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Updated: Mar 27, 2026
Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line
Published on: September 28, 2022
Epstein-Barr virus glycoprotein gM can interact with the cellular protein p32 and knockdown of p32 impairs virus
Harish Changotra1, Susan M Turk1, Antonio Artigues2
1Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, Shreveport, LA, USA.
Abstract:
The Epstein-Barr virus glycoprotein complex gMgN has been implicated in assembly and release of fully enveloped virus, although the precise role that it plays has not been elucidated. We report here that the long predicted cytoplasmic tail of gM is not required for complex formation and that it interacts with the cellular protein p32, which has been reported to be involved in nuclear egress of human cytomegalovirus and herpes simplex virus. Although redistribution of p32 and colocalization with gM was not observed in virus infected cells, knockdown of p32 expression by siRNA or lentivirus-delivered shRNA recapitulated the phenotype of a virus lacking expression of gNgM. A proportion of virus released from cells sedimented with characteristics of virus lacking an intact envelope and there was an increase in virus trapped in nuclear condensed chromatin. The observations suggest the possibility that p32 may also be involved in nuclear egress of Epstein-Barr virus.
Insights
The Epstein-Barr virus (EBV) gMgN glycoprotein complex
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- The Epstein-Barr virus (EBV) glycoprotein complex gMgN is crucial for enveloped virus assembly and release.
- Its precise function and interactions within the viral lifecycle remain largely uncharacterized.
Purpose of the Study:
- To investigate the role of the Epstein-Barr virus (EBV) gMgN glycoprotein complex in viral assembly and release.
- To identify cellular proteins interacting with the gMgN complex and elucidate their function in EBV pathogenesis.
Main Methods:
- Analysis of the cytoplasmic tail of EBV gM for complex formation.
- Investigating the interaction between gM and cellular protein p32 using siRNA and shRNA knockdown.
- Phenotypic analysis of virus release and nuclear localization in knockdown cells.
Main Results:
- The cytoplasmic tail of EBV gM is not essential for gMgN complex formation.
- EBV gM interacts with cellular protein p32, known to be involved in nuclear egress of other herpesviruses.
- Knockdown of p32 mimics the phenotype of gMgN-deficient EBV, leading to aberrant virus release and nuclear retention.
Conclusions:
- The cellular protein p32 plays a significant role in the assembly and release of Epstein-Barr virus (EBV).
- p32 may be involved in the nuclear egress of EBV, similar to its role in human cytomegalovirus and herpes simplex virus.
- These findings provide new insights into the molecular mechanisms of EBV replication and suggest p32 as a potential therapeutic target.
