Baculovirus infection induces disruption of the nuclear lamina

Zhang, Xiaomei; Xu, Kaiyan; Wei, Denghui; Wu, Wenbi; Yang, Kai; Yuan, Meijin

doi:10.1038/s41598-017-08437-5

Cited by 21 publications

(13 citation statements)

References 65 publications

(94 reference statements)

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“…Insights into the cellular architecture of suspension‐adapted cells, including the organization of genomic DNA, were clearly visualized. A singular nucleus morphology was observed in insect cells in the form of grained‐like structures (Figure 2b,c), likely due to nuclear envelope fragmentation during baculovirus infection, as reported elsewhere (Zhang et al, 2017). Interestingly, VLPs were detected in filopodia from the outer part of the cell membrane in the three systems (white arrow, Figure 2a–c).…”

Section: Resultssupporting

confidence: 80%

Quantification of the HIV‐1 virus‐like particle production process by super‐resolution imaging: From VLP budding to nanoparticle analysis

Puente‐Massaguer

Cervera

Gòdia

2020

Biotech & Bioengineering

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Virus‐like particles (VLPs) offer great promise in the field of nanomedicine. Enveloped VLPs are a class of these nanoparticles and their production process occurs by a budding process, which is known to be the most critical step at intracellular level. In this study, we developed a novel imaging method based on super‐resolution fluorescence microscopy (SRFM) to assess the generation of VLPs in living cells. This methodology was applied to study the production of Gag VLPs in three animal cell platforms of reference: HEK 293‐transient gene expression (TGE), High Five‐baculovirus expression vector system (BEVS) and Sf9‐BEVS. Quantification of the number of VLP assembly sites per cell ranged from 500 to 3,000 in the different systems evaluated. Although the BEVS was superior in terms of Gag polyprotein expression, the HEK 293‐TGE platform was more efficient regarding the assembly of Gag as VLPs. This was translated into higher levels of non‐assembled Gag monomer in BEVS harvested supernatants. Furthermore, the presence of contaminating nanoparticles was evidenced in all three systems, specifically in High Five cells. The SRFM‐based method here developed was also successfully applied to measure the concentration of VLPs in crude supernatants. The lipid membrane of VLPs and the presence of nucleic acids alongside these nanoparticles could also be detected using common staining procedures. Overall, a complete picture of the VLP production process was achieved in these three production platforms. The robustness and sensitivity of this new approach broaden the applicability of SRFM toward the development of new detection, diagnosis and quantification methods based on confocal microscopy in living systems.

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Section: Resultssupporting

confidence: 80%

Quantification of the HIV‐1 virus‐like particle production process by super‐resolution imaging: From VLP budding to nanoparticle analysis

Puente‐Massaguer

Cervera

Gòdia

2020

Biotech & Bioengineering

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“…The budding may consist of a series of steps. First, the nuclear lamina underlying the nucleoplasmic face of the INM needs to be disrupted, because the nucleocapsids are too large to pass through the crossover spacing of the nuclear lamina (5,51), while the formation of the intranuclear microvesicles requires a more fluid nuclear membrane (6,11). Second, membrane curvature will be generated at the budding sites (52), despite the inverse directions of budding in these two process.…”

Section: Discussionmentioning

confidence: 99%

Autographa californica Multiple Nucleopolyhedrovirus ac75 Is Required for the Nuclear Egress of Nucleocapsids and Intranuclear Microvesicle Formation

