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- W2077695260 abstract "The unordered N-termini of parvovirus capsid proteins (Nt) are translocated through a channel at the icosahedral five-fold axis to serve for virus traffick. Heterologous peptides were genetically inserted at the Nt of MVM to study their functional tolerance to manipulations. Insertion of a 5T4-single-chain antibody at VP2-Nt (2Nt) yielded chimeric capsid subunits failing to enter the nucleus. The VEGFR2-binding peptide (V1) inserted at both 2Nt and VP1-Nt efficiently assembled in virions, but V1 disrupted VP1 and VP2 entry functions. The VP2 defect correlated with restricted externalization of V1-2Nt out of the coat. The specific infectivity of MVM and wtVP-pseudotyped mosaic MVM-V1 virions, upon heating and/or partial 2Nt cleavage, demonstrated that some 2Nt domains become intracellularly translocated out of the virus shell and cleaved to initiate entry. The V1 insertion defines a VP2-driven endosomal enlargement of the channel as an essential structural rearrangement performed by the MVM virion to infect." @default.
- W2077695260 created "2016-06-24" @default.
- W2077695260 creator A5056504955 @default.
- W2077695260 creator A5059234407 @default.
- W2077695260 creator A5072084139 @default.
- W2077695260 creator A5086836093 @default.
- W2077695260 creator A5091282555 @default.
- W2077695260 date "2012-10-01" @default.
- W2077695260 modified "2023-09-26" @default.
- W2077695260 title "Essential role of the unordered VP2 n-terminal domain of the parvovirus MVM capsid in nuclear assembly and endosomal enlargement of the virion fivefold channel for cell entry" @default.
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- W2077695260 doi "https://doi.org/10.1016/j.virol.2012.05.025" @default.
- W2077695260 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22727830" @default.
- W2077695260 hasPublicationYear "2012" @default.
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