5xea | pdb_00005xea
Structure of Thogoto virus envelope glycoprotein
Structural highlights
FunctionENV_THOGV Possible role in endocytotic fusion events during infection. Publication Abstract from PubMedThogotoviruses are emerging tick-borne zoonotic orthomyxoviruses infecting both humans and domestic animals with severe clinical consequences. These viruses utilize a single-envelope glycoprotein (Gp) to facilitate their entry into host cells. Here, we present the Gp structures of Thogoto and Dhori viruses, both of which are members of the Thogotovirus genus in the family Orthomyxoviridae These structures, determined in the postfusion conformation, identified them as class III viral fusion proteins. It is intriguing that the Gp structures are similar to the envelope protein of baculovirus, although sharing a low sequence identity of approximately 28%. Detailed structural and phylogenic analyses demonstrated that these Gps originated from a common ancestor. Among the structures, domain I is the most conserved region, particularly the fusion loops. Domain II showed the highest variability among different viruses, which might be related to their distinct host tropism. These findings increase our understanding of the divergent evolution processes of various orthomyxoviruses and indicate potential targets for developing antiviral therapeutics by intercepting virus entry. Structures of human-infecting Thogotovirus fusogens support a common ancestor with insect baculovirus.,Peng R, Zhang S, Cui Y, Shi Y, Gao GF, Qi J Proc Natl Acad Sci U S A. 2017 Oct 17;114(42):E8905-E8912. doi:, 10.1073/pnas.1706125114. Epub 2017 Oct 4. PMID:29073031[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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