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  Inhibition of the Hantavirus Fusion Process by Predicted Domain III and Stem Peptides from Glycoprotein Gc

Barriga, G. P., Villalon-Letelier, F., Marquez, C. L., Bignon, E. A., Acuna, R., Ross, B. H., et al. (2016). Inhibition of the Hantavirus Fusion Process by Predicted Domain III and Stem Peptides from Glycoprotein Gc. PLOS Neglected Tropical Diseases, 10(7): e0004799. doi:10.1371/journal.pntd.0004799.

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© 2016 Barriga et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Barriga, Gonzalo P.1, Autor
Villalon-Letelier, Fernando1, Autor
Marquez, Chantal L.1, Autor
Bignon, Eduardo A.1, Autor
Acuna, Rodrigo1, Autor
Ross, Breyan H.2, Autor           
Monasterio, Octavio1, Autor
Mardones, Gonzalo A.1, Autor
Vidal, Simon E.1, Autor
Tischler, Nicole D.1, Autor
Affiliations:
1external, ou_persistent22              
2Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              

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Schlagwörter: VIRUS-MEMBRANE-FUSION; WEST-NILE-VIRUS; PROTEIN SECONDARY STRUCTURE; CIRCULAR-DICHROISM SPECTRA; BORNE ENCEPHALITIS-VIRUS; VALLEY FEVER VIRUS; ENVELOPE PROTEIN; DENGUE-VIRUS; HEMORRHAGIC-FEVER; RENAL SYNDROMEInfectious Diseases; Parasitology; Tropical Medicine;
 Zusammenfassung: Hantaviruses can cause hantavirus pulmonary syndrome or hemorrhagic fever with renal syndrome in humans. To enter cells, hantaviruses fuse their envelope membrane with host cell membranes. Previously, we have shown that the Gc envelope glycoprotein is the viral fusion protein sharing characteristics with class II fusion proteins. The ectodomain of class II fusion proteins is composed of three domains connected by a stem region to a transmembrane anchor in the viral envelope. These fusion proteins can be inhibited through exogenous fusion protein fragments spanning domain III (DIII) and the stem region. Such fragments are thought to interact with the core of the fusion protein trimer during the transition from its pre-fusion to its post-fusion conformation. Based on our previous homology model structure for Gc from Andes hantavirus (ANDV), here we predicted and generated recombinant DIII and stem peptides to test whether these fragments inhibit hantavirus membrane fusion and cell entry. Recombinant ANDV DIII was soluble, presented disulfide bridges and beta-sheet secondary structure, supporting the in silico model. Using DIII and the C-terminal part of the stem region, the infection of cells by ANDV was blocked up to 60% when fusion of ANDV occurred within the endosomal route, and up to 95% when fusion occurred with the plasma membrane. Furthermore, the fragments impaired ANDV glycoprotein-mediated cell-cell fusion, and cross-inhibited the fusion mediated by the glycoproteins from Puumala virus (PUUV). The Gc fragments interfered in ANDV cell entry by preventing membrane hemifusion and pore formation, retaining Gc in a non-resistant homotrimer stage, as described for DIII and stem peptide inhibitors of class II fusion proteins. Collectively, our results demonstrate that hantavirus Gc shares not only structural, but also mechanistic similarity with class II viral fusion proteins, and will hopefully help in developing novel therapeutic strategies against hantaviruses.

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Sprache(n): eng - English
 Datum: 2016-07-14
 Publikationsstatus: Online veröffentlicht
 Seiten: 23
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: ISI: 000381017800019
DOI: 10.1371/journal.pntd.0004799
 Art des Abschluß: -

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Titel: PLOS Neglected Tropical Diseases
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA : PUBLIC LIBRARY SCIENCE
Seiten: - Band / Heft: 10 (7) Artikelnummer: e0004799 Start- / Endseite: - Identifikator: ISSN: 1935-2735