{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T17:03:22Z","timestamp":1791219802994,"version":"4.1.0"},"reference-count":34,"publisher":"MDPI AG","issue":"1","license":[{"start":{"date-parts":[[2011,1,18]],"date-time":"2011-01-18T00:00:00Z","timestamp":1295308800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Viruses"],"abstract":"<jats:p>In their recent publication, Rossman et al. [1] describe how the inherent budding capability of its M2 protein allows influenza A virus to bypass recruitment of the cellular ESCRT machinery enlisted by several other enveloped RNA and DNA viruses, including HIV, Ebola, rabies, herpes simplex type 1 and hepatitis B. Studies from the same laboratory [2] and other laboratories [3\u20136] indicate that budding of plasmid-derived virus-like particles can be mediated by the influenza virus hemagglutinin and neuraminidase proteins in the absence of M2. These events are also independent of canonical ESCRT components [2,7]. Understanding how intrinsic properties of these influenza virus proteins permit ESCRT-independent budding expands our understanding of the budding process itself.<\/jats:p>","DOI":"10.3390\/v3010026","type":"journal-article","created":{"date-parts":[[2011,1,18]],"date-time":"2011-01-18T11:35:06Z","timestamp":1295350506000},"page":"26-31","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Un-\u201cESCRT\u201d-ed Budding"],"prefix":"10.3390","volume":"3","author":[{"given":"Mark","family":"Yondola","sequence":"first","affiliation":[{"name":"Department of Microbiology, Mount Sinai School of Medicine, New York, NY 10128, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carol","family":"Carter","sequence":"additional","affiliation":[{"name":"Department of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, NY 11794, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2011,1,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1016\/j.cell.2010.08.029","article-title":"Influenza virus M2 protein mediates ESCRT-independent membrane scission","volume":"142","author":"Rossman","year":"2010","journal-title":"Cell"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"7111","DOI":"10.1128\/JVI.00361-07","article-title":"Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles","volume":"81","author":"Chen","year":"2007","journal-title":"J. Virol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"2322","DOI":"10.1099\/vir.0.019935-0","article-title":"Formation of virus-like particles from human cell lines exclusively expressing influenza neuraminidase","volume":"91","author":"Lai","year":"2010","journal-title":"J. Gen. Virol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"11538","DOI":"10.1128\/JVI.74.24.11538-11547.2000","article-title":"Influenza virus matrix protein is the major driving force in virus budding","volume":"74","author":"Albo","year":"2000","journal-title":"J. Virol."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"6154","DOI":"10.1128\/JVI.75.13.6154-6165.2001","article-title":"Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins","volume":"75","author":"Latham","year":"2001","journal-title":"J. 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