In addition to specificity and speed, recombinant technology offers advantages with respect to purity and product design. GATEWAY Demonstration Program Purpose: demonstrate new SSL products in real-world applications that save energy, match or improve illumination, and are cost effective. For example, expresSF+ cells have been used to produce recombinant proteins at scales ranging from two to 21000 L [44]. , Please enable it to take advantage of the complete set of features! Grimm, D. Role of N-linked glycans in the functions of hepatitis C virus envelope proteins incorporated into infectious virions. The BEVS platform, being based on recombinant technology, offers the flexibility and genetic control required for the design and manufacture of these universal vaccine candidates.
Protein Expression Systems - Sigma-Aldrich A second feature is the growing number of BEVSderived products that have been approved by regulatory agencies worldwide (Table (Table1).1). rAAVbased treatments for retinal degeneration, including macular degeneration and Leber's congenital amaurosis type 2, are another area of intense investigation [70, 71]. However, the main drawback of these conventional vaccines is the lack of differentiability of infected from vaccinated animals (DIVA concept . Liu L.J., Suzuki T., Tsunemitsu H., Kataoka M., Ngata N., Takeda N., Wakita T., Miyamura T., Li T.C. An extensive analysis on the global codon usage pattern of baculoviruses. 5D). The other non-enveloped VLP, multilayered VLP (Fig. Synthesis and immunogenicity of the rotavirus major capsid antigen using a baculovirus expression system. Kato T., Murata T., Usui T., Park E.Y. Roldao A., Mellado M.C., Castilho L.R., Carrondo M.J., Alves P.M. Virus-like particles in vaccine development. Analysis of AAV serotypes 19 mediated gene expression and tropism in mice after systemic injection. IX and X, the membrane proteins are transported through the Golgi apparatus onto the plasