Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses
Raman spectroscopy was applied to study the structural differences between herpes simplex virus Type I (HSV-1) and Epstein–Barr virus (EBV). Raman spectra were first collected with statistical validity on clusters of the respective virions and analyzed according to principal component analysis (PCA)...
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MDPI AG
2023-10-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/21/15567 |
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| author | Giuseppe Pezzotti Eriko Ohgitani Hayata Imamura Saki Ikegami Masaharu Shin-Ya Tetsuya Adachi Keiji Adachi Toshiro Yamamoto Narisato Kanamura Elia Marin Wenliang Zhu Koichiro Higasa Yoshiki Yasukochi Kazu Okuma Osam Mazda |
| author_facet | Giuseppe Pezzotti Eriko Ohgitani Hayata Imamura Saki Ikegami Masaharu Shin-Ya Tetsuya Adachi Keiji Adachi Toshiro Yamamoto Narisato Kanamura Elia Marin Wenliang Zhu Koichiro Higasa Yoshiki Yasukochi Kazu Okuma Osam Mazda |
| author_sort | Giuseppe Pezzotti |
| collection | DOAJ |
| description | Raman spectroscopy was applied to study the structural differences between herpes simplex virus Type I (HSV-1) and Epstein–Barr virus (EBV). Raman spectra were first collected with statistical validity on clusters of the respective virions and analyzed according to principal component analysis (PCA). Then, average spectra were computed and a machine-learning approach applied to deconvolute them into sub-band components in order to perform comparative analyses. The Raman results revealed marked structural differences between the two viral strains, which could mainly be traced back to the massive presence of carbohydrates in the glycoproteins of EBV virions. Clear differences could also be recorded for selected tyrosine and tryptophan Raman bands sensitive to pH at the virion/environment interface. According to the observed spectral differences, Raman signatures of known biomolecules were interpreted to link structural differences with the viral functions of the two strains. The present study confirms the unique ability of Raman spectroscopy for answering structural questions at the molecular level in virology and, despite the structural complexity of viral structures, its capacity to readily and reliably differentiate between different virus types and strains. |
| first_indexed | 2024-03-11T11:29:57Z |
| format | Article |
| id | doaj.art-a42af5f8393544c29b62f0d7bb9f8dcf |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T11:29:57Z |
| publishDate | 2023-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-a42af5f8393544c29b62f0d7bb9f8dcf2023-11-10T15:04:27ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-10-0124211556710.3390/ijms242115567Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr VirusesGiuseppe Pezzotti0Eriko Ohgitani1Hayata Imamura2Saki Ikegami3Masaharu Shin-Ya4Tetsuya Adachi5Keiji Adachi6Toshiro Yamamoto7Narisato Kanamura8Elia Marin9Wenliang Zhu10Koichiro Higasa11Yoshiki Yasukochi12Kazu Okuma13Osam Mazda14Ceramic Physics Laboratory, Kyoto Institute of Technology, Sakyo-Ku, Matsugasaki, Kyoto 606-8585, JapanDepartment of Immunology, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, 465 Kajii-Cho, Kyoto 602-8566, JapanCeramic Physics Laboratory, Kyoto Institute of Technology, Sakyo-Ku, Matsugasaki, Kyoto 606-8585, JapanCeramic Physics Laboratory, Kyoto Institute of Technology, Sakyo-Ku, Matsugasaki, Kyoto 606-8585, JapanDepartment of Immunology, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, 465 Kajii-Cho, Kyoto 602-8566, JapanDepartment of Immunology, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, 465 Kajii-Cho, Kyoto 602-8566, JapanDepartment of Dental Medicine, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, Kyoto 602-8566, JapanDepartment of Dental Medicine, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, Kyoto 602-8566, JapanDepartment of Dental Medicine, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, Kyoto 602-8566, JapanCeramic Physics Laboratory, Kyoto Institute of Technology, Sakyo-Ku, Matsugasaki, Kyoto 606-8585, JapanCeramic Physics Laboratory, Kyoto Institute of Technology, Sakyo-Ku, Matsugasaki, Kyoto 606-8585, JapanGenome Analysis, Institute of Biomedical Science, Kansai Medical University, 2-3-1 Shinmachi, Hirakata 573-1191, JapanGenome Analysis, Institute of Biomedical Science, Kansai Medical University, 2-3-1 Shinmachi, Hirakata 573-1191, JapanDepartment of Microbiology, School of Medicine, Kansai Medical University, 2-5-1 Shinmachi, Hirakata 573-1010, JapanDepartment of Immunology, Graduate School of Medical Science, Kyoto Prefectural University of Medicine, Kamigyo-Ku, 465 Kajii-Cho, Kyoto 602-8566, JapanRaman spectroscopy was applied to study the structural differences between herpes simplex virus Type I (HSV-1) and Epstein–Barr virus (EBV). Raman spectra were first collected with statistical validity on clusters of the respective virions and analyzed according to principal component analysis (PCA). Then, average spectra were computed and a machine-learning approach applied to deconvolute them into sub-band components in order to perform comparative analyses. The Raman results revealed marked structural differences between the two viral strains, which could mainly be traced back to the massive presence of carbohydrates in the glycoproteins of EBV virions. Clear differences could also be recorded for selected tyrosine and tryptophan Raman bands sensitive to pH at the virion/environment interface. According to the observed spectral differences, Raman signatures of known biomolecules were interpreted to link structural differences with the viral functions of the two strains. The present study confirms the unique ability of Raman spectroscopy for answering structural questions at the molecular level in virology and, despite the structural complexity of viral structures, its capacity to readily and reliably differentiate between different virus types and strains.https://www.mdpi.com/1422-0067/24/21/15567herpes simplex virus type IEpstein–Barr virusRaman spectroscopyglycoproteinssurface pHsecondary protein structure |
| spellingShingle | Giuseppe Pezzotti Eriko Ohgitani Hayata Imamura Saki Ikegami Masaharu Shin-Ya Tetsuya Adachi Keiji Adachi Toshiro Yamamoto Narisato Kanamura Elia Marin Wenliang Zhu Koichiro Higasa Yoshiki Yasukochi Kazu Okuma Osam Mazda Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses International Journal of Molecular Sciences herpes simplex virus type I Epstein–Barr virus Raman spectroscopy glycoproteins surface pH secondary protein structure |
| title | Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses |
| title_full | Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses |
| title_fullStr | Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses |
| title_full_unstemmed | Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses |
| title_short | Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses |
| title_sort | raman multi omic snapshot and statistical validation of structural differences between herpes simplex type i and epstein barr viruses |
| topic | herpes simplex virus type I Epstein–Barr virus Raman spectroscopy glycoproteins surface pH secondary protein structure |
| url | https://www.mdpi.com/1422-0067/24/21/15567 |
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