{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zhang Y"],"funding":["Ocean University of China","Qingdao National Laboratory for Marine Science and Technology","Qingdao University","Natural Science Foundation of Shandong Province","National Natural Science Foundation of China"],"pagination":["105660"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10865405"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["300(2)"],"pubmed_abstract":["Persistent high-risk HPV infection is closely associated with cervical cancer development, and there is no drug targeting HPV on the market at present, so it is particularly important to understand the interaction mechanism between HPV and the host which may provide the novel strategies for treating HPV diseases. HPV can hijack cell surface heparan sulfate proteoglycans (HSPGs) as primary receptors. However, the secondary entry receptors for HPV remain elusive. We identify myosin-9 (NMHC-IIA) as a host factor that interacts with HPV L1 protein and mediates HPV internalization. Efficient HPV entry required myosin-9 redistribution to the cell surface regulated by HPV-hijacked MEK-MLCK signaling. Myosin-9 maldistribution by ML-7 or ML-9 significantly inhibited HPV pseudoviruses infection in v"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Myosin 9 and N-glycans jointly regulate human papillomavirus entry."],"pmcid":["PMC10865405"],"funding_grant_id":["81874320","82173860","CHO677","CHO745","2022QNLM030003"],"pubmed_authors":["He F","Liu YJ","Zhang Y","Jiang H","Wang W","Hao C","Liu W"],"additional_accession":[]},"is_claimable":false,"name":"Myosin 9 and N-glycans jointly regulate human papillomavirus entry.","description":"Persistent high-risk HPV infection is closely associated with cervical cancer development, and there is no drug targeting HPV on the market at present, so it is particularly important to understand the interaction mechanism between HPV and the host which may provide the novel strategies for treating HPV diseases. HPV can hijack cell surface heparan sulfate proteoglycans (HSPGs) as primary receptors. However, the secondary entry receptors for HPV remain elusive. We identify myosin-9 (NMHC-IIA) as a host factor that interacts with HPV L1 protein and mediates HPV internalization. Efficient HPV entry required myosin-9 redistribution to the cell surface regulated by HPV-hijacked MEK-MLCK signaling. Myosin-9 maldistribution by ML-7 or ML-9 significantly inhibited HPV pseudoviruses infection in v","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2026-06-11T06:07:54.81Z","creation":"2025-04-21T15:19:29.562Z"},"accession":"S-EPMC10865405","cross_references":{"pubmed":["38242322"],"doi":["10.1016/j.jbc.2024.105660"]}}