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

CNRS, Institut de Biologie de Lille

¹ E-mail: jean.dubuisson{at}ibl.fr

Yellow fever virus 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 anti-parallel transmembrane alpha-helices that contain ER retention signals. To further understand the ER retention of prME heterodimer, we characterized the subcellular localization of chimeric proteins made of a reporter protein fused to the transmembrane segments of yellow fever virus envelope proteins. We showed that at least three of the transmembrane segments of prME heterodimer are ER retention signals. Interestingly, increasing the length of these alpha-helices led to the export of the chimeric proteins out of the ER. Furthermore, adding a di-acidic 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 prME heterodimer, suggesting the presence of a stronger ER retention signal outside of the first transmembrane segment of E. Importantly, the di-acidic 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 yellow fever virus envelope protein heterodimer.

Received 24 July 2009; accepted 20 October 2009.