Shi

Zuo

et al. 2018

J Virol

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Autographa californica multiple nucleopolyhedrovirus (AcMNPV) () is a highly conserved gene of unknown function. In this study, we constructed an knockout AcMNPV bacmid and investigated the role of in the baculovirus life cycle. The expression and distribution of the Ac75 protein were characterized, and its interaction with another viral protein was analyzed to further understand its function. Our data indicated that was required for the nuclear egress of nucleocapsids, intranuclear microvesicle formation, and subsequent budded virion (BV) formation, as well as occlusion-derived virion (ODV) envelopment and embedding of ODVs into polyhedra. Western blot analyses showed that two forms, of 18 and 15 kDa, of FLAG-tagged Ac75 protein were detected. Ac75 was associated with both nucleocapsid and envelope fractions of BVs but with only the nucleocapsid fraction of ODVs; the 18-kDa form was associated with only BVs, whereas the 15-kDa form was associated with both types of virion. Ac75 was localized predominantly in the intranuclear ring zone during infection and exhibited a nuclear rim distribution during the early phase of infection. A phase separation assay suggested that Ac75 was not an integral membrane protein. A coimmunoprecipitation assay revealed an interaction between Ac75 and the integral membrane protein Ac76, and bimolecular fluorescence complementation assays identified the sites of the interaction within the cytoplasm and at the nuclear membrane and ring zone in AcMNPV-infected cells. Our results have identified as a second gene that is required for both the nuclear egress of nucleocapsids and the formation of intranuclear microvesicles. During the baculovirus life cycle, the morphogenesis of both budded virions (BVs) and occlusion-derived virions (ODVs) is proposed to involve a budding process at the nuclear membrane, which occurs while nucleocapsids egress from the nucleus or when intranuclear microvesicles are produced. However, the exact mechanism of virion morphogenesis remains unknown. In this study, we identified as a second gene, in addition to, that is essential for the nuclear egress of nucleocapsids, intranuclear microvesicle formation, and subsequent BV formation, as well as ODV envelopment and embedding of ODVs into polyhedra. Ac75 is not an integral membrane protein. However, it interacts with an integral membrane protein (Ac76) and is associated with the nuclear membrane. These data enhance our understanding of the commonalities between nuclear egress of nucleocapsids and intranuclear microvesicle formation and may help to reveal insights into the mechanism of baculovirus virion morphogenesis.

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“…As some DNA viral infections can disrupt nuclear lamina, it would be interesting to study whether the viruses can induce cellular senescence because cell cycle arrest during cellular senescence is beneficial for viral replication (Cano‐Monreal, Wylie, Cao, Tavis, & Morrison, ; C.‐P. Lee et al, ; Sharma, Kamil, Coughlin, Reim, & Coen, ; W. Wei et al, ; X. Zhang et al, ).…”

Section: Cellular Machinery Changes During Cellular Senescencementioning

confidence: 99%

Cellular senescence: Molecular mechanisms and pathogenicity

Wei

2018

Journal Cellular Physiology

153

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Cellular senescence is the arrest of normal cell division. Oncogenic genes and oxidative stress, which cause genomic DNA damage and generation of reactive oxygen species, lead to cellular senescence. The senescence-associated secretory phenotype is a distinct feature of senescence. Senescence is normally involved in the embryonic development. Senescent cells can communicate with immune cells to invoke an immune response. Senescence emerges during the aging process in several tissues and organs. In fact, increasing evidence shows that cellular senescence is implicated in aging-related diseases, such as nonalcoholic fatty liver disease, obesity and diabetes, pulmonary hypertension, and tumorigenesis. Cellular senescence can also be induced by microbial infection. During cellular senescence, several signaling pathways, including those of p53, nuclear factor-κB (NF-κB), mammalian target of rapamycin, and transforming growth factor-beta, play important roles. Accumulation of senescent cells can trigger chronic inflammation, which may contribute to the pathological changes in the elderly. Given the variety of deleterious effects caused by cellular senescence in humans, strategies have been proposed to control senescence. In this review, we will focus on recent studies to provide a brief introduction to cellular senescence, including associated signaling pathways and pathology.

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Baculovirus infection induces disruption of the nuclear lamina

Cited by 21 publications

References 65 publications

Quantification of the HIV‐1 virus‐like particle production process by super‐resolution imaging: From VLP budding to nanoparticle analysis

Quantification of the HIV‐1 virus‐like particle production process by super‐resolution imaging: From VLP budding to nanoparticle analysis

Autographa californica Multiple Nucleopolyhedrovirus ac75 Is Required for the Nuclear Egress of Nucleocapsids and Intranuclear Microvesicle Formation

Cellular senescence: Molecular mechanisms and pathogenicity

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