Pawit SomnukeRichard E. HauhartJohn P. AtkinsonMichael S. DiamondPanisadee AvirutnanWashington University in St. Louis, School of MedicineMahidol University2018-05-032018-05-032011-05-10Virology. Vol.413, No.2 (2011), 253-26410960341004268222-s2.0-79954633991https://repository.li.mahidol.ac.th/handle/20.500.14594/12048Dengue virus (DENV) NS1 is a versatile non-structural glycoprotein that is secreted as a hexamer, binds to the cell surface of infected and uninfected cells, and has immune evasive functions. DENV NS1 displays two conserved N-linked glycans at N130 and N207. In this study, we examined the role of these two N-linked glycans on NS1 secretion, stability, and function. Because some groups have reported reduced yields of infectious DENV when N130 and N207 are changed, we analyzed glycosylation-deficient NS1 phenotypes using a transgenic expression system. We show that the N-linked glycan at position 130 is required for stabilization of the secreted hexamer whereas the N-linked glycan at residue 207 facilitates secretion and extracellular protein stability. Moreover, NS1 mutan ts lacking an N-linked glycan at N130 did not interact efficiently with complement components C1s and C4. In summary, our results elucidate the contribution of N-linked glycosylation to the function of DENV NS1. © 2011 Elsevier Inc.Mahidol UniversityImmunology and MicrobiologyArticleSCOPUS10.1016/j.virol.2011.02.022