{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,20]],"date-time":"2026-03-20T04:56:17Z","timestamp":1773982577456,"version":"3.50.1"},"reference-count":37,"publisher":"Microbiology Society","issue":"6","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2014,6,1]]},"abstract":"<jats:p>All influenza viruses bud and egress from lipid rafts within the apical plasma membrane of infected epithelial cells. As a result, all components of progeny virions must be transported to these lipid rafts for assembly and budding. Although the mechanism of transport for other influenza proteins has been elucidated, influenza B virus (IBV) glycoprotein NB subcellular localization and transport are not understood completely. To address the aforementioned properties of NB, a series of trafficking experiments were conducted. Here, we showed that NB co-localized with markers specific for the endoplasmic reticulum (ER) and Golgi region. The data from chemical treatment of NB-expressing cells by Brefeldin A, a fungal antibiotic and a known chemical inhibitor of the protein secretory pathway, further confirmed that NB is transported through the ER\u2013Golgi pathway as it restricted NB localization to the perinuclear region. Using NB deletion mutants, the hydrophobic transmembrane domain was identified as being required for NB transport to the plasma membrane. Furthermore, palmitoylation was also required for transport of NB to the plasma membrane. Systematic mutation of cysteines to serines in NB demonstrated that cysteine 49, likely in a palmitoylated form, is also required for transport to the plasma membrane. Surprisingly, further analysis demonstrated that<jats:italic>in vitro<\/jats:italic>replication of NBC49S mutant virus was delayed relative to the parental IBV. The results demonstrated that NB is the third influenza virus protein to have been shown to be palmitoylated and together these findings may aid in future studies aimed at elucidating the function of NB.<\/jats:p>","DOI":"10.1099\/vir.0.063511-0","type":"journal-article","created":{"date-parts":[[2014,3,27]],"date-time":"2014-03-27T04:55:57Z","timestamp":1395896157000},"page":"1211-1220","source":"Crossref","is-referenced-by-count":17,"title":["Palmitoylation is required for intracellular trafficking of influenza B virus NB protein and efficient influenza B virus growth in vitro"],"prefix":"10.1099","volume":"95","author":[{"given":"Andrew","family":"Demers","sequence":"first","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Veterinary and Biomedical Sciences, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Biology and Microbiology, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhiguang","family":"Ran","sequence":"additional","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Veterinary and Biomedical Sciences, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Qiji","family":"Deng","sequence":"additional","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Veterinary and Biomedical Sciences, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dan","family":"Wang","sequence":"additional","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Biology and Microbiology, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Brody","family":"Edman","sequence":"additional","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Biology and Microbiology, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wuxun","family":"Lu","sequence":"additional","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Biology and Microbiology, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Feng","family":"Li","sequence":"additional","affiliation":[{"name":"Center for Infectious Disease Research and Vaccinology, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Veterinary and Biomedical Sciences, South Dakota State University, Brookings, SD 57007, USA"},{"name":"Department of Biology and Microbiology, South Dakota State University, Brookings, SD 57007, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"345","reference":[{"key":"r1","doi-asserted-by":"publisher","DOI":"10.1016\/S0168-1702(01)00266-0"},{"key":"r2","doi-asserted-by":"publisher","DOI":"10.1016\/S0962-8924(02)00008-9"},{"key":"r3","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M100583200"},{"key":"r4","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.0323"},{"key":"r5","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M404410200"},{"key":"r6","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.78.4.1865-1872.2004"},{"key":"r7","doi-asserted-by":"crossref","first-page":"18545","DOI":"10.1016\/S0021-9258(19)81393-5","article-title":"Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum","volume":"263","author":"Fujiwara","year":"1988","journal-title":"J Biol