Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses
Abstract
:1. Introduction
2. Results
2.1. Average Raman Spectra and Assignments of Deconvoluted Sub-Bands
2.2. PCA Statistical Analysis and Raman Barcoding
3. Discussion
3.1. Raman Fingerprints of Structural Differences between HSV-1 and EBV
3.2. Raman Evidences for O-Glycosylation in EBV
3.3. Comparison and Validation through the Literature Data from Raman and Other Analytical Methods
4. Materials and Methods
4.1. Virus Samples
4.2. Raman Samples and Spectroscopic Procedures
4.3. Statistical Analyses and Buildup of Raman Barcodes
5. Conclusions
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Structural Difference | Raman Fingerprints | Implications |
---|---|---|
Carbohydrate signals: stronger in EBV than HSV-1 | 940, 983, 1054, and 1088 cm−1 (C−C & C−O stretching in Glc ring) 1250~1360 cm−1 (CH2 twisting & wagging) | These signals reveal the prominent presence of glycoproteins in EBV |
Tyrosine ratio, RTyr = I851/I823, higher in EBV than HSV-1 | 851/823 cm−1 tyrosine doublet (in-plane & out-of-plane ring vibrations) | Significantly more acidic pH at EBV virion/environment interface |
Differences in Raman genomic structures between EBV and HSV-1 | 1528 (C) &1374 (T) cm−1 (ring stretching in pyrimidines) 1336 (A) & 1485 (G) cm−1 (C−N ring stretching in purines) | Different fractions of purines and pyrimidines as expected from different genome structures |
Differences in protein secondary structure: β-sheet/β-turn fractions higher in EBV than HSV-1 | Amide I bands: 1634~1636 cm−1 → β-sheet 1653 cm−1 → α-sheet 1669 cm−1 → random coil 1686/1705 cm−1 → β-turn | More rigid protein structure in EBV; it also justifies the stronger threonine signals found in EBV |
Increased tryptophan torsional angle, χ2,1, in EBV as compared to HSV-1 | 1557 → 1551 cm−1 (C=C stretching in tryptophan pyrrole ring) | Higher hydrophilicity in EBV helps to retain temperature and pH during latency |
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Pezzotti, G.; Ohgitani, E.; Imamura, H.; Ikegami, S.; Shin-Ya, M.; Adachi, T.; Adachi, K.; Yamamoto, T.; Kanamura, N.; Marin, E.; et al. Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses. Int. J. Mol. Sci. 2023, 24, 15567. https://doi.org/10.3390/ijms242115567
Pezzotti G, Ohgitani E, Imamura H, Ikegami S, Shin-Ya M, Adachi T, Adachi K, Yamamoto T, Kanamura N, Marin E, et al. Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses. International Journal of Molecular Sciences. 2023; 24(21):15567. https://doi.org/10.3390/ijms242115567
Chicago/Turabian StylePezzotti, Giuseppe, Eriko Ohgitani, Hayata Imamura, Saki Ikegami, Masaharu Shin-Ya, Tetsuya Adachi, Keiji Adachi, Toshiro Yamamoto, Narisato Kanamura, Elia Marin, and et al. 2023. "Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein–Barr Viruses" International Journal of Molecular Sciences 24, no. 21: 15567. https://doi.org/10.3390/ijms242115567