Improved Adenovirus Type 5 Vector-Mediated Transduction of Resistant Cells by Piggybacking on Coxsackie B-Adenovirus Receptor-Pseudotyped Baculovirus

Granio, Ophélia; Porcherot, Marine; Corjon, Stéphanie; Kitidee, Kuntida; Henning, Petra; Eljaafari, Assia; Cimarelli, Andrea; Lindholm, Leif; Miossec, Pierre; Boulanger, Pierre; Hong, Saw-See

doi:10.1128/jvi.00012-09

Cited by 15 publications

(34 citation statements)

References 85 publications

(137 reference statements)

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“…VLP specimens were processed and observed under EM as previously described [17]. In brief, VLPs were diluted in 20 μL 0.14 M NaCl, 0.05 M Tris–HCl buffer, pH 8.2 (Tris-buffered saline; TBS) and adsorbed onto carbon-coated formvar membrane on grids.…”

Section: Methodsmentioning

confidence: 99%

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A novel platform for virus-like particle-display of flaviviral envelope domain III: induction of Dengue and West Nile virus neutralizing antibodies

Chua

Vituret

Tan

et al. 2013

Virol J

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CD16-RIgE is a chimeric human membrane glycoprotein consisting of the CD16 ectodomain fused to the transmembrane domain and cytoplasmic tail of the gamma chain of the high affinity receptor of IgE (RIgE). Coexpression of CD16-RIgE and HIV-1 Pr55Gag polyprotein precursor (Pr55GagHIV) in insect cells resulted in the incorporation of CD16-RIgE glycoprotein into the envelope of extracellular virus-like particles (VLPs), a phenomenon known as pseudotyping. Taking advantage of this property, we replaced the CD16 ectodomain of CD16-RIgE by the envelope glycoprotein domain III (DIII) of dengue virus serotype 1 (DENV1) or West Nile virus Kunjin (WNVKun). The two resulting chimeric proteins, DIII-DENV1-RIgE and DIII-WNVKun-RIgE, were addressed to the plasma membrane, exposed at the surface of human and insect cells, and incorporated into extracellular VLPs when coexpressed with Pr55GagHIV in insect cells. The DIII domains were accessible at the surface of retroviral VLPs, as shown by their reactivity with specific antibodies, and notably antibodies from patient sera. The DIII-RIgE proteins were found to be incorporated in VLPs made of SIV, MLV, or chimeric MLV-HIV Gag precursors, indicating that DIII-RIgE could pseudotype a wide variety of retroviral VLPs. VLP-displayed DIII were capable of inducing specific neutralizing antibodies against DENV and WNV in mice. Although the neutralization response was modest, our data confirmed the capability of DIII to induce a flavivirus neutralization response, and suggested that our VLP-displayed CD16-RIgE-based platform could be developed as a vaccine vector against different flaviviruses and other viral pathogens.

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Section: Methodsmentioning

confidence: 99%

“…Substitution of the viral envelope gene by another type of envelope glycoprotein is a phenomenon which is referred to as pseudotyping. Pseudotyping has been described for various enveloped viruses, including retroviruses, lentiviruses, vesicular stomatitis virus (VSV), HCV and baculoviruses [17-22]. …”

Section: Introductionmentioning

confidence: 99%

A novel platform for virus-like particle-display of flaviviral envelope domain III: induction of Dengue and West Nile virus neutralizing antibodies

Chua

Vituret

Tan

et al. 2013

Virol J

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“…The titer in physical particles (viral particles; vp) was determined by absorbance measurement at 260 nm ( A 260 ) of 1-ml samples of SDS-denatured virions (0.1% SDS for 1 min at 56°C) in a 1-cm-path-length cuvette, using the respective formula: A 260 of 1.0 = 1.1×10 12 vp/ml for HAdV5 (genomic DNA = 36 kbp). HAdV5 particle titers ranged from 5×10 11 to 1×10 12 vp/ml, with infectious titers between 2×10 10 and 5×10 10 PFU/ml [95].…”

Section: Methodsmentioning

confidence: 99%

Cell Entry and Trafficking of Human Adenovirus Bound to Blood Factor X Is Determined by the Fiber Serotype and Not Hexon:Heparan Sulfate Interaction

