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Identification of a dominant endoplasmic reticulum-retention signal in yellow fever virus pre-membrane protein

Yann Ciczora^1,2,3,

Nathalie Callens^1,2,3,

¹ Université Lille Nord de France, F-59000 Lille, France
² CNRS, Institut de Biologie de Lille (UMR8161), F-59021 Lille, France
³ Institut Pasteur de Lille, F-59019 Lille, France

Correspondence
Jean Dubuisson
jean.dubuisson{at}ibl.fr

Yellow fever virus (YFV) encodes two envelope proteins, pre-membrane (prM) and envelope (E), that accumulate in the endoplasmic reticulum (ER). The C termini of prM and E form two antiparallel transmembrane -helices that contain ER-retention signals. To understand further the ER retention of the prME heterodimer, we characterized the subcellular localization of chimeric proteins made of a reporter protein fused to the transmembrane segments of YFV envelope proteins. We showed that at least three of the transmembrane segments of the prME heterodimer are ER-retention signals. Interestingly, increasing the length of these -helices led to the export of the chimeric proteins out of the ER. Furthermore, adding a diacidic export signal at the C terminus of the first transmembrane segment of the E protein also induced export to the cell surface. However, adding this export signal at the C terminus of the first transmembrane segment of E in the context of prME did not change the subcellular localization of the prME heterodimer, suggesting the presence of a stronger ER-retention signal outside the first transmembrane segment of E. Importantly, the diacidic export motif added to the C terminus of the first transmembrane segment of the prM protein was not sufficient to export a chimeric protein out of the ER, indicating that this sequence is a dominant ER-retention signal. Together, these data indicate that a combination of several signals of different strengths contributes to the ER retention of the YFV envelope protein heterodimer.

These authors contributed equally to this work.