Adeno-Associated Virus Type 2 Capsids with Externalized VP1/VP2 Trafficking Domains Are Generated prior to Passage through the Cytoplasm and Are Maintained until Uncoating Occurs in the Nucleus

Common features of parvovirus capsids are open pores at the fivefold symmetry axes that traverse the virion shell. Upon limited heat treatment in vitro, the pores can function as portals to externalize VP1/VP2 protein N-terminal sequences which harbor infection-relevant functional domains, such as a...

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Bibliographic Details
Main Authors: Sonntag, Florian, Bleker, Svenja, Leuchs, Barbara, Fischer, Roger, Kleinschmidt, Jürgen A.
Format: Artigo
Language:Inglês
Published: American Society for Microbiology 2006
Subjects:
Virus-Cell Interactions
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC1642181/
https://ncbi.nlm.nih.gov/pubmed/16956943
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JVI.01056-06
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