{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,7]],"date-time":"2026-04-07T09:51:58Z","timestamp":1775555518373,"version":"3.50.1"},"reference-count":59,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2004,8,1]],"date-time":"2004-08-01T00:00:00Z","timestamp":1091318400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2004,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The trimeric fusion (F) glycoproteins of morbilliviruses are activated by furin cleavage of the precursor F\n            <jats:sub>0<\/jats:sub>\n            into the F\n            <jats:sub>1<\/jats:sub>\n            and F\n            <jats:sub>2<\/jats:sub>\n            subunits. Here we show that an additional membrane-proximal cleavage occurs and modulates F protein function. We initially observed that the ectodomain of approximately one in three measles virus (MV) F proteins is cleaved proximal to the membrane. Processing occurs after cleavage activation of the precursor F\n            <jats:sub>0<\/jats:sub>\n            into the F\n            <jats:sub>1<\/jats:sub>\n            and F\n            <jats:sub>2<\/jats:sub>\n            subunits, producing F\n            <jats:sub>1a<\/jats:sub>\n            and F\n            <jats:sub>1b<\/jats:sub>\n            fragments that are incorporated in viral particles. We also detected the F\n            <jats:sub>1b<\/jats:sub>\n            fragment, including the transmembrane domain and cytoplasmic tail, in cells expressing the canine distemper virus (CDV) or mumps virus F protein. Six membrane-proximal amino acids are necessary for efficient CDV F\n            <jats:sub>1a\/b<\/jats:sub>\n            cleavage. These six amino acids can be exchanged with the corresponding MV F protein residues of different sequence without compromising function. Thus, structural elements of different sequence are functionally exchangeable. Finally, we showed that the alteration of a block of membrane-proximal amino acids results in diminished fusion activity in the context of a recombinant CDV. We envisage that selective loss of the membrane anchor in the external subunits of circularly arranged F protein trimers may disengage them from pulling the membrane centrifugally, thereby facilitating fusion pore formation.\n          <\/jats:p>","DOI":"10.1128\/jvi.78.15.7894-7903.2004","type":"journal-article","created":{"date-parts":[[2004,7,14]],"date-time":"2004-07-14T19:35:34Z","timestamp":1089833734000},"page":"7894-7903","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":26,"title":["Canine Distemper Virus and Measles Virus Fusion Glycoprotein Trimers: Partial Membrane-Proximal Ectodomain Cleavage Enhances Function"],"prefix":"10.1128","volume":"78","author":[{"given":"Veronika","family":"von Messling","sequence":"first","affiliation":[{"name":"Molecular Medicine Program"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dragana","family":"Milosevic","sequence":"additional","affiliation":[{"name":"Molecular Medicine Program"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patricia","family":"Devaux","sequence":"additional","affiliation":[{"name":"Molecular Medicine Program"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roberto","family":"Cattaneo","sequence":"additional","affiliation":[{"name":"Molecular Medicine Program"},{"name":"Virology and Gene Therapy Graduate Track, Mayo Clinic College of Medicine, Rochester, Minnesota"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1042\/bj3530663"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(00)80458-X"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1006\/viro.2002.1497"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.89.8.3443"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.72.2.1224-1234.1998"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0969-2126(01)00581-0"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm1076"},{"key":"e_1_3_2_9_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.77.12.6913-6922.2003"},{"key":"e_1_3_2_10_2","doi-asserted-by":"publisher","DOI":"10.1038\/81002"},{"key":"e_1_3_2_11_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.70.1.777"},{"key":"e_1_3_2_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(03)00683-4"},{"key":"e_1_3_2_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature02239"},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.151098198"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.95.17.10224"},{"key":"e_1_3_2_16_2","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1990.tb07643.x"},{"key":"e_1_3_2_17_2","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.77.20.11040-11049.2003"},{"key":"e_1_3_2_18_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M211169200"},{"key":"e_1_3_2_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-3527(00)55005-2"},{"key":"e_1_3_2_20_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.cellbio.12.1.627"},{"key":"e_1_3_2_21_2","doi-asserted-by":"publisher","DOI":"10.1016\/0378-1119(89)90358-2"},{"key":"e_1_3_2_22_2","first-page":"519","volume":"112","year":"2003","unstructured":"Jahn, R., T. 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