ArticleJournal of virology2008
Multimerization of tegument protein pp28 within the assembly compartment is required for cytoplasmic envelopment of human cytomegalovirus.
Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Palmitoylation of the human cytomegalovirus tegument protein pp28 facilitates virus release.PLoS pathogens · 2026Article
- Features and Functions of the Conserved Herpesvirus Tegument Protein UL11 and Its Binding Partners.Frontiers in microbiology · 2022Review
- Phosphorylation of tegument protein pp28 contributes to trafficking to the assembly compartment in human cytomegalovirus infection.Journal of microbiology (Seoul, Korea) · 2020Article
- Human Cytomegalovirus Primary Infection and Reactivation: Insights From Virion-Carried Molecules.Frontiers in microbiology · 2020Review
- Article
- Distinct functional domains within the acidic cluster of tegument protein pp28 required for trafficking and cytoplasmic envelopment of human cytomegalovirus.The Journal of general virology · 2016Article
- Crystal Structure of Human Herpesvirus 6B Tegument Protein U14.PLoS pathogens · 2016Article
- Review
- Human cytomegalovirus pUL37x1-induced calcium flux activates PKCα, inducing altered cell shape and accumulation of cytoplasmic vesicles.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Review
- Viral mitochondria-localized inhibitor of apoptosis (UL37 exon 1 protein) does not protect human neural precursor cells from human cytomegalovirus-induced cell death.The Journal of general virology · 2012Article
- A mutation deleting sequences encoding the amino terminus of human cytomegalovirus UL84 impairs interaction with UL44 and capsid localization.Journal of virology · 2012Article
- Interaction between the human cytomegalovirus tegument proteins UL94 and UL99 is essential for virus replication.Journal of virology · 2012Article
- Viral and host control of cytomegalovirus maturation.Trends in microbiology · 2012Review
- The human cytomegalovirus (HCMV) tegument protein UL94 is essential for secondary envelopment of HCMV virions.Journal of virology · 2012Article
- A leucine zipper motif of a tegument protein triggers final envelopment of human cytomegalovirus.Journal of virology · 2012Article
- Identification of binary interactions between human cytomegalovirus virion proteins.Journal of virology · 2011Article
- Structure and capsid association of the herpesvirus large tegument protein UL36.Journal of virology · 2010Article
- Bicaudal D1-dependent trafficking of human cytomegalovirus tegument protein pp150 in virus-infected cells.Journal of virology · 2010Article
- The endoplasmic reticulum chaperone BiP/GRP78 is important in the structure and function of the human cytomegalovirus assembly compartment.Journal of virology · 2009Article
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2 authors.
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Abstract
Human cytomegalovirus (HCMV) UL99-encoded pp28 is an essential tegument protein required for envelopment and production of infectious virus. Nonenveloped virions accumulate in the cytoplasm of cells infected with recombinant viruses with the UL99 gene deleted. Previous results have suggested that a key function of pp28 in the envelopment of infectious HCMV is expressed after the protein localizes in the assembly compartment (AC). In this study, we investigated the potential role of pp28 multimerization in the envelopment of the infectious virion. Our results indicated that pp28 multimerized during viral infection and that interacting domains responsible for self-interaction were localized in the amino terminus of the protein (amino acids [aa] 1 to 43). The results from transient-expression and/or infection assays indicated that the self-interaction took place in the AC. A mutant pp28 molecule containing only the first 35 aa failed to accumulate in the AC, did not interact with pp28 in the AC, and could not support virus replication. In contrast, the first 50 aa of pp28 was sufficient for the self-interaction within the AC and the assembly of infectious virus. Recombinant viruses encoding an in-frame deletion of aa 26 to 33 of pp28 were replication competent, whereas infectious virus was not recovered from HCMV BACs lacking aa 26 to 43. These findings suggested that the accumulation of pp28 was a prerequisite for multimerization of pp28 within the AC and that pp28 multimerization in the AC represented an essential step in the envelopment and production of infectious virions.
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