Transient expression of a bovine leukemia virus envelope glycoprotein in plants by a recombinant TBSV vector

Zhumabek, Aiganym T.; Abeuova, Laura S.; Mukhametzhanov, Nurzhan S.; Scholthof, Karen‐Beth G.; Ramankulov, Yerlan; Manabayeva, Shuga A.

doi:10.1016/j.jviromet.2018.01.016

Cited by 6 publications

(5 citation statements)

References 28 publications

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“…sBLV-EnvFm protein was also recognized by bovine sera as shown by WB, strengthening the ELISA results (using murine sera). A recombinant BLV gp51 expressed in TBSV showed similar reactivity using positive bovine sera when analysed by WB 63 . Thus, this recombinant protein expressed in S2 cells represents an excellent tool to detect specific anti-BLV antibodies.…”

Section: Discussionmentioning

confidence: 86%

Characterization and application of recombinant Bovine Leukemia Virus Env protein

Tomé-Poderti,

Olivero-Deibe,

Carrión

et al. 2024

Sci Rep

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The Bovine Leukemia Virus (BLV) Envelope (Env) glycoprotein complex is instrumental in viral infectivity and shapes the host’s immune response. This study presents the production and characterization of a soluble furin-mutated BLV Env ectodomain (sBLV-EnvFm) expressed in a stable S2 insect cell line. We purified a 63 kDa soluble protein, corresponding to the monomeric sBLV-EnvFm, which predominantly presented oligomannose and paucimannose N-glycans, with a high content of core fucose structures. Our results demonstrate that our recombinant protein can be recognized from specific antibodies in BLV infected cattle, suggesting its potential as a powerful diagnostic tool. Moreover, the robust humoral immune response it elicited in mice shows its potential contribution to the development of subunit-based vaccines against BLV.

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Section: Discussionmentioning

confidence: 86%

Characterization and application of recombinant Bovine Leukemia Virus Env protein

Tomé-Poderti,

Olivero-Deibe,

Carrión

et al. 2024

Sci Rep

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“…The rgp 51 coated in a microplate can specifically react with BLV-infected bovine serum samples. Overall, high sensitivity (95.8 %) and specificity (91.6 %) were observed when using the rgp 51 in ELISA for the detection of antibodies in bovine sera [53]. Recently, N. benthamiana produced a nucleocapsid protein of PRRSV that was used to detect the anti-PRRSV antibodies present in swine sera using Western blot [54].…”

Section: Pathogenmentioning

confidence: 99%

Molecular Farming Strategy for the Rapid Production of Protein-Based Reagents for Use in Infectious Disease Diagnostics

Shanmugaraj¹,

Jirarojwattana

Phoolcharoen

2023

Planta Med

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Recombinant proteins are a major breakthrough in biomedical research with a wide range of applications from diagnostics to therapeutics. Strategic construct design, consistent expression platforms, suitable upstream and downstream techniques are key considerations to produce commercially viable recombinant proteins. The recombinant antigenic protein production for use either as a diagnostic reagent or subunit vaccine formulations is usually carried out in prokaryotic or eukaryotic expression platforms. Microbial and mammalian systems dominate the biopharmaceutical industry for such applications. However, there is no universal expression system that can meet all the requirements for different types of proteins. The adoptability of any expression system is likely based on the quality and quantity of the proteins that can be produced from it. The huge demand of recombinant proteins for different applications requires an inexpensive production platform for rapid development. The molecular farming scientific community has been promoting the plant system for nearly three decades as a cost-effective alternative to produce high-quality proteins for research, diagnostic and therapeutic applications. Here, we discuss how plant biotechnology could offer solutions for the rapid and scalable production of protein antigens as low-cost diagnostic reagents for use in functional assays.

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“…Efficient procedures have been devised for the transient expression of recombinant proteins in N. benthamiana that often involve the vacuum infiltration of leaf tissue with agrobacteria harboring a DNA transgene for the protein of interest delivered by either a viral replicon or a binary vector system (Leuzinger et al., 2013; Norkunas et al., 2018). A variety of therapeutic and diagnostic proteins have been produced in agroinfiltrated N. benthamiana plants recently, including mammalian antibodies (Qiu et al., 2014; Jutras et al., 2016; Li et al., 2016; Lee et al., 2018; Marusic et al., 2018; Kommineni et al., 2019; Kopertekh et al., 2019), viral antigens (Jutras et al., 2015; Tusé et al., 2015; Regnard et al., 2017; Mbewana et al., 2018; Roychowdhury et al., 2018; Tottey et al., 2018; Vanmarsenille et al., 2018; Zhumabek et al., 2018; Laughlin et al., 2019), and other proteins of potential clinical value (Rattanapisit et al., 2017, 2019; Fu et al., 2018; Ramirez-Alanis et al., 2018; Silberstein et al., 2018).…”

Section: Introductionmentioning

confidence: 99%

Production of Biopharmaceuticals in Nicotiana benthamiana—Axillary Stem Growth as a Key Determinant of Total Protein Yield

et al. 2019

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Data are scarce about the influence of basic cultural conditions on growth patterns and overall performance of plants used as heterologous production hosts for protein pharmaceuticals. Higher plants are complex organisms with young, mature, and senescing organs that show distinct metabolic backgrounds and differ in their ability to sustain foreign protein expression and accumulation. Here, we used the transient protein expression host Nicotiana benthamiana as a model to map the accumulation profile of influenza virus hemagglutinin H1, a clinically promising vaccine antigen, at the whole plant scale. Greenhouse-grown plants submitted to different light regimes, submitted to apical bud pruning, or treated with the axillary growth-promoting cytokinin 6-benzylaminopurine were vacuum-infiltrated with agrobacteria harboring a DNA sequence for H1 and allowed to express the viral antigen for 7 days in growth chamber under similar environmental conditions. Our data highlight the importance of young leaves on H1 yield per plant, unlike older leaves which account for a significant part of the plant biomass but contribute little to total antigen titer. Our data also highlight the key contribution of axillary stem leaves, which contribute more than 50% of total yield under certain conditions despite representing only one-third of the total biomass. These findings underline the relevance of both considering main stem leaves and axillary stem leaves while modeling heterologous protein production in N. benthamiana. They also demonstrate the potential of exogenously applied growth-promoting hormones to modulate host plant architecture for improvement of protein yields.

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Transient expression of a bovine leukemia virus envelope glycoprotein in plants by a recombinant TBSV vector

Cited by 6 publications

References 28 publications

Characterization and application of recombinant Bovine Leukemia Virus Env protein

Characterization and application of recombinant Bovine Leukemia Virus Env protein

Molecular Farming Strategy for the Rapid Production of Protein-Based Reagents for Use in Infectious Disease Diagnostics

Production of Biopharmaceuticals in Nicotiana benthamiana—Axillary Stem Growth as a Key Determinant of Total Protein Yield

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