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Hantavirus Gc glycoprotein: evidence for a class II fusion protein

¹ Fundación Ciencia para la Vida, Zañartu 1482, Santiago, Chile
² Instituto Milenio MIFAB, Zañartu 1482, Santiago, Chile
³ Centro de Genómica y Bioinformática, Pontificia Universidad Católica, Zañartu 1482, Santiago, Chile
⁴ Universidad Andrés Bello, Zañartu 1482, Santiago, Chile

Correspondence
Nicole D. Tischler
nicole.tischler{at}bionova.cl or
nicoletis{at}yahoo.com

Hantavirus cell entry is promoted by its envelope glycoproteins, Gn and Gc, through cell attachment and by fusion between viral and endosomal membranes at low pH. However, the role of Gn and Gc in receptor binding and cell fusion has not yet been defined. In this work, a sequence presenting characteristics similar to those of class II fusion peptides (FPs) of alphavirus E1 and flavivirus E proteins is identified within the hantavirus Gc glycoprotein. A three-dimensional comparative molecular model based on crystallographic data of tick-borne encephalitis virus E protein is proposed for the Andes virus (ANDV) Gc ectodomain, which supports a feasible class II fusion-protein fold. In vitro experimental evidence is provided for the binding activity of the ANDV FP candidate to artificial membranes, as demonstrated by fluorescence anisotropy assays. Taken together, these results support the hypothesis that the Gc glycoprotein of hantaviruses and of other members of the family Bunyaviridae directs the viral fusion activity and that it may be classified as a class II viral fusion protein.

Published online ahead of print on 24 August 2005 as DOI 10.1099/vir.0.81083-0.

The GenBank accession number for the ANDV glycoprotein precursor sequence reported in this paper is 30313865 (nucleotide sequence, AY228238).

Supplementary figures and tables are available in JGV Online.

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