KSHV ORF67 encoded lytic protein localizes on the nuclear membrane and alters emerin distribution

• Published in: Virus research Vol. 175; no. 2; pp. 143 - 150
• Main Authors: Farina, Antonella, Santarelli, Roberta, Bloise, Rossella, Gonnella, Roberta, Granato, Marisa, Bei, Roberto, Modesti, Andrea, Cirone, Mara, Bengtsson, Luiza, Angeloni, Antonio, Faggioni, Alberto
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.08.2013
• Subjects: Cell Line; Herpesvirus 8, Human - physiology; Host-Pathogen Interactions; Human herpesvirus 8; Humans; KSHV; Membrane Proteins - metabolism; neoplasm cells; Nuclear envelope; Nuclear Envelope - chemistry; nuclear membrane; Nuclear Proteins - metabolism; nucleocapsid; ORF67; ORF69; proteins; Viral egress; Viral Proteins - metabolism; Virus Replication; ORF69; ORF67; KSHV; Nuclear envelope; Viral egress
• ISSN: 0168-1702; 1872-7492
• DOI: 10.1016/j.virusres.2013.04.001

p29, a newly identified Kaposi's sarcoma-associated herpesvirus (KSHV) protein, is the product of ORF67, the positional homolog of the conserved herpesvirus protein UL34. Like its homologues in other herpesviruses, p29 is expressed early during viral lytic cycle, and is localized on the nuclear rim. Upon chemical induction of viral replication in primary effusion lymphoma cells, p29 interacts with p33, encoded by ORF69, the positional homolog of the conserved herpesvirus protein UL31, and both proteins colocalize on the nuclear membrane. IFA and biochemical analysis of infected or transfected cells showed that p29 expression resulted in delocalization and hyperphosphorylation of emerin, whereas other nuclear lamin associated proteins, such as LUMA, LB1 and LBR were not affected. Mislocalization of emerin was robustly increased upon combined expression of p29 and p33, suggesting that emerin destabilization might represent the first step in nuclear lamina disassembling, a process necessary for nucleocapsid maturation.