et al. 2011

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Human adenovirus serotype 5 (HAdV5)-based vectors administered intravenously accumulate in the liver as the result of their direct binding to blood coagulation factor X (FX) and subsequent interaction of the FX-HAdV5 complex with heparan sulfate proteoglycan (HSPG) at the surface of liver cells. Intriguingly, the serotype 35 fiber-pseudotyped vector HAdV5F35 has liver transduction efficiencies 4-logs lower than HAdV5, even though both vectors carry the same hexon capsomeres. In order to reconcile this apparent paradox, we investigated the possible role of other viral capsid proteins on the FX/HSPG-mediated cellular uptake of HAdV5-based vectors. Using CAR- and CD46-negative CHO cells varying in HSPG expression, we confirmed that FX bound to serotype 5 hexon protein and to HAdV5 and HAdV5F35 virions via its Gla-domain, and enhanced the binding of both vectors to surface-immobilized hypersulfated heparin and cellular HSPG. Using penton mutants, we found that the positive effect of FX on HAdV5 binding to HSPG and cell transduction did not depend on the penton base RGD and fiber shaft KKTK motifs. However, we found that FX had no enhancing effect on the HAdV5F35-mediated cell transduction, but a negative effect which did not involve the cell attachment or endocytic step, but the intracellular trafficking and nuclear import of the FX-HAdV5F35 complex. By cellular imaging, HAdV5F35 particles were observed to accumulate in the late endosomal compartment, and were released in significant amounts into the extracellular medium via exocytosis. We showed that the stability of serotype 5 hexon∶FX interaction was higher at low pH compared to neutral pH, which could account for the retention of FX-HAdV5F35 complexes in the late endosomes. Our results suggested that, despite the high affinity interaction of hexon capsomeres to FX and cell surface HSPG, the adenoviral fiber acted as the dominant determinant of the internalization and trafficking pathway of HAdV5-based vectors.

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“…HAdV5-GFP and HAdV5F35-GFP vectors have been described in previous studies [36], [55], [64]. The capsid of HAdV5F35-GFP consisted of hexon and penton base capsomers of HAdV5, and of chimeric fibers made up of the shaft and knob domains of serotype 35 fiber (F35) fused to HAdV5 fiber tail.…”

Section: Methodsmentioning

confidence: 99%

“…The titer in physical virus particles of AcMPV-VSV-G vector was determined by adsorbance measurement at 260 nm ( A 260 ) on 1-mL samples of SDS-denatured virions (0.1% SDS for 1 min at 56°C) in 1-cm pathlength cuvette, using the following formula : A 260 of 1.0 = 0.3×10 12 vp/mL, considering the length of 134 kbp for the viral genomic DNA. Infectious titers of stocks of AcMPV-VSV-G concentrated by ultracentrifugation were usually 5×10 9 to 1×10 10 pfu/mL, and the corresponding physical particle titers ranged between 1×10 12 and 5×10 12 vp/mL [36].…”

Section: Methodsmentioning

confidence: 99%

Microparticle-Mediated Transfer of the Viral Receptors CAR and CD46, and the CFTR Channel in a CHO Cell Model Confers New Functions to Target Cells

et al. 2012

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Cell microparticles (MPs) released in the extracellular milieu can embark plasma membrane and intracellular components which are specific of their cellular origin, and transfer them to target cells. The MP-mediated, cell-to-cell transfer of three human membrane glycoproteins of different degrees of complexity was investigated in the present study, using a CHO cell model system. We first tested the delivery of CAR and CD46, two monospanins which act as adenovirus receptors, to target CHO cells. CHO cells lack CAR and CD46, high affinity receptors for human adenovirus serotype 5 (HAdV5), and serotype 35 (HAdV35), respectively. We found that MPs derived from CHO cells (MP-donor cells) constitutively expressing CAR (MP-CAR) or CD46 (MP-CD46) were able to transfer CAR and CD46 to target CHO cells, and conferred selective permissiveness to HAdV5 and HAdV35. In addition, target CHO cells incubated with MP-CD46 acquired the CD46-associated function in complement regulation. We also explored the MP-mediated delivery of a dodecaspanin membrane glycoprotein, the CFTR to target CHO cells. CFTR functions as a chloride channel in human cells and is implicated in the genetic disease cystic fibrosis. Target CHO cells incubated with MPs produced by CHO cells constitutively expressing GFP-tagged CFTR (MP-GFP-CFTR) were found to gain a new cellular function, the chloride channel activity associated to CFTR. Time-course analysis of the appearance of GFP-CFTR in target cells suggested that MPs could achieve the delivery of CFTR to target cells via two mechanisms: the transfer of mature, membrane-inserted CFTR glycoprotein, and the transfer of CFTR-encoding mRNA. These results confirmed that cell-derived MPs represent a new class of promising therapeutic vehicles for the delivery of bioactive macromolecules, proteins or mRNAs, the latter exerting the desired therapeutic effect in target cells via de novo synthesis of their encoded proteins.

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Improved Adenovirus Type 5 Vector-Mediated Transduction of Resistant Cells by Piggybacking on Coxsackie B-Adenovirus Receptor-Pseudotyped Baculovirus

Cited by 15 publications

References 85 publications

A novel platform for virus-like particle-display of flaviviral envelope domain III: induction of Dengue and West Nile virus neutralizing antibodies

A novel platform for virus-like particle-display of flaviviral envelope domain III: induction of Dengue and West Nile virus neutralizing antibodies

Cell Entry and Trafficking of Human Adenovirus Bound to Blood Factor X Is Determined by the Fiber Serotype and Not Hexon:Heparan Sulfate Interaction

Microparticle-Mediated Transfer of the Viral Receptors CAR and CD46, and the CFTR Channel in a CHO Cell Model Confers New Functions to Target Cells

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