Title |
Prediction of antiviral peptides derived from viral fusion proteins potentially active against herpes simplex and influenza A viruses |
Authors |
Torres Jesús1, López Rogelio1, Cetina Abraham1, López Uriel1, García J- Daniel1, Méndez-Tenorio Alfonso2 & Barrón Blanca Lilia1* |
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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bbarron@ipn.mx; *Corresponding author
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Article Type |
Hypothesis
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Date |
Received August 28, 2012; Accepted September 03, 2012; Published September 21, 20122
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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 antivirals is not a rare event. Hence, the design of new antiviral drugs is important. We describe the prediction of peptides with antiviral activity (AVP) derived from the viral glycoproteins involved in the entrance of herpes simplex (HSV) and influenza A viruses into their host cells. It is known, that during this event viral glycoproteins suffer several conformational changes due to protein-protein interactions, which lead to membrane fusion between the viral envelope and the cellular membrane. Our hypothesis is that AVPs can be derived from these viral glycoproteins, specifically from regions highly conserved in amino acid sequences, which at the same time have the physicochemical properties of being highly exposed (antigenic), hydrophilic, flexible, and charged, since these properties are important for protein-protein interactions. For that, we separately analyzed the HSV glycoprotein H and B, and influenza A viruses hemagglutinin (HA), using several bioinformatics tools. A set of multiple alignments was carried out, to find the most conserved regions in the amino acid sequences. Then, the physicochemical properties indicated above were analyzed. We predicted several peptides 12-20 amino acid length which by docking analysis were able to interact with the fusion viral glycoproteins and thus may prevent conformational changes in them, blocking the viral infection. Our strategy to design AVPs seems to be very promising since the peptides were synthetized and their antiviral activities have produced very encouraging results.
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Keywords |
Herpes simplex viruses, influenza A viruses, antiviral peptides (AVPs), gB, gH, HA, proteins
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Citation |
Jesús et al.
Bioinformation 8(18): 870-874 (2012) |
Edited by |
P Kangueane
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ISSN |
0973-2063
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Publisher |
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License |
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |