Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2
Dengue virus is a growing public health threat that affects hundreds of million peoples every year and leave huge economic and social damage. The virus is transmitted by mosquitoes and the incidence of the disease is increasing, among other causes, due to the geographical expansion of the vector’s r...
Saved in:
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2017-01-01
|
| Series: | Advances in Virology |
| Online Access: | http://dx.doi.org/10.1155/2017/1827341 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850209270097772544 |
|---|---|
| author | Carolina de la Guardia Mario Quijada Ricardo Lleonart |
| author_facet | Carolina de la Guardia Mario Quijada Ricardo Lleonart |
| author_sort | Carolina de la Guardia |
| collection | DOAJ |
| description | Dengue virus is a growing public health threat that affects hundreds of million peoples every year and leave huge economic and social damage. The virus is transmitted by mosquitoes and the incidence of the disease is increasing, among other causes, due to the geographical expansion of the vector’s range and the lack of effectiveness in public health interventions in most prevalent countries. So far, no highly effective vaccine or antiviral has been developed for this virus. Here we employed phage display technology to identify peptides able to block the DENV2. A random peptide library presented in M13 phages was screened with recombinant dengue envelope and its fragment domain III. After four rounds of panning, several binding peptides were identified, synthesized, and tested against the virus. Three peptides were able to block the infectivity of the virus while not being toxic to the target cells. Blind docking simulations were done to investigate the possible mode of binding, showing that all peptides appear to bind domain III of the protein and may be mostly stabilized by hydrophobic interactions. These results are relevant to the development of novel therapeutics against this important virus. |
| format | Article |
| id | doaj-art-91faca4df7744e3e9bae485b028d6eb1 |
| institution | OA Journals |
| issn | 1687-8639 1687-8647 |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Advances in Virology |
| spelling | doaj-art-91faca4df7744e3e9bae485b028d6eb12025-08-20T02:10:02ZengWileyAdvances in Virology1687-86391687-86472017-01-01201710.1155/2017/18273411827341Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2Carolina de la Guardia0Mario Quijada1Ricardo Lleonart2Center of Cellular and Molecular Biology of Diseases, Instituto de Investigaciones Científicas y Servicios de Alta Tecnología (INDICASAT AIP), Building 219, Ciudad del Saber, Apartado 0843-01103, Panamá, PanamaCenter of Cellular and Molecular Biology of Diseases, Instituto de Investigaciones Científicas y Servicios de Alta Tecnología (INDICASAT AIP), Building 219, Ciudad del Saber, Apartado 0843-01103, Panamá, PanamaCenter of Cellular and Molecular Biology of Diseases, Instituto de Investigaciones Científicas y Servicios de Alta Tecnología (INDICASAT AIP), Building 219, Ciudad del Saber, Apartado 0843-01103, Panamá, PanamaDengue virus is a growing public health threat that affects hundreds of million peoples every year and leave huge economic and social damage. The virus is transmitted by mosquitoes and the incidence of the disease is increasing, among other causes, due to the geographical expansion of the vector’s range and the lack of effectiveness in public health interventions in most prevalent countries. So far, no highly effective vaccine or antiviral has been developed for this virus. Here we employed phage display technology to identify peptides able to block the DENV2. A random peptide library presented in M13 phages was screened with recombinant dengue envelope and its fragment domain III. After four rounds of panning, several binding peptides were identified, synthesized, and tested against the virus. Three peptides were able to block the infectivity of the virus while not being toxic to the target cells. Blind docking simulations were done to investigate the possible mode of binding, showing that all peptides appear to bind domain III of the protein and may be mostly stabilized by hydrophobic interactions. These results are relevant to the development of novel therapeutics against this important virus.http://dx.doi.org/10.1155/2017/1827341 |
| spellingShingle | Carolina de la Guardia Mario Quijada Ricardo Lleonart Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2 Advances in Virology |
| title | Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2 |
| title_full | Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2 |
| title_fullStr | Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2 |
| title_full_unstemmed | Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2 |
| title_short | Phage-Displayed Peptides Selected to Bind Envelope Glycoprotein Show Antiviral Activity against Dengue Virus Serotype 2 |
| title_sort | phage displayed peptides selected to bind envelope glycoprotein show antiviral activity against dengue virus serotype 2 |
| url | http://dx.doi.org/10.1155/2017/1827341 |
| work_keys_str_mv | AT carolinadelaguardia phagedisplayedpeptidesselectedtobindenvelopeglycoproteinshowantiviralactivityagainstdenguevirusserotype2 AT marioquijada phagedisplayedpeptidesselectedtobindenvelopeglycoproteinshowantiviralactivityagainstdenguevirusserotype2 AT ricardolleonart phagedisplayedpeptidesselectedtobindenvelopeglycoproteinshowantiviralactivityagainstdenguevirusserotype2 |