It appears you don't have support to open PDFs in this web browser. To view this file, Open with your PDF reader
Abstract
Chikungunya virus (CHIKV) is the etiologic agent of Chikungunya fever, a globally spreading mosquito-borne disease. There is no approved antiviral or vaccine against CHIKV, highlighting an urgent need for novel therapies. In this context, snake venom proteins have demonstrated antiviral activity against several viruses, including arboviruses which are relevant to public health. In particular, the phospholipase A2CB (PLA2CB), a protein isolated from the venom of Crotalus durissus terrificus was previously shown to possess anti-inflammatory, antiparasitic, antibacterial and antiviral activities. In this study, we investigated the multiple effects of PLA2CB on the CHIKV replicative cycle in BHK-21 cells using CHIKV-nanoluc, a marker virus carrying nanoluciferase reporter. The results demonstrated that PLA2CB possess a strong anti-CHIKV activity with a selectivity index of 128. We identified that PLA2CB treatment protected cells against CHIKV infection, strongly impairing virus entry by reducing adsorption and post-attachment stages. Moreover, PLA2CB presented a modest yet significant activity towards post-entry stages of CHIKV replicative cycle. Molecular docking calculations indicated that PLA2CB may interact with CHIKV glycoproteins, mainly with E1 through hydrophobic interactions. In addition, infrared spectroscopy measurements indicated interactions of PLA2CB and CHIKV glycoproteins, corroborating with data from in silico analyses. Collectively, this data demonstrated the multiple antiviral effects of PLA2CB on the CHIKV replicative cycle, and suggest that PLA2CB interacts with CHIKV glycoproteins and that this interaction blocks binding of CHIKV virions to the host cells.
You have requested "on-the-fly" machine translation of selected content from our databases. This functionality is provided solely for your convenience and is in no way intended to replace human translation. Show full disclaimer
Neither ProQuest nor its licensors make any representations or warranties with respect to the translations. The translations are automatically generated "AS IS" and "AS AVAILABLE" and are not retained in our systems. PROQUEST AND ITS LICENSORS SPECIFICALLY DISCLAIM ANY AND ALL EXPRESS OR IMPLIED WARRANTIES, INCLUDING WITHOUT LIMITATION, ANY WARRANTIES FOR AVAILABILITY, ACCURACY, TIMELINESS, COMPLETENESS, NON-INFRINGMENT, MERCHANTABILITY OR FITNESS FOR A PARTICULAR PURPOSE. Your use of the translations is subject to all use restrictions contained in your Electronic Products License Agreement and by using the translation functionality you agree to forgo any and all claims against ProQuest or its licensors for your use of the translation functionality and any output derived there from. Hide full disclaimer
Details
1 Federal University of Uberlândia (UFU), Institute of Biomedical Science (ICBIM), Uberlândia, Brazil (GRID:grid.411284.a) (ISNI:0000 0004 4647 6936)
2 Federal University of Uberlândia (UFU), Institute of Biomedical Science (ICBIM), Uberlândia, Brazil (GRID:grid.411284.a) (ISNI:0000 0004 4647 6936); São Paulo State University (Unesp), Institute of Biosciences, Humanities and Exact Sciences (Ibilce), São José do Rio Preto, Brazil (GRID:grid.410543.7) (ISNI:0000 0001 2188 478X)
3 University of São Paulo (USP), Department of Clinical, Toxicological and Bromatological Analyses, School of Pharmaceutical Sciences of Ribeirao Preto, Ribeirão Preto, Brazil (GRID:grid.11899.38) (ISNI:0000 0004 1937 0722)
4 Federal University of Uberlândia (UFU), Institute of Biotechnology, Uberlândia, Brazil (GRID:grid.411284.a) (ISNI:0000 0004 4647 6936)
5 University of Tartu, Institute of Technology, Tartu, Estonia (GRID:grid.10939.32) (ISNI:0000 0001 0943 7661)
6 University of Leeds, Faculty of Biological Sciences and Astbury Centre for Structural Molecular Biology, Leeds, UK (GRID:grid.9909.9) (ISNI:0000 0004 1936 8403)