Latent nuclear antigen of Kaposi's sarcoma-associated herpesvirus interacts with RING3, a homolog of the Drosophila female sterile homeotic (fsh) gene

Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) is the likely infectious cause of Kaposi's sarcoma, primary effusion lymphoma, and some cases of multicentric Castleman's disease. Its latent nuclear antigen (LANA) is expressed in the nuclei of latently infected cells and may play...

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Bibliographic Details
Published in:Journal of virology 1999-12, Vol.73 (12), p.9789-9795
Main Authors: Platt, G M, Simpson, G R, Mittnacht, S, Schulz, T F
Format: Article
Language:English
Subjects:
AIDS/HIV
Animals
Binding Sites
Cell Line
Cell Line, Transformed
Chromosome Mapping
Drosophila - genetics
episomes
Female
fsh gene
Genes, Insect
Herpesvirus 8, Human
Human herpesvirus 8
Humans
Kaposi's sarcoma-associated herpesvirus
latent nuclear antigen
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Phosphoproteins
Phosphorylation
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Rabbits
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
RING-3 protein
Spodoptera - cytology
Tumor Cells, Cultured
Virus-Cell Interactions
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Summary:Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) is the likely infectious cause of Kaposi's sarcoma, primary effusion lymphoma, and some cases of multicentric Castleman's disease. Its latent nuclear antigen (LANA) is expressed in the nuclei of latently infected cells and may play a role in the persistence of episomal viral DNA in dividing cells. Here we report that LANA interacts with RING3, a nuclear protein and member of the Drosophila fsh (female sterile homeotic) family of proteins, some of which have previously been implicated in controlling gene expression. Binding of RING3 to LANA involves the ET domain, characteristic of fsh-related proteins, suggesting that this highly conserved region is involved in protein-protein interactions. The interaction between RING3 and LANA results in phosphorylation of serine and threonine residues located between amino acids 951 and 1107 in the carboxy-terminal region of LANA. However, RING3 is not itself a kinase but appears to recruit an as yet unidentified serine/threonine protein kinase into the complex which it forms with LANA.
ISSN:0022-538X
1098-5514
DOI:10.1128/JVI.73.12.9789-9795.1999