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.
journal_name
Virologyjournal_title
Virologyauthors
Sánchez-Martínez C,Grueso E,Carroll M,Rommelaere J,Almendral JMdoi
10.1016/j.virol.2012.05.025subject
Has Abstractpub_date
2012-10-10 00:00:00pages
45-56issue
1eissn
0042-6822issn
1096-0341pii
S0042-6822(12)00276-0journal_volume
432pub_type
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