Rab8, a Vesicular Traffic Regulator, Is Involved in Dengue Virus Infection in HepG2 Cells

Xu, Xiao-Feng; Chen, Zongtao; Zhang, Junlei; Chen, Wei; Wang, Jiali; Tian, Yanping; Gao, Na; An, Jing

doi:10.1159/000151531

Cited by 12 publications

(15 citation statements)

References 33 publications

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“…The endogenous Rab8 antigen predominantly localized, similar to previous findings, in the cytoplasm from the perinuclear region to the plasma membrane in HepG2 cells ( fig. 5 a) [3,11,12] , and our mouse anti-Myo5c pAb specifically discriminated against Myo5c antigen in HepG2 cells ( fig. 5 b).…”

Section: The Decrease Of Viral Release Is Probably Associated With Thmentioning

confidence: 80%

“…The location of the DV2 antigen was in the cytoplasm, which is similar to our previous observation ( fig. 1 e) [3] . Although DV2 infection induced this disintegration, the colocalization of Myo5c with DV2 antigens was rarely observed ( fig.…”

Section: The Distribution Of Myo5c Is Disrupted By Dv2 Infectionmentioning

confidence: 99%

“…Rabbit anti-DV2 polyclonal antibody (pAb) had been prepared in our lab and used in our previous work [3] . To obtain rabbit antiRab8 pAb, a protein containing 6 !…”

Section: Antibodiesmentioning

confidence: 99%

“…Myosin Vc Is Involved in the Release of DV2 Intervirology 2009;52:258-265 259 infection [2,3] . As actin-mediated movements of Rab8-positive vesicles are largely dependent on Rab8 activity, Rab8 is ideal in regulating specific recruitment of motor proteins to defined vesicles [4] .…”

Section: Introductionmentioning

confidence: 99%

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Myosin Vc, a Member of the Actin Motor Family Associated with Rab8, Is Involved in the Release of DV2 from HepG2 Cells

Chen

Gao

et al. 2009

Intervirology

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Objective: The pathogenesis of the dengue virus (DV) infection has not been well defined. We have reported that actin and Rab8 are involved in DV2 infection. Myosin Vc (Myo5c) is a novel member of the class V myosins and regulates the actin-mediated membrane trafficking associated with Rab8. In this study, the involvement of Myo5c in the release of DV2 was investigated in HpeG2 cells. Methods: Distributions of actin, Myo5c, DV2 and Rab8 were revealed by fluorescent staining. HepG2^Myo5c-tail cells expressing a dominant-negative mutant of Myo5c were constructed by transfection and were assessed by Western blotting. The viral titers were detected by plaque assay, and the expression of Rab8 was analyzed by flow cytometry. Results: DV2 infection altered the distribution pattern of Myo5c, which might be associated with the depolymerization of actin, though colocalization rates of Myo5c with DV2 or actin were low. Furthermore, the release of DV2, but not the intracellular viral production, was reduced from HepG2^Myo5c-tail cells. Moreover, Myo5c colocalized with Rab8 and an increase of Rab8 was associated with the decrease of the viral release caused by the Myo5c tail.Conclusions: Our data suggest that Myo5c associated with Rab8 is involved in the release of DV2 from HepG2 cells.

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Section: The Decrease Of Viral Release Is Probably Associated With Thmentioning

confidence: 80%

Section: The Distribution Of Myo5c Is Disrupted By Dv2 Infectionmentioning

confidence: 99%

“…Rabbit anti-DV2 polyclonal antibody (pAb) had been prepared in our lab and used in our previous work [3] . To obtain rabbit antiRab8 pAb, a protein containing 6 !…”

Section: Antibodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Myosin Vc, a Member of the Actin Motor Family Associated with Rab8, Is Involved in the Release of DV2 from HepG2 Cells

Chen

Gao

et al. 2009

Intervirology

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“…Dengue virus and Hantavirus exploit Rab8-related regulatory mechanisms for viral particle release (35)(36)(37). These viral particles, including WNV, assemble and bud into intracellular organelles, such as the ER or Golgi apparatus, and are transported by vesicular trafficking to the plasma membrane (10,37).…”

Section: Discussionmentioning

confidence: 99%

Rab8b Regulates Transport of West Nile Virus Particles from Recycling Endosomes

Kobayashi

Suzuki

Kawaguchi

et al. 2016

Journal of Biological Chemistry

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West Nile virus (WNV) particles assemble at and bud into the endoplasmic reticulum (ER) and are secreted from infected cells through the secretory pathway. However, the host factor related to these steps is not fully understood. Rab proteins, belonging to the Ras superfamily, play essential roles in regulating many aspects of vesicular trafficking. In this study, we sought to determine which Rab proteins are involved in intracellular trafficking of nascent WNV particles. RNAi analysis revealed that Rab8b plays a role in WNV particle release. We found that Rab8 and WNV antigen were colocalized in WNV-infected human neuroblastoma cells, and that WNV infection enhanced Rab8 expression in the cells. In addition, the amount of WNV particles in the supernatant of Rab8b-deficient cells was significantly decreased compared with that of wild-type cells. We also demonstrated that WNV particles accumulated in the recycling endosomes in WNV-infected cells. In summary, these results suggest that Rab8b is involved in trafficking of WNV particles from recycling endosomes to the plasma membrane.

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Rab27a facilitates human parainfluenza virus type 2 growth by promoting cell surface transport of envelope proteins

Ohta

Matsumoto

Nishio

2018

Med Microbiol Immunol

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Human parainfluenza virus type 2 (hPIV-2) proteins and genomes newly synthesized in the cytoplasm need to be transported to the plasma membrane where budding occurs. This mechanism, where Rab proteins regulate intracellular traffic by switching between GTP-bound active form and GDP-bound inactive form, is not fully understood. mRNA and protein expression levels of Rab8a, Rab11a, and Rab27a are not altered by hPIV-2 infection. hPIV-2 growth is affected by depletion of Rab27a but not Rab8a and Rab11a. Overexpression of a constitutively active mutant of Rab27a Q78L promotes the cell surface levels of fusion (F) and hemagglutinin-neuraminidase (HN) proteins in hPIV-2-infected cells without affecting viral mRNA levels. Increase in the cell surface level of F and HN proteins by Rab27a Q78L is noticeable when these proteins are coexpressed independent of hPIV-2 infection. Our results collectively suggest that the active form of Rab27a enhances hPIV-2 growth by promoting transport of F and HN proteins to the plasma membrane.

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Rab8, a Vesicular Traffic Regulator, Is Involved in Dengue Virus Infection in HepG2 Cells

Cited by 12 publications

References 33 publications

Myosin Vc, a Member of the Actin Motor Family Associated with Rab8, Is Involved in the Release of DV2 from HepG2 Cells

Myosin Vc, a Member of the Actin Motor Family Associated with Rab8, Is Involved in the Release of DV2 from HepG2 Cells

Rab8b Regulates Transport of West Nile Virus Particles from Recycling Endosomes

Rab27a facilitates human parainfluenza virus type 2 growth by promoting cell surface transport of envelope proteins

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