Release of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex

Journal Article · Fri Jul 20 04:00:00 EDT 2012 · Virology

DOI:https://doi.org/10.1016/J.VIROL.2012.03.009· OSTI ID:22149284

Yang, Kui; Wills, Elizabeth G. ^[1]

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1. Department of Microbiology and Immunology, Cornell University, Ithaca, NY 14853 (United States)

We identify an NLS within herpes simplex virus scaffold proteins that is required for optimal nuclear import of these proteins into infected or uninfected nuclei, and is sufficient to mediate nuclear import of GFP. A virus lacking this NLS replicated to titers reduced by 1000-fold, but was able to make capsids containing both scaffold and portal proteins suggesting that other functions can complement the NLS in infected cells. We also show that Vp22a, the major scaffold protein, is sufficient to mediate the incorporation of portal protein into capsids, whereas proper portal immunoreactivity in the capsid requires the larger scaffold protein pU{sub L}26. Finally, capsid angularization in infected cells did not require the HSV-1 protease unless full length pU{sub L}26 was expressed. These data suggest that the HSV-1 portal undergoes conformational changes during capsid maturation, and reveal that full length pU{sub L}26 is required for this conformational change.

• OSTI ID: 22149284
• Journal Information: Virology, Journal Name: Virology Journal Issue: 1 Vol. 429; ISSN VIRLAX; ISSN 0042-6822
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
CLEAVAGE
CONFORMATIONAL CHANGES
ELECTRON MICROSCOPY
HERPES SIMPLEX
VIRUSES