Monkeypox Virus Aggressively Invades via GP120 Domains and PI3K/GTPase-like System of F13 Protein

05 October 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Infection with the monkeypox virus (MPXV) causes a condition comparable to that of smallpox, albeit with fewer symptoms and severity. The typical magnitude and duration of monkeypox epidemics will increase as human protection from the smallpox vaccine wanes. In this study, the bioinformatics technique of domain search was utilized to investigate the biological function of the F13 protein of the E protein of the monkeypox virus. According to the research annotation results, the F13 protein has G120, EF-hand, Protein kinase(PI3K) and phosphatase(PPM), GB1/RHD3-type, GAP/GEF, PhoLip ATPase, and Dynamin GTPase domains. The PI3K domain regulates Dynamin GTPase activity in a unique manner. This shows that the monkeypox virus binds to cellular receptors in a manner similar to HIV and then completes the membrane fusion process by mechanisms PI3K and GTPase -like system.


Protein kinase
Phospholipid transporting


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