Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study

Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This p...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Muhammad, Ashraf M. [verfasserIn] Salum, Ghada M. Meguid, Mai Abd El Fotouh, Basma E. Dawood, Reham M.

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	HCV Humoral response Cellular responses CD4 CD8 Toxicity Antigenicity Docking scores Vaccine development

Anmerkung:	© The Author(s) 2023

Übergeordnetes Werk:	Enthalten in: Journal of Genetic Engineering and Biotechnology - Amsterdam [u.a.] : Elsevier, 2011, 21(2023), 1 vom: 14. Nov.
Übergeordnetes Werk:	volume:21 ; year:2023 ; number:1 ; day:14 ; month:11

Links:	Volltext

DOI / URN:	10.1186/s43141-023-00583-w

Katalog-ID:	SPR053745027

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520			\|a Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors.
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650		4	\|a Docking scores \|7 (dpeaa)DE-He213
650		4	\|a Vaccine development \|7 (dpeaa)DE-He213
700	1		\|a Salum, Ghada M. \|0 (orcid)0000-0002-8837-2065 \|4 aut
700	1		\|a Meguid, Mai Abd El \|4 aut
700	1		\|a Fotouh, Basma E. \|4 aut
700	1		\|a Dawood, Reham M. \|4 aut
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Indexfelder

