Prediction of antiviral peptides derived from viral fusion proteins potentially active against herpes simplex and influenza A viruses |
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Authors: | Torres Jes��s L��pez Rogelio Cetina Abraham L��pez Uriel Garc��a J- Daniel M��ndez-Tenorio Alfonso Barr��n Blanca Lilia |
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Affiliation: | 1Microbiology Department, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Carpio y Plan de Ayala S/N, Casco de Santo Tomás, México D.F. 11340, México;2Biochemestry Department, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Carpio y Plan de Ayala S/N, Casco de Santo Tomás, México D.F. 11340, México |
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Abstract: | There are very few antiviral drugs available to fight viral infections and the appearance of viral strains resistant to these antiviralsis not a rare event. Hence, the design of new antiviral drugs is important. We describe the prediction of peptides with antiviralactivity (AVP) derived from the viral glycoproteins involved in the entrance of herpes simplex (HSV) and influenza A viruses intotheir host cells. It is known, that during this event viral glycoproteins suffer several conformational changes due to protein-proteininteractions, which lead to membrane fusion between the viral envelope and the cellular membrane. Our hypothesis is that AVPscan be derived from these viral glycoproteins, specifically from regions highly conserved in amino acid sequences, which at thesame time have the physicochemical properties of being highly exposed (antigenic), hydrophilic, flexible, and charged, since theseproperties are important for protein-protein interactions. For that, we separately analyzed the HSV glycoprotein H and B, andinfluenza A viruses hemagglutinin (HA), using several bioinformatics tools. A set of multiple alignments was carried out, to findthe most conserved regions in the amino acid sequences. Then, the physicochemical properties indicated above were analyzed. Wepredicted several peptides 12-20 amino acid length which by docking analysis were able to interact with the fusion viralglycoproteins and thus may prevent conformational changes in them, blocking the viral infection. Our strategy to design AVPsseems to be very promising since the peptides were synthetized and their antiviral activities have produced very encouragingresults. |
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Keywords: | Herpes simplex viruses influenza A viruses antiviral peptides (AVPs) gB gH HA proteins |
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