{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T21:31:14Z","timestamp":1787002274577,"version":"build-2736575974"},"reference-count":47,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100005762","name":"National Taiwan University Hospital","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005762","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020595","name":"National Science and Technology Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100020595","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Insect Biochemistry and Molecular Biology"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.ibmb.2026.104643","type":"journal-article","created":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T06:46:29Z","timestamp":1785307589000},"page":"104643","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Aedes aegypti calreticulin promotes dengue virus replication and transmission by glycan-dependent binding to the prM protein"],"prefix":"10.1016","volume":"194","author":[{"given":"Shih-Che","family":"Weng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu-Chieh","family":"Hsu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Po-Nien","family":"Tsao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7749-7807","authenticated-orcid":false,"given":"Shin-Hong","family":"Shiao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ibmb.2026.104643_bib1","article-title":"Beyond the bite: how mosquito salivary proteins modulate midgut biology and malaria parasite transmission","volume":"69","author":"Alves E Silva","year":"2025","journal-title":"Curr. Opin. Insect Sci."},{"key":"10.1016\/j.ibmb.2026.104643_bib2","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/S0074-7696(01)05004-5","article-title":"Endoplasmic reticulum of animal cells and its organization into structural and functional domains","volume":"205","author":"Baumann","year":"2001","journal-title":"Int. Rev. Cytol."},{"key":"10.1016\/j.ibmb.2026.104643_bib3","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/0968-0004(94)90205-4","article-title":"Calnexin: a membrane-bound chaperone of the endoplasmic reticulum","volume":"19","author":"Bergeron","year":"1994","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.ibmb.2026.104643_bib4","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/j.virol.2007.05.007","article-title":"Glycosylation of the dengue 2 virus E protein at N67 is critical for virus growth in vitro but not for growth in intrathoracically inoculated Aedes aegypti mosquitoes","volume":"366","author":"Bryant","year":"2007","journal-title":"Virology"},{"key":"10.1016\/j.ibmb.2026.104643_bib5","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1186\/1743-422X-10-127","article-title":"Development of a transmission model for dengue virus","volume":"10","author":"Christofferson","year":"2013","journal-title":"Virol. J."},{"key":"10.1016\/j.ibmb.2026.104643_bib6","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0004941","article-title":"Aedes aegypti D7 saliva protein inhibits dengue virus infection","volume":"10","author":"Conway","year":"2016","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.ibmb.2026.104643_bib7","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1128\/JVI.02235-13","article-title":"Mosquito saliva serine protease enhances dissemination of dengue virus into the mammalian host","volume":"88","author":"Conway","year":"2013","journal-title":"J. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib8","doi-asserted-by":"crossref","first-page":"564","DOI":"10.1128\/JVI.74.1.564-572.2000","article-title":"Alpha-glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulum","volume":"74","author":"Courageot","year":"2000","journal-title":"J. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib9","doi-asserted-by":"crossref","first-page":"2233","DOI":"10.1105\/tpc.11.11.2233","article-title":"Saturation of the endoplasmic reticulum retention machinery reveals anterograde bulk flow","volume":"11","author":"Crofts","year":"1999","journal-title":"Plant Cell"},{"key":"10.1016\/j.ibmb.2026.104643_bib10","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/825039","article-title":"Progress in the identification of dengue virus entry\/fusion inhibitors","volume":"2014","author":"De La Guardia","year":"2014","journal-title":"Biomed Res. Int."},{"key":"10.1016\/j.ibmb.2026.104643_bib11","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.cell.2005.08.032","article-title":"Cell-surface calreticulin initiates clearance of viable or apoptotic cells through trans-activation of LRP on the phagocyte","volume":"123","author":"Gardai","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.ibmb.2026.104643_bib12","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1093\/protein\/3.5.433","article-title":"Sequence differences between glycosylated and non-glycosylated Asn-X-Thr\/Ser acceptor sites: implications for protein engineering","volume":"3","author":"Gavel","year":"1990","journal-title":"Protein Eng."},{"key":"10.1016\/j.ibmb.2026.104643_bib13","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1096\/fj.09-145482","article-title":"Calreticulin: non-endoplasmic reticulum functions in physiology and disease","volume":"24","author":"Gold","year":"2010","journal-title":"FASEB J."