{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lakshmanan RV"],"funding":["NIH R21","NIAID NIH HHS","NIGMS NIH HHS","NIH HHS"],"pagination":["1922"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9505059"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["14(9)"],"pubmed_abstract":["Parvovirus B19 (B19V) is a human pathogen that is the causative agent of fifth disease in children. It is also known to cause hydrops in fetuses, anemia in AIDS patients, and transient aplastic crisis in patients with sickle cell disease. The unique N-terminus of Viral Protein 1 (VP1u) of parvoviruses, including B19V, exhibits phospholipase A<sub>2</sub> (PLA<sub>2</sub>) activity, which is required for endosomal escape. Presented is the structural dynamics of B19V VP1u under conditions that mimic the pHs of cell entry and endosomal trafficking to the nucleus. Using circular dichroism spectroscopy, the receptor-binding domain of B19V VP1u is shown to exhibit an α-helical fold, whereas the PLA<sub>2</sub> domain exhibits a probable molten globule state, both of which are pH invariant. Diffe"],"journal":["Viruses"],"pubmed_title":["Structural Dynamics and Activity of B19V VP1u during the pHs of Cell Entry and Endosomal Trafficking."],"pmcid":["PMC9505059"],"funding_grant_id":["R01 GM109524","AI126583","R01 GM082946","R21 AI126583"],"pubmed_authors":["Burg M","Hull JA","Berry L","Bothner B","Agbandje-McKenna M","Lakshmanan RV","McKenna R"],"additional_accession":[]},"is_claimable":false,"name":"Structural Dynamics and Activity of B19V VP1u during the pHs of Cell Entry and Endosomal Trafficking.","description":"Parvovirus B19 (B19V) is a human pathogen that is the causative agent of fifth disease in children. It is also known to cause hydrops in fetuses, anemia in AIDS patients, and transient aplastic crisis in patients with sickle cell disease. The unique N-terminus of Viral Protein 1 (VP1u) of parvoviruses, including B19V, exhibits phospholipase A<sub>2</sub> (PLA<sub>2</sub>) activity, which is required for endosomal escape. Presented is the structural dynamics of B19V VP1u under conditions that mimic the pHs of cell entry and endosomal trafficking to the nucleus. Using circular dichroism spectroscopy, the receptor-binding domain of B19V VP1u is shown to exhibit an α-helical fold, whereas the PLA<sub>2</sub> domain exhibits a probable molten globule state, both of which are pH invariant. Diffe","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2026-04-08T11:50:02.766Z","creation":"2025-02-19T00:44:03.558Z"},"accession":"S-EPMC9505059","cross_references":{"pubmed":["36146728"],"doi":["10.3390/v14091922"]}}