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J. Virol. doi:10.1128/JVI.02154-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Electron cryomicroscopy reveals different F1+F2 protein states in intact parainfluenza virions

Forschungszentrum für Elektronenmikroskopie, Freie Universität Berlin, Fabeckstr. 36a, D-14195 Berlin, Germany; Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, Institut für Biologie/Biophysik, Invalidenstr. 42, D-10115 Berlin, Germany; Institut für Immunologie und Molekularbiologie, Fachbereich Veterinärmedizin, Freie Universität Berlin, Philippstr. 13, D-10115 Berlin

^* To whom correspondence should be addressed. Email: bottcher{at}chemie.fu-berlin.de. andreas.herrmann{at}rz.hu-berlin.de.

	Abstract

Electron cryomicrographs of intact PIV5 virions revealed two different surface structures, a continuous layer and distinct individual spikes. The structure of these spikes reconstructed from intact virions was compared with known F-ectodomain structures and was found to be different from the prefusion PIV5 F0, but surprisingly very similar to the hPIV3 F postfusion structure. Hence, we conclude that the individual F1+F2 spikes in intact PIV5 viruses also correspond to the postfusion state. As the observed fusion activity of PIV5 viruses has to be associated with prefusion F1+F2 proteins they have necessarily to be localised in the continuous surface structure. The data therefore strongly suggest that the prefusion state of the F1+F2 requires stabilization, most probably by the association with hemagglutinin-neuraminidase (HN). The conversion of F1+F2 proteins from the prefusion towards the postfusion state while embedded in the virus membrane is topologically difficult to comprehend on the basis of established models. and demands reconsideration of our current understanding.

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