},{"key":"10.1016\/j.ibmb.2026.104643_bib14","doi-asserted-by":"crossref","first-page":"82","DOI":"10.3390\/biom15010082","article-title":"Unraveling the molecular mechanisms of mosquito salivary proteins: new frontiers in disease transmission and control","volume":"15","author":"Guo","year":"2025","journal-title":"Biomolecules"},{"key":"10.1016\/j.ibmb.2026.104643_bib15","doi-asserted-by":"crossref","first-page":"913","DOI":"10.1073\/pnas.91.3.913","article-title":"Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control","volume":"91","author":"Hammond","year":"1994","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1016\/j.ibmb.2026.104643_bib16","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1038\/s41392-024-01886-1","article-title":"Glycosylation: mechanisms, biological functions and clinical implications","volume":"9","author":"He","year":"2024","journal-title":"Signal Transduct. Targeted Ther."},{"key":"10.1016\/j.ibmb.2026.104643_bib17","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/S0014-5793(00)01666-5","article-title":"Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?","volume":"476","author":"High","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ibmb.2026.104643_bib18","doi-asserted-by":"crossref","first-page":"1751","DOI":"10.1007\/s00705-016-2855-2","article-title":"Glycosylation of dengue virus glycoproteins and their interactions with carbohydrate receptors: possible targets for antiviral therapy","volume":"161","author":"Idris","year":"2016","journal-title":"Arch. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib19","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1111\/j.1348-0421.2001.tb02627.x","article-title":"Comparative sequences of two type 1 dengue virus strains possessing different growth characteristics in vitro","volume":"45","author":"Ishak","year":"2001","journal-title":"Microbiol. Immunol."},{"key":"10.1016\/j.ibmb.2026.104643_bib20","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-3-540-46410-5_1","article-title":"Lectins of the ER quality control machinery","volume":"33","author":"Jakob","year":"2001","journal-title":"Results Probl. Cell Differ."},{"key":"10.1016\/j.ibmb.2026.104643_bib21","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1006\/viro.1994.1481","article-title":"The envelope glycoproteins of dengue 1 and dengue 2 viruses grown in mosquito cells differ in their utilization of potential glycosylation sites","volume":"203","author":"Johnson","year":"1994","journal-title":"Virology"},{"key":"10.1016\/j.ibmb.2026.104643_bib22","doi-asserted-by":"crossref","first-page":"44","DOI":"10.3390\/ph10020044","article-title":"Pathogenesis and inhibition of flaviviruses from a carbohydrate perspective","volume":"10","author":"Kim","year":"2017","journal-title":"Pharmaceuticals (Basel)"},{"key":"10.1016\/j.ibmb.2026.104643_bib23","series-title":"Fundamental Virology","author":"Knipe","year":"2001"},{"key":"10.1016\/j.ibmb.2026.104643_bib24","doi-asserted-by":"crossref","first-page":"283","DOI":"10.4155\/fmc.10.290","article-title":"Profiling of influenza viruses by high-throughput carbohydrate membrane array","volume":"3","author":"Lao","year":"2011","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ibmb.2026.104643_bib25","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1126\/science.1153263","article-title":"The flavivirus precursor membrane-envelope protein complex: structure and maturation","volume":"319","author":"Li","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.ibmb.2026.104643_bib26","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.bbrc.2008.12.070","article-title":"Interaction of dengue virus envelope protein with endoplasmic reticulum-resident chaperones facilitates dengue virus production","volume":"379","author":"Limjindaporn","year":"2009","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ibmb.2026.104643_bib27","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001252","article-title":"Induction of a peptide with activity against a broad spectrum of pathogens in the Aedes aegypti salivary gland, following infection with Dengue Virus","volume":"7","author":"Luplertlop","year":"2011","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.ibmb.2026.104643_bib28","doi-asserted-by":"crossref","first-page":"1881","DOI":"10.1128\/JVI.01218-13","article-title":"Analysis of early dengue virus infection in mice as modulated by Aedes aegypti probing","volume":"88","author":"McCracken","year":"2014","journal-title":"J. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib29","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.virol.2014.07.019","article-title":"Aedes aegypti salivary protein \u201caegyptin\u201d co-inoculation modulates dengue virus infection in the vertebrate host","volume":"468\u2013470","author":"McCracken","year":"2014","journal-title":"Virology"},{"key":"10.1016\/j.ibmb.2026.104643_bib30","doi-asserted-by":"crossref","first-page":"6986","DOI":"10.1073\/pnas.0832193100","article-title":"A ligand-binding pocket in the dengue virus envelope glycoprotein","volume":"100","author":"Modis","year":"2003","journal-title":"Proc. Natl. Acad. Sci. USA."},{"key":"10.1016\/j.ibmb.2026.104643_bib31","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1128\/JVI.79.2.1223-1231.2005","article-title":"Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein","volume":"79","author":"Modis","year":"2005","journal-title":"J. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib32","doi-asserted-by":"crossref","first-page":"7136","DOI":"10.1128\/JVI.00116-07","article-title":"Essential role of dengue virus envelope protein N glycosylation at asparagine-67 during viral propagation","volume":"81","author":"Mondotte","year":"2007","journal-title":"J. