[{"oa":1,"language":[{"iso":"eng"}],"publication_identifier":{"eissn":["23795042"]},"article_number":"e01024-20","publication":"mSphere","day":"14","doi":"10.1128/mSphere.01024-20","user_id":"4359f0d1-fa6c-11eb-b949-802e58b17ae8","title":"Oligomerization and cell egress controlled by two microdomains of canine distemper virus matrix protein","pmid":1,"acknowledgement":"This work was supported by the Swiss National Science Foundation (referencenumber 310030_173185 to P. P.).","year":"2021","department":[{"_id":"Bio"}],"article_processing_charge":"No","citation":{"apa":"Gast, M., Kadzioch, N. P., Milius, D., Origgi, F., &#38; Plattet, P. (2021). Oligomerization and cell egress controlled by two microdomains of canine distemper virus matrix protein. <i>MSphere</i>. American Society for Microbiology. <a href=\"https://doi.org/10.1128/mSphere.01024-20\">https://doi.org/10.1128/mSphere.01024-20</a>","ieee":"M. Gast, N. P. Kadzioch, D. Milius, F. Origgi, and P. Plattet, “Oligomerization and cell egress controlled by two microdomains of canine distemper virus matrix protein,” <i>mSphere</i>, vol. 6, no. 2. American Society for Microbiology, 2021.","chicago":"Gast, Matthieu, Nicole P. Kadzioch, Doreen Milius, Francesco Origgi, and Philippe Plattet. “Oligomerization and Cell Egress Controlled by Two Microdomains of Canine Distemper Virus Matrix Protein.” <i>MSphere</i>. American Society for Microbiology, 2021. <a href=\"https://doi.org/10.1128/mSphere.01024-20\">https://doi.org/10.1128/mSphere.01024-20</a>.","short":"M. Gast, N.P. Kadzioch, D. Milius, F. Origgi, P. Plattet, MSphere 6 (2021).","mla":"Gast, Matthieu, et al. “Oligomerization and Cell Egress Controlled by Two Microdomains of Canine Distemper Virus Matrix Protein.” <i>MSphere</i>, vol. 6, no. 2, e01024-20, American Society for Microbiology, 2021, doi:<a href=\"https://doi.org/10.1128/mSphere.01024-20\">10.1128/mSphere.01024-20</a>.","ista":"Gast M, Kadzioch NP, Milius D, Origgi F, Plattet P. 2021. Oligomerization and cell egress controlled by two microdomains of canine distemper virus matrix protein. mSphere. 6(2), e01024-20.","ama":"Gast M, Kadzioch NP, Milius D, Origgi F, Plattet P. Oligomerization and cell egress controlled by two microdomains of canine distemper virus matrix protein. <i>mSphere</i>. 2021;6(2). doi:<a href=\"https://doi.org/10.1128/mSphere.01024-20\">10.1128/mSphere.01024-20</a>"},"publisher":"American Society for Microbiology","has_accepted_license":"1","type":"journal_article","tmp":{"legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","short":"CC BY (4.0)","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"file":[{"relation":"main_file","success":1,"file_size":3379349,"date_updated":"2021-05-04T12:41:38Z","content_type":"application/pdf","file_name":"2021_mSphere_Gast.pdf","date_created":"2021-05-04T12:41:38Z","access_level":"open_access","creator":"kschuh","checksum":"310748d140c8838335c1314431095898","file_id":"9370"}],"date_updated":"2023-08-08T13:26:12Z","oa_version":"Published Version","isi":1,"ddc":["570"],"month":"04","status":"public","external_id":{"pmid":["33853875"],"isi":["000663823400025"]},"publication_status":"published","date_created":"2021-05-02T22:01:28Z","file_date_updated":"2021-05-04T12:41:38Z","abstract":[{"lang":"eng","text":"The multimeric matrix (M) protein of clinically relevant paramyxoviruses orchestrates assembly and budding activity of viral particles at the plasma membrane (PM). We identified within the canine distemper virus (CDV) M protein two microdomains, potentially assuming α-helix structures, which are essential for membrane budding activity. Remarkably, while two rationally designed microdomain M mutants (E89R, microdomain 1 and L239D, microdomain 2) preserved proper folding, dimerization, interaction with the nucleocapsid protein, localization at and deformation of the PM, the virus-like particle formation, as well as production of infectious virions (as monitored using a membrane budding-complementation system), were, in sharp contrast, strongly impaired. Of major importance, raster image correlation spectroscopy (RICS) revealed that both microdomains contributed to finely tune M protein mobility specifically at the PM. Collectively, our data highlighted the cornerstone membrane budding-priming activity of two spatially discrete M microdomains, potentially by coordinating the assembly of productive higher oligomers at the PM."}],"scopus_import":"1","date_published":"2021-04-14T00:00:00Z","intvolume":"         6","author":[{"full_name":"Gast, Matthieu","first_name":"Matthieu","last_name":"Gast"},{"full_name":"Kadzioch, Nicole P.","first_name":"Nicole P.","last_name":"Kadzioch"},{"id":"384050BC-F248-11E8-B48F-1D18A9856A87","full_name":"Milius, Doreen","first_name":"Doreen","last_name":"Milius"},{"full_name":"Origgi, Francesco","first_name":"Francesco","last_name":"Origgi"},{"last_name":"Plattet","first_name":"Philippe","full_name":"Plattet, Philippe"}],"volume":6,"quality_controlled":"1","license":"https://creativecommons.org/licenses/by/4.0/","issue":"2","_id":"9361"}]