HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors
Abstract Herpes virus1(HSV1) is a neurotropic virus that has been linked to Alzheimer’s disease. An In-silico structural homology search using α -Bgtx, identified structural homology between HSV1 gD and the nicotinic receptor neurotoxin α-Bgtx. SPR binding studies using acetylcholine binding protein...
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| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-06-01
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| Series: | npj Viruses |
| Online Access: | https://doi.org/10.1038/s44298-025-00109-w |
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| _version_ | 1849472901792661504 |
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| author | Sabina Yeasmin Kavita Sharma Christopher Nicolet Laura DeCristofano Yeganeh Ataian Arina Ranjit Ali Aghazadeh-Habashi Dong Xu Marvin Schulte |
| author_facet | Sabina Yeasmin Kavita Sharma Christopher Nicolet Laura DeCristofano Yeganeh Ataian Arina Ranjit Ali Aghazadeh-Habashi Dong Xu Marvin Schulte |
| author_sort | Sabina Yeasmin |
| collection | DOAJ |
| description | Abstract Herpes virus1(HSV1) is a neurotropic virus that has been linked to Alzheimer’s disease. An In-silico structural homology search using α -Bgtx, identified structural homology between HSV1 gD and the nicotinic receptor neurotoxin α-Bgtx. SPR binding studies using acetylcholine binding protein from Lymnaea stagnalis, and functional two electrode voltage clamp studies of α7 nAChRs demonstrate the ability of HSV1 to interact directly with nAChRs. Molecular docking studies support the binding of a neurotoxin-like binding loop in HSV1 to a binding site similar to the neurotoxin binding domain. Interaction of HSV1 with nAChRs provides novel insights into a potential mechanism of action of HSV and its potential role in Alzheimer’s disease. |
| format | Article |
| id | doaj-art-33191f5d72ad4401b5aaf8a95045fa8f |
| institution | Kabale University |
| issn | 2948-1767 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | npj Viruses |
| spelling | doaj-art-33191f5d72ad4401b5aaf8a95045fa8f2025-08-20T03:24:22ZengNature Portfolionpj Viruses2948-17672025-06-013111310.1038/s44298-025-00109-wHSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptorsSabina Yeasmin0Kavita Sharma1Christopher Nicolet2Laura DeCristofano3Yeganeh Ataian4Arina Ranjit5Ali Aghazadeh-Habashi6Dong Xu7Marvin Schulte8Department of Biomedical and Pharmaceutical Sciences, Idaho State UniversityDepartment of Biomedical and Pharmaceutical Sciences, Idaho State UniversityDepartment of Biomedical and Pharmaceutical Sciences, Idaho State UniversityDepartment of Pharmaceutical Sciences, Saint Joseph’s UniversityDepartment of Chemistry and Biochemistry, University of Alaska FairbanksDepartment of Biomedical and Pharmaceutical Sciences, Idaho State UniversityDepartment of Biomedical and Pharmaceutical Sciences, Idaho State UniversityDepartment of Biomedical and Pharmaceutical Sciences, Idaho State UniversityDepartment of Biomedical and Pharmaceutical Sciences, Idaho State UniversityAbstract Herpes virus1(HSV1) is a neurotropic virus that has been linked to Alzheimer’s disease. An In-silico structural homology search using α -Bgtx, identified structural homology between HSV1 gD and the nicotinic receptor neurotoxin α-Bgtx. SPR binding studies using acetylcholine binding protein from Lymnaea stagnalis, and functional two electrode voltage clamp studies of α7 nAChRs demonstrate the ability of HSV1 to interact directly with nAChRs. Molecular docking studies support the binding of a neurotoxin-like binding loop in HSV1 to a binding site similar to the neurotoxin binding domain. Interaction of HSV1 with nAChRs provides novel insights into a potential mechanism of action of HSV and its potential role in Alzheimer’s disease.https://doi.org/10.1038/s44298-025-00109-w |
| spellingShingle | Sabina Yeasmin Kavita Sharma Christopher Nicolet Laura DeCristofano Yeganeh Ataian Arina Ranjit Ali Aghazadeh-Habashi Dong Xu Marvin Schulte HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors npj Viruses |
| title | HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors |
| title_full | HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors |
| title_fullStr | HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors |
| title_full_unstemmed | HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors |
| title_short | HSV1 glycoprotein D utilizes an LY6-like binding domain to inhibit alpha7 nicotinic receptors |
| title_sort | hsv1 glycoprotein d utilizes an ly6 like binding domain to inhibit alpha7 nicotinic receptors |
| url | https://doi.org/10.1038/s44298-025-00109-w |
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