6gg0
Cryo-EM structure of BK polyomavirus like particle in complex with single chain antibody ScFv41F17Cryo-EM structure of BK polyomavirus like particle in complex with single chain antibody ScFv41F17
Structural highlights
Function[Q65613_POVBK] Forms an icosahedral capsid with a T=7 symmetry.[PIRNR:PIRNR003376] Publication Abstract from PubMedHuman polyomaviruses cause a common childhood infection worldwide and typically elicit a neutralizing antibody and cellular immune response, while establishing a dormant infection in the kidney with minimal clinical manifestations. However, viral reactivation can cause severe pathology in immunocompromised individuals. We developed a high-throughput, functional antibody screen to examine the humoral response to BK polyomavirus. This approach enabled the isolation of antibodies from all peripheral B cell subsets and revealed the anti-BK virus antibody repertoire as clonally complex with respect to immunoglobulin sequences and isotypes (both IgM and IgG), including a high frequency of monoclonal antibodies that broadly neutralize BK virus subtypes and the related JC polyomavirus. Cryo-electron microscopy of a broadly neutralizing IgG single-chain variable fragment complexed with BK virus-like particles revealed the quaternary nature of a conserved viral epitope at the junction between capsid pentamers. These features unravel a potent modality for inhibiting polyomavirus infection in kidney transplant recipients and other immunocompromised patients. Human Memory B Cells Harbor Diverse Cross-Neutralizing Antibodies against BK and JC Polyomaviruses.,Lindner JM, Cornacchione V, Sathe A, Be C, Srinivas H, Riquet E, Leber XC, Hein A, Wrobel MB, Scharenberg M, Pietzonka T, Wiesmann C, Abend J, Traggiai E Immunity. 2019 Feb 16. pii: S1074-7613(19)30048-2. doi:, 10.1016/j.immuni.2019.02.003. PMID:30824324[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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