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Prediction of three-independent scales endowed on poliovirus proteinase 2A sequence
Naganori Numao1, Yoshiyuki Fukazawa, Kazuyoshi Tanaka
1BioFrontier Institute Inc., Sagamihara, Japan. fukazawa@kanagawa-iri.go.jp
Abstract:
Mulliken's electronegativity (M) scale was found as a parameterization to predict (elucidate) a virtually specific interaction between Poliovirus proteinase 2A and mitogen-activated protein (MAP) kinase p38α, as well as that between the 2A and apoptotic protein activating factor 1c (Apaf 1c) (or prion) with intermolecular frequency symmetry (IFS) rule. Also, Lacey's hydropathical (H) scale and Garel's (G) one could be found in the specific relationship between the 2A and the extracellular signal-regulated kinase 2 (ERK2) [or fibroblast growth factor receptor 3 (FGFR3)], and that between the 2A and the c-Jun N-terminal kinase 2 (JNK2) [or forkhead box P2-1 (FOXP2-1)], respectively. Based on these, both the same physicochemical scale and almost the same resonant frequency (f) value would be conserved in the same succession of a signal transduction process in a Poliovirus-infected cell. Furthermore, the 2A could play a trigger role to cause cancer, prion disease, bone disease, or speech and language disorder.
Insights
Poliovirus proteinase 2A interacts with key human proteins, suggesting its role in diseases like cancer and prion disorders. Physicochemical scales predict these specific interactions, revealing conserved patterns in infected cells.
Area of Science:
- Biochemistry
- Virology
- Molecular Biology
Background:
- Poliovirus proteinase 2A (2A) is a viral enzyme with known roles in replication.
- Specific interactions between viral proteins and host cell machinery are crucial for viral pathogenesis.
- Understanding these interactions can reveal new therapeutic targets and disease mechanisms.
Purpose of the Study:
- To investigate the specific interactions between Poliovirus proteinase 2A and host cell proteins using physicochemical scales.
- To explore the potential role of these interactions in disease development, including cancer and prion diseases.
- To identify conserved physicochemical properties and resonant frequencies in signal transduction pathways.
Main Methods:
- Application of Mulliken's electronegativity (M) scale to predict interactions between 2A and MAP kinase p38α, and 2A and Apaf 1c/prion.
- Utilizing Lacey's hydropathical (H) scale and Garel's (G) scale to analyze interactions between 2A and ERK2/FGFR3, and 2A and JNK2/FOXP2-1.
- Analysis of intermolecular frequency symmetry (IFS) rules.
Main Results:
- Mulliken's scale successfully predicted specific interactions between 2A and p38α, and 2A and Apaf 1c/prion.
- Lacey's and Garel's scales identified specific relationships between 2A and ERK2/FGFR3, and 2A and JNK2/FOXP2-1.
- Conserved physicochemical scales and resonant frequencies were observed in signal transduction within Poliovirus-infected cells.
Conclusions:
- Poliovirus 2A engages in specific interactions with multiple human signaling proteins, including MAP kinases and apoptotic factors.
- These interactions, predictable by physicochemical scales, suggest a conserved mechanism in viral-host cell signaling.
- Poliovirus 2A may act as a trigger for various diseases, including cancer, prion diseases, and neurological disorders, highlighting its broader pathogenic potential.
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