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib33","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1006\/viro.1996.0406","article-title":"Mutagenesis of the N-linked glycosylation sites of the yellow fever virus NS1 protein: effects on virus replication and mouse neurovirulence","volume":"222","author":"Muylaert","year":"1996","journal-title":"Virology"},{"key":"10.1016\/j.ibmb.2026.104643_bib34","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/j.cell.2005.11.042","article-title":"Cryo-EM reconstruction of dengue virus in complex with the carbohydrate recognition domain of DC-SIGN","volume":"124","author":"Pokidysheva","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.ibmb.2026.104643_bib35","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1006\/viro.1993.1318","article-title":"The effects of site-directed mutagenesis on the dimerization and secretion of the NS1 protein specified by dengue virus","volume":"194","author":"Pryor","year":"1993","journal-title":"Virology"},{"key":"10.1016\/j.ibmb.2026.104643_bib36","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1016\/j.sbi.2011.08.005","article-title":"Mechanisms and principles of N-linked protein glycosylation","volume":"21","author":"Schwarz","year":"2011","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.ibmb.2026.104643_bib37","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.virol.2011.02.022","article-title":"N-linked glycosylation of dengue virus NS1 protein modulates secretion, cell-surface expression, hexamer stability, and interactions with human complement","volume":"413","author":"Somnuke","year":"2011","journal-title":"Virology"},{"key":"10.1016\/j.ibmb.2026.104643_bib38","doi-asserted-by":"crossref","DOI":"10.1016\/j.ibmb.2019.103181","article-title":"A salivary protein of Aedes aegypti promotes dengue-2 virus replication and transmission","volume":"111","author":"Sri-In","year":"2019","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.ibmb.2026.104643_bib39","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0233618","article-title":"A simplified method for blood feeding, oral infection, and saliva collection of the dengue vector mosquitoes","volume":"15","author":"Sri-In","year":"2020","journal-title":"PLoS One"},{"key":"10.1016\/j.ibmb.2026.104643_bib40","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1038\/jid.2013.251","article-title":"Aedes aegypti saliva contains a prominent 34-kDa protein that strongly enhances dengue virus replication in human keratinocytes","volume":"134","author":"Surasombatpattana","year":"2013","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.ibmb.2026.104643_bib41","doi-asserted-by":"crossref","first-page":"2103","DOI":"10.1038\/jid.2012.76","article-title":"Aedes aegypti saliva enhances dengue virus infection of human keratinocytes by suppressing innate immune responses","volume":"132","author":"Surasombatpattana","year":"2012","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.ibmb.2026.104643_bib42","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0006439","article-title":"Mosquito saliva alone has profound effects on the human immune system","volume":"12","author":"Vogt","year":"2018","journal-title":"PLoS Neglected Trop. Dis."},{"key":"10.1016\/j.ibmb.2026.104643_bib43","doi-asserted-by":"crossref","first-page":"2547","DOI":"10.1128\/JVI.73.3.2547-2551.1999","article-title":"PrM- and cell-binding domains of the dengue virus E protein","volume":"73","author":"Wang","year":"1999","journal-title":"J. Virol."},{"key":"10.1016\/j.ibmb.2026.104643_bib44","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1111\/1744-7917.13193","article-title":"Research progress toward the influence of mosquito salivary proteins on the transmission of mosquito-borne viruses","volume":"31","author":"Wang","year":"2024","journal-title":"Insect Sci."},{"key":"10.1016\/j.ibmb.2026.104643_bib45","doi-asserted-by":"crossref","DOI":"10.1016\/j.ibmb.2022.103723","article-title":"A flavivirus-inducible gene expression system that modulates broad-spectrum antiviral activity against dengue and Zika viruses","volume":"142","author":"Weng","year":"2022","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.ibmb.2026.104643_bib46","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0042-6822(88)90408-4","article-title":"Evidence that the mature form of the flavivirus nonstructural protein NS1 is a dimer","volume":"162","author":"Winkler","year":"1988","journal-title":"Virology"},{"issue":"12","key":"10.1016\/j.ibmb.2026.104643_bib47","doi-asserted-by":"crossref","first-page":"4019","DOI":"10.1128\/jvi.61.12.4019-4022.1987","article-title":"Expression of dengue virus structural proteins and nonstructural protein NS1 by a recombinant vaccinia virus","volume":"61","author":"Zhao","year":"1987","journal-title":"J. Virol."}],"container-title":["Insect Biochemistry and Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0965174826001670?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0965174826001670?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T20:32:12Z","timestamp":1786998732000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0965174826001670"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":47,"alternative-id":["S0965174826001670"],"URL":"https:\/\/doi.org\/10.1016\/j.ibmb.2026.104643","relation":{},"ISSN":["0965-1748"],"issn-type":[{"value":"0965-1748","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Aedes aegypti calreticulin promotes dengue virus replication and transmission by glycan-dependent binding to the prM protein","name":"articletitle","label":"Article Title"},{"value":"Insect Biochemistry and Molecular Biology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ibmb.2026.104643","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier Ltd. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"104643"}}