospathogens/article/file?id=10.1371/journal.ppat.1000251&type=printable |
| work_keys_str_mv | AT stephencgraham rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT reneassenberg rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT olivierdelmas rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT anilverma rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT alirezagholami rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT chiraztalbi rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT raymondjowens rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT davidistuart rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT jonathanmgrimes rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation AT hervebourhy rhabdovirusmatrixproteinstructuresrevealanovelmodeofselfassociation |