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Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein.

Wang L, Liu L, Che Y, Wang L, Jiang L, Dong C, Zhang Y, Li Q - Virol. J. (2010)

Bottom Line: In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro.The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication.Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute Of Medical Biology, Chinese Academy of Medicine Science, Peking Union Medical College, Kunming 650118, P. R. China.

ABSTRACT
HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro. The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication. Additionally, analysis of a recombinant virus HSV-1-UG showed that mutating VP26 resulted in a decreased viral replication rate and in aggregation of viral mutant capsids in the nucleus. Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.

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Morphological analysis on HSV-1 capsids aggregating in the cell with CTMP-7 expression inhibited (X30, 000). KMB-17 cells transfected with pGE-1 or pGE-CTMP plasmid were infected at an MOI of 1 with HSV-1 and incubated at 37°C. At 48 hour post-infection, samples of cell were harvested, and the enveloping process of viral capsids was observed by electron microscopy. a. HSV-1 capsids were observed aggregating in the area closing to nuclear membrane (NM) of cells transfected by pGE-CTMP. b. HSV-1 capsids were localized separately in nuclear and cytoplasma of cells transfected by pGE-1 mock plasmid. c. HSV-1 capsids were counted in difference EM fields. n = 3 for all fields. Error bars represent the standard error of the mean.
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Figure 6: Morphological analysis on HSV-1 capsids aggregating in the cell with CTMP-7 expression inhibited (X30, 000). KMB-17 cells transfected with pGE-1 or pGE-CTMP plasmid were infected at an MOI of 1 with HSV-1 and incubated at 37°C. At 48 hour post-infection, samples of cell were harvested, and the enveloping process of viral capsids was observed by electron microscopy. a. HSV-1 capsids were observed aggregating in the area closing to nuclear membrane (NM) of cells transfected by pGE-CTMP. b. HSV-1 capsids were localized separately in nuclear and cytoplasma of cells transfected by pGE-1 mock plasmid. c. HSV-1 capsids were counted in difference EM fields. n = 3 for all fields. Error bars represent the standard error of the mean.

Mentions: The previous experiments demonstrated that viral replication is similarly affected, i.e., reduced, in cells infected by HSV-1 viruses in the absence of either VP26 or CTMP-7. The detailed mechanism of how these proteins affect HSV-1 replication remains unclear, although the available evidence suggests that the absence of CTMP-7 affects the egress of viral particles. In attempt to determine the mechanism, a morphological analysis was performed using electron microscopy to observe the enveloping process of viral capsids. The HSV-1 capsids were observed aggregating in cells in which CTMP-7 expression was inhibited by RNAi (Fig.6a). However, in control cells the capsids were localized separately to the cytoplasma (Fig.6b). This observation suggests preliminarily that VP26 and CTMP-7 may contribute to the egress of viral particles by contributing to the process of enveloping of viral capsids.


Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein.

Wang L, Liu L, Che Y, Wang L, Jiang L, Dong C, Zhang Y, Li Q - Virol. J. (2010)

Morphological analysis on HSV-1 capsids aggregating in the cell with CTMP-7 expression inhibited (X30, 000). KMB-17 cells transfected with pGE-1 or pGE-CTMP plasmid were infected at an MOI of 1 with HSV-1 and incubated at 37°C. At 48 hour post-infection, samples of cell were harvested, and the enveloping process of viral capsids was observed by electron microscopy. a. HSV-1 capsids were observed aggregating in the area closing to nuclear membrane (NM) of cells transfected by pGE-CTMP. b. HSV-1 capsids were localized separately in nuclear and cytoplasma of cells transfected by pGE-1 mock plasmid. c. HSV-1 capsids were counted in difference EM fields. n = 3 for all fields. Error bars represent the standard error of the mean.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2913958&req=5

Figure 6: Morphological analysis on HSV-1 capsids aggregating in the cell with CTMP-7 expression inhibited (X30, 000). KMB-17 cells transfected with pGE-1 or pGE-CTMP plasmid were infected at an MOI of 1 with HSV-1 and incubated at 37°C. At 48 hour post-infection, samples of cell were harvested, and the enveloping process of viral capsids was observed by electron microscopy. a. HSV-1 capsids were observed aggregating in the area closing to nuclear membrane (NM) of cells transfected by pGE-CTMP. b. HSV-1 capsids were localized separately in nuclear and cytoplasma of cells transfected by pGE-1 mock plasmid. c. HSV-1 capsids were counted in difference EM fields. n = 3 for all fields. Error bars represent the standard error of the mean.
Mentions: The previous experiments demonstrated that viral replication is similarly affected, i.e., reduced, in cells infected by HSV-1 viruses in the absence of either VP26 or CTMP-7. The detailed mechanism of how these proteins affect HSV-1 replication remains unclear, although the available evidence suggests that the absence of CTMP-7 affects the egress of viral particles. In attempt to determine the mechanism, a morphological analysis was performed using electron microscopy to observe the enveloping process of viral capsids. The HSV-1 capsids were observed aggregating in cells in which CTMP-7 expression was inhibited by RNAi (Fig.6a). However, in control cells the capsids were localized separately to the cytoplasma (Fig.6b). This observation suggests preliminarily that VP26 and CTMP-7 may contribute to the egress of viral particles by contributing to the process of enveloping of viral capsids.

Bottom Line: In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro.The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication.Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute Of Medical Biology, Chinese Academy of Medicine Science, Peking Union Medical College, Kunming 650118, P. R. China.

ABSTRACT
HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study, a member of the tetraspanin superfamily, CTMP-7, was shown to physically interact with HSV-1 protein VP26, and the VP26-CTMP-7 complex was detected both in vivo and in vitro. The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication. Additionally, analysis of a recombinant virus HSV-1-UG showed that mutating VP26 resulted in a decreased viral replication rate and in aggregation of viral mutant capsids in the nucleus. Together, our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process.

Show MeSH
Related in: MedlinePlus