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Degradation and Aggresome Formation of the Gn Tail of the Apathogenic Tula Hantavirus

Haartman Institute, University of Helsinki

¹ E-mail: hao.wang{at}helsinki.fi

The cytoplasmic tails of envelope glycoprotein Gn of pathogenic hantaviruses but not of the apathogenic hantavirus Prospect Hill (PHV) were recently reported to be proteasomally degraded in simian COS7 cells. Here, we show that the Gn tails of the apathogenic hantaviruses Tula (TULV) and of PHV are also degraded through the ubiquitin-proteasome pathway, both in human HEK-293 and simian Vero E6 cells. TULV Gn tails formed aggresomes in cells with proteasomal inhibitors. We conclude that degradation upon aggregation of Gn tails, which may represent a general cellular response to mis-folded protein used by hantaviruses to control maturation of virions, is unrelated to pathogenicity.

Received 31 March 2009; accepted 10 August 2009.