author_variant	a m m am amm g m s gm gms m a e m mae maem b e f be bef r m d rm rmd
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allfields	10.1186/s43141-023-00583-w doi (DE-627)SPR053745027 (SPR)s43141-023-00583-w-e DE-627 ger DE-627 rakwb eng Muhammad, Ashraf M. verfasserin aut Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2023 Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. HCV (dpeaa)DE-He213 Humoral response (dpeaa)DE-He213 Cellular responses (dpeaa)DE-He213 CD4 (dpeaa)DE-He213 CD8 (dpeaa)DE-He213 Toxicity (dpeaa)DE-He213 Antigenicity (dpeaa)DE-He213 Docking scores (dpeaa)DE-He213 Vaccine development (dpeaa)DE-He213 Salum, Ghada M. (orcid)0000-0002-8837-2065 aut Meguid, Mai Abd El aut Fotouh, Basma E. aut Dawood, Reham M. aut Enthalten in Journal of Genetic Engineering and Biotechnology Amsterdam [u.a.] : Elsevier, 2011 21(2023), 1 vom: 14. Nov. (DE-627)672802031 (DE-600)2637420-1 2090-5920 nnns volume:21 year:2023 number:1 day:14 month:11 https://dx.doi.org/10.1186/s43141-023-00583-w kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2023 1 14 11
spelling	10.1186/s43141-023-00583-w doi (DE-627)SPR053745027 (SPR)s43141-023-00583-w-e DE-627 ger DE-627 rakwb eng Muhammad, Ashraf M. verfasserin aut Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2023 Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. HCV (dpeaa)DE-He213 Humoral response (dpeaa)DE-He213 Cellular responses (dpeaa)DE-He213 CD4 (dpeaa)DE-He213 CD8 (dpeaa)DE-He213 Toxicity (dpeaa)DE-He213 Antigenicity (dpeaa)DE-He213 Docking scores (dpeaa)DE-He213 Vaccine development (dpeaa)DE-He213 Salum, Ghada M. (orcid)0000-0002-8837-2065 aut Meguid, Mai Abd El aut Fotouh, Basma E. aut Dawood, Reham M. aut Enthalten in Journal of Genetic Engineering and Biotechnology Amsterdam [u.a.] : Elsevier, 2011 21(2023), 1 vom: 14. Nov. (DE-627)672802031 (DE-600)2637420-1 2090-5920 nnns volume:21 year:2023 number:1 day:14 month:11 https://dx.doi.org/10.1186/s43141-023-00583-w kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2023 1 14 11
allfields_unstemmed	10.1186/s43141-023-00583-w doi (DE-627)SPR053745027 (SPR)s43141-023-00583-w-e DE-627 ger DE-627 rakwb eng Muhammad, Ashraf M. verfasserin aut Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2023 Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. HCV (dpeaa)DE-He213 Humoral response (dpeaa)DE-He213 Cellular responses (dpeaa)DE-He213 CD4 (dpeaa)DE-He213 CD8 (dpeaa)DE-He213 Toxicity (dpeaa)DE-He213 Antigenicity (dpeaa)DE-He213 Docking scores (dpeaa)DE-He213 Vaccine development (dpeaa)DE-He213 Salum, Ghada M. (orcid)0000-0002-8837-2065 aut Meguid, Mai Abd El aut Fotouh, Basma E. aut Dawood, Reham M. aut Enthalten in Journal of Genetic Engineering and Biotechnology Amsterdam [u.a.] : Elsevier, 2011 21(2023), 1 vom: 14. Nov. (DE-627)672802031 (DE-600)2637420-1 2090-5920 nnns volume:21 year:2023 number:1 day:14 month:11 https://dx.doi.org/10.1186/s43141-023-00583-w kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2023 1 14 11
allfieldsGer	10.1186/s43141-023-00583-w doi (DE-627)SPR053745027 (SPR)s43141-023-00583-w-e DE-627 ger DE-627 rakwb eng Muhammad, Ashraf M. verfasserin aut Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2023 Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. HCV (dpeaa)DE-He213 Humoral response (dpeaa)DE-He213 Cellular responses (dpeaa)DE-He213 CD4 (dpeaa)DE-He213 CD8 (dpeaa)DE-He213 Toxicity (dpeaa)DE-He213 Antigenicity (dpeaa)DE-He213 Docking scores (dpeaa)DE-He213 Vaccine development (dpeaa)DE-He213 Salum, Ghada M. (orcid)0000-0002-8837-2065 aut Meguid, Mai Abd El aut Fotouh, Basma E. aut Dawood, Reham M. aut Enthalten in Journal of Genetic Engineering and Biotechnology Amsterdam [u.a.] : Elsevier, 2011 21(2023), 1 vom: 14. Nov. (DE-627)672802031 (DE-600)2637420-1 2090-5920 nnns volume:21 year:2023 number:1 day:14 month:11 https://dx.doi.org/10.1186/s43141-023-00583-w kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2023 1 14 11
allfieldsSound	10.1186/s43141-023-00583-w doi (DE-627)SPR053745027 (SPR)s43141-023-00583-w-e DE-627 ger DE-627 rakwb eng Muhammad, Ashraf M. verfasserin aut Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2023 Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. HCV (dpeaa)DE-He213 Humoral response (dpeaa)DE-He213 Cellular responses (dpeaa)DE-He213 CD4 (dpeaa)DE-He213 CD8 (dpeaa)DE-He213 Toxicity (dpeaa)DE-He213 Antigenicity (dpeaa)DE-He213 Docking scores (dpeaa)DE-He213 Vaccine development (dpeaa)DE-He213 Salum, Ghada M. (orcid)0000-0002-8837-2065 aut Meguid, Mai Abd El aut Fotouh, Basma E. aut Dawood, Reham M. aut Enthalten in Journal of Genetic Engineering and Biotechnology Amsterdam [u.a.] : Elsevier, 2011 21(2023), 1 vom: 14. Nov. (DE-627)672802031 (DE-600)2637420-1 2090-5920 nnns volume:21 year:2023 number:1 day:14 month:11 https://dx.doi.org/10.1186/s43141-023-00583-w kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 21 2023 1 14 11
language	English
source	Enthalten in Journal of Genetic Engineering and Biotechnology 21(2023), 1 vom: 14. Nov. volume:21 year:2023 number:1 day:14 month:11
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topic_facet	HCV Humoral response Cellular responses CD4 CD8 Toxicity Antigenicity Docking scores Vaccine development
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authorswithroles_txt_mv	Muhammad, Ashraf M. @@aut@@ Salum, Ghada M. @@aut@@ Meguid, Mai Abd El @@aut@@ Fotouh, Basma E. @@aut@@ Dawood, Reham M. @@aut@@
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Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. 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author	Muhammad, Ashraf M.
spellingShingle	Muhammad, Ashraf M. misc HCV misc Humoral response misc Cellular responses misc CD4 misc CD8 misc Toxicity misc Antigenicity misc Docking scores misc Vaccine development Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study
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topic_title	Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study HCV (dpeaa)DE-He213 Humoral response (dpeaa)DE-He213 Cellular responses (dpeaa)DE-He213 CD4 (dpeaa)DE-He213 CD8 (dpeaa)DE-He213 Toxicity (dpeaa)DE-He213 Antigenicity (dpeaa)DE-He213 Docking scores (dpeaa)DE-He213 Vaccine development (dpeaa)DE-He213
topic	misc HCV misc Humoral response misc Cellular responses misc CD4 misc CD8 misc Toxicity misc Antigenicity misc Docking scores misc Vaccine development
topic_unstemmed	misc HCV misc Humoral response misc Cellular responses misc CD4 misc CD8 misc Toxicity misc Antigenicity misc Docking scores misc Vaccine development
topic_browse	misc HCV misc Humoral response misc Cellular responses misc CD4 misc CD8 misc Toxicity misc Antigenicity misc Docking scores misc Vaccine development
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title	Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study
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title_full	Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study
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author_browse	Muhammad, Ashraf M. Salum, Ghada M. Meguid, Mai Abd El Fotouh, Basma E. Dawood, Reham M.
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title_sort	bioinformatics analysis of multi-epitope peptide vaccines against hepatitis c virus: a molecular docking study
title_auth	Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study
abstract	Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. © The Author(s) 2023
abstractGer	Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. © The Author(s) 2023
abstract_unstemmed	Background Hepatitis C Virus (HCV) infection is one of the causal agents of liver disease burden. Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. Also, P2941 is strongly bound to T cell (CD4 and CD8) receptors. © The Author(s) 2023
collection_details	GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2027 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700
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title_short	Bioinformatics analysis of multi-epitope peptide vaccines against Hepatitis C virus: a molecular docking study
url	https://dx.doi.org/10.1186/s43141-023-00583-w
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author2	Salum, Ghada M. Meguid, Mai Abd El Fotouh, Basma E. Dawood, Reham M.
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up_date	2024-07-03T21:43:32.303Z
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Six multiple antigenic peptides were synthesized including (P315, P412, and P517) plus (P1771, P2121, and P2941) to induce humoral and cellular responses, respectively against HCV infection. Aim: This paper aimed to employ computational tools to evaluate the efficacy of each peptide individually and to determine the most effective one for better vaccine development and/or immunotherapy. Methods VaxiJen web and AllerTOP servers were used for antigenicity and allergenicity prediction, respectively. The ToxinPred web server was used to investigate the peptide toxicity. Each peptide was docked with its corresponding receptors. Results No peptides were expected to be toxic. P315 and P2941 are predicted to have robust antigenic properties, lowest allergenicity, and minimal sOPEP energies. In turn, P315 (derived from gpE1) formed the highest hydrophobic bonds with the BCR and CD81 receptors that will elicit B cell function. P2941 (derived from NS5B) was shown to strongly bind to both CD4 and CD8 receptors that will elicit T cell function. Conclusion P315 successfully bound to B cell (BCR and CD81) receptors. 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