In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting
IntroductionThe Nipah virus (NiV), a zoonotic paramyxovirus closely related to the Hendra virus, poses a significant global health threat due to its high mortality rate, zoonotic nature, and recurring outbreaks primarily in Malaysia, Bangladesh, and India. Infection with NiV leads to severe encephal...
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Frontiers Media S.A.
2025-06-01
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| Series: | Frontiers in Bioinformatics |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fbinf.2025.1526566/full |
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| author | Ayesha Sajjad Ihteshamul Haq Rabia Syed Faheem Anwar Muhammad Hamza Muhammad Hamza Muhammad Musharaf Tehmina Kiani Faisal Nouroz |
| author_facet | Ayesha Sajjad Ihteshamul Haq Rabia Syed Faheem Anwar Muhammad Hamza Muhammad Hamza Muhammad Musharaf Tehmina Kiani Faisal Nouroz |
| author_sort | Ayesha Sajjad |
| collection | DOAJ |
| description | IntroductionThe Nipah virus (NiV), a zoonotic paramyxovirus closely related to the Hendra virus, poses a significant global health threat due to its high mortality rate, zoonotic nature, and recurring outbreaks primarily in Malaysia, Bangladesh, and India. Infection with NiV leads to severe encephalitis and carries a case fatality rate ranging from 40% to 75%. The lack of a vaccine and limited understanding of NiV pathogenesis underscore the urgent need for effective therapeutics. This study focuses on identifying viral peptides of the Nipah virus using the peptide mass fingerprinting technique. This approach identified antiviral peptides acting as potent inhibitors, targeting the viral G-protein’s interaction with cellular ephrin-B2 and B3 receptors. These receptors are crucial for viral entry into host cells and subsequent pathogenesis.MethodsIdentifying NiV viral peptides not only enhances our understanding of the virus’s structural and functional properties but also opens avenues for developing novel therapeutic strategies. By blocking the interaction between the viral G-protein and host receptors, these antiviral peptides offer promising prospects for drug development against NiV.Results and DiscussionTwenty-one peptides were identified using peptide mass fingerprinting. These peptides were then subjected to docking analysis with two antiviral peptides of the ephrin B2 receptor and a monoclonal antibody, demonstrating robust stability and binding affinity. These predicted peptides contribute to the broader field of virology by elucidating key aspects of NiV biology and paving the way for the development of targeted antiviral therapies. Future studies may further explore the therapeutic potential of these peptides and their application in combating other viral infections. |
| format | Article |
| id | doaj-art-ca422b4b7c7c40e38641eab059b3e757 |
| institution | Kabale University |
| issn | 2673-7647 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Bioinformatics |
| spelling | doaj-art-ca422b4b7c7c40e38641eab059b3e7572025-08-20T03:32:24ZengFrontiers Media S.A.Frontiers in Bioinformatics2673-76472025-06-01510.3389/fbinf.2025.15265661526566In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprintingAyesha Sajjad0Ihteshamul Haq1Rabia Syed2Faheem Anwar3Muhammad Hamza4Muhammad Hamza5Muhammad Musharaf6Tehmina Kiani7Faisal Nouroz8Department of Bioinformatics, Govt. Postgraduate College Mandian Abbottabad, Abbotabad, Khyber Pakhtunkhwa, PakistanCollege of Life Sciences and Technology, Beijing University of Chemical Technology, Beijing, ChinaDepartment of Bioinformatics, Govt. Postgraduate College Mandian Abbottabad, Abbotabad, Khyber Pakhtunkhwa, PakistanAcademy of medical engineering and translational medicine Tianjin University China, Tianjin, ChinaDepartment of Bioinformatics, Govt. Postgraduate College Mandian Abbottabad, Abbotabad, Khyber Pakhtunkhwa, PakistanDepartment of Bioinformatics, Hazara University Mansehra, Dhodial, Khyber Pakhtunkhwa, PakistanDepartment of Bioinformatics, Govt. Postgraduate College Mandian Abbottabad, Abbotabad, Khyber Pakhtunkhwa, PakistanDepartment of Bioinformatics, Govt. Postgraduate College Mandian Abbottabad, Abbotabad, Khyber Pakhtunkhwa, PakistanDepartment of Bioinformatics, Hazara University Mansehra, Dhodial, Khyber Pakhtunkhwa, PakistanIntroductionThe Nipah virus (NiV), a zoonotic paramyxovirus closely related to the Hendra virus, poses a significant global health threat due to its high mortality rate, zoonotic nature, and recurring outbreaks primarily in Malaysia, Bangladesh, and India. Infection with NiV leads to severe encephalitis and carries a case fatality rate ranging from 40% to 75%. The lack of a vaccine and limited understanding of NiV pathogenesis underscore the urgent need for effective therapeutics. This study focuses on identifying viral peptides of the Nipah virus using the peptide mass fingerprinting technique. This approach identified antiviral peptides acting as potent inhibitors, targeting the viral G-protein’s interaction with cellular ephrin-B2 and B3 receptors. These receptors are crucial for viral entry into host cells and subsequent pathogenesis.MethodsIdentifying NiV viral peptides not only enhances our understanding of the virus’s structural and functional properties but also opens avenues for developing novel therapeutic strategies. By blocking the interaction between the viral G-protein and host receptors, these antiviral peptides offer promising prospects for drug development against NiV.Results and DiscussionTwenty-one peptides were identified using peptide mass fingerprinting. These peptides were then subjected to docking analysis with two antiviral peptides of the ephrin B2 receptor and a monoclonal antibody, demonstrating robust stability and binding affinity. These predicted peptides contribute to the broader field of virology by elucidating key aspects of NiV biology and paving the way for the development of targeted antiviral therapies. Future studies may further explore the therapeutic potential of these peptides and their application in combating other viral infections.https://www.frontiersin.org/articles/10.3389/fbinf.2025.1526566/fullpeptide mass fingerprintingparamyxovirusephrin B2 and B3 receptorviral g proteinnipah virus (NiV) |
| spellingShingle | Ayesha Sajjad Ihteshamul Haq Rabia Syed Faheem Anwar Muhammad Hamza Muhammad Hamza Muhammad Musharaf Tehmina Kiani Faisal Nouroz In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting Frontiers in Bioinformatics peptide mass fingerprinting paramyxovirus ephrin B2 and B3 receptor viral g protein nipah virus (NiV) |
| title | In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting |
| title_full | In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting |
| title_fullStr | In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting |
| title_full_unstemmed | In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting |
| title_short | In-silico molecular analysis and blocking of the viral G protein of Nipah virus interacting with ephrin B2 and B3 receptor by using peptide mass fingerprinting |
| title_sort | in silico molecular analysis and blocking of the viral g protein of nipah virus interacting with ephrin b2 and b3 receptor by using peptide mass fingerprinting |
| topic | peptide mass fingerprinting paramyxovirus ephrin B2 and B3 receptor viral g protein nipah virus (NiV) |
| url | https://www.frontiersin.org/articles/10.3389/fbinf.2025.1526566/full |
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