Chem"},{"key":"r8","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.01129-09"},{"key":"r9","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M802048200"},{"key":"r10","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.77.10.6050-6054.2003"},{"key":"r11","doi-asserted-by":"publisher","DOI":"10.1086\/368218"},{"key":"r12","doi-asserted-by":"crossref","first-page":"1219","DOI":"10.1128\/JVI.69.2.1219-1225.1995","article-title":"Analysis of the posttranslational modifications of the influenza virus M2 protein","volume":"69","author":"Holsinger","year":"1995","journal-title":"J Virol"},{"key":"r13","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1042\/bj3030749","article-title":"Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif","volume":"303","author":"Koegl","year":"1994","journal-title":"Biochem J"},{"key":"r14","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M102782200"},{"key":"r15","doi-asserted-by":"crossref","first-page":"6508","DOI":"10.1128\/JVI.70.9.6508-6515.1996","article-title":"Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells","volume":"70","author":"Kundu","year":"1996","journal-title":"J Virol"},{"key":"r16","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.142.1.51"},{"key":"r17","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2235688100"},{"key":"r18","doi-asserted-by":"publisher","DOI":"10.1016\/j.virol.2005.03.028"},{"key":"r19","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.6.3910"},{"key":"r20","doi-asserted-by":"crossref","first-page":"3857","DOI":"10.1002\/j.1460-2075.1990.tb07604.x","article-title":"Fatty acids on the A\/Japan\/305\/57 influenza virus hemagglutinin have a role in membrane fusion","volume":"9","author":"Naeve","year":"1990","journal-title":"EMBO J"},{"key":"r21","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.cellbio.21.012704.133214"},{"key":"r22","first-page":"1647","volume-title":"Fields Virology","author":"Palese","year":"2007"},{"key":"r23","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(80)90233-0"},{"key":"r24","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.75.10.5071"},{"key":"r25","doi-asserted-by":"crossref","first-page":"1065","DOI":"10.1128\/JVI.45.3.1065-1073.1983","article-title":"Basolateral maturation of retroviruses in polarized epithelial cells","volume":"45","author":"Roth","year":"1983","journal-title":"J Virol"},{"key":"r26","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.274.4.2038"},{"key":"r27","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.80.16.4879"},{"key":"r28","doi-asserted-by":"publisher","DOI":"10.1038\/35036052"},{"key":"r29","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1128\/JVI.66.2.790-803.1992","article-title":"Alterations to influenza virus hemagglutinin cytoplasmic tail modulate virus infectivity","volume":"66","author":"Simpson","year":"1992","journal-title":"J Virol"},{"key":"r30","doi-asserted-by":"publisher","DOI":"10.1016\/0042-6822(91)90867-B"},{"key":"r31","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2235620100"},{"key":"r32","doi-asserted-by":"publisher","DOI":"10.1126\/science.1142204"},{"key":"r33","doi-asserted-by":"crossref","first-page":"2491","DOI":"10.1128\/JVI.65.5.2491-2500.1991","article-title":"Site-specific mutagenesis identifies three cysteine residues in the cytoplasmic tail as acylation sites of influenza virus hemagglutinin","volume":"65","author":"Veit","year":"1991","journal-title":"J Virol"},{"key":"r34","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.77.19.10630-10637.2003"},{"key":"r35","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.275.1.261"},{"key":"r36","doi-asserted-by":"crossref","first-page":"4317","DOI":"10.1128\/MCB.6.12.4317","article-title":"Determination of the orientation of an integral membrane protein and sites of glycosylation by oligonucleotide-directed mutagenesis: influenza B virus NB glycoprotein lacks a cleavable signal sequence and has an extracellular NH2-terminal region","volume":"6","author":"Williams","year":"1986","journal-title":"Mol Cell Biol"},{"key":"r37","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1128\/MCB.8.3.1186","article-title":"Polylactosaminoglycan modification of a small integral membrane glycoprotein, influenza B virus NB","volume":"8","author":"Williams","year":"1988","journal-title":"Mol Cell Biol"}],"container-title":["Journal of General Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.063511-0?crawler=true","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,31]],"date-time":"2022-03-31T02:42:55Z","timestamp":1648694575000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.microbiologyresearch.org\/content\/journal\/jgv\/10.1099\/vir.0.063511-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,6,1]]},"references-count":37,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2014,6,1]]}},"URL":"https:\/\/doi.org\/10.1099\/vir.0.063511-0","relation":{},"ISSN":["0022-1317","1465-2099"],"issn-type":[{"value":"0022-1317","type":"print"},{"value":"1465-2099","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,6,1]]}}}