Encapsidation of viral DNA requires the adenovirus L1 52/55-kilodalton protein

Previous work demonstrated that the adenovirus L1 52/55-kDa protein is required for assembly of viral particles, although its exact role in the assembly process is unclear. The 52/55-kDa protein's early expression, however, suggests that it might have other roles at earlier times during infecti...

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Bibliographic Details
Published in:Journal of virology Vol. 72; no. 10; p. 7860
Main Authors: Gustin, K E, Imperiale, M J
Format: Journal Article
Language:English
Published: United States 01.10.1998
Subjects:
Adenoviridae - genetics
Adenoviridae - physiology
Base Sequence
Capsid - genetics
Cell Line
DNA Primers
DNA, Viral - genetics
Genome, Viral
Humans
Microscopy, Electron
Viral Proteins - genetics
Virus Assembly
ISSN:0022-538X
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Summary:Previous work demonstrated that the adenovirus L1 52/55-kDa protein is required for assembly of viral particles, although its exact role in the assembly process is unclear. The 52/55-kDa protein's early expression, however, suggests that it might have other roles at earlier times during infection. To uncover any role the 52/55-kDa protein might have at early times and to better characterize its role in assembly, a mutant adenovirus incapable of expressing the 52/55-kDa protein was constructed (H5pm8001). Analysis of the onset and extent of DNA replication and late protein synthesis revealed that H5pm8001-infected 293 cells entered the late stage of infection at the same time as did adenovirus type 5 (Ad5)-infected cells. Interestingly, H5pm8001-infected cells displayed slightly lower levels of replicated viral DNA and late proteins, suggesting that although not required, the 52/55-kDa protein does augment these activities during infection. Analysis of transcripts produced from the major late and IVa2 promoters indicated a slight reduction in H5pm8001-infected compared to Ad5-infected cells at 18 h postinfection that was not apparent at later times. Analysis of particles formed in H5pm8001 cells revealed that empty capsids could form, suggesting that the 52/55-kDa protein does not function as a scaffolding protein. Subsequent characterization of these particles demonstrated that they lacked any associated viral DNA. These findings indicate that the 52/55 kDa-protein is required to mediate stable association between the viral DNA and empty capsid and suggest that it functions in the DNA encapsidation process.
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ISSN:0022-538X
DOI:10.1128/jvi.72.10.7860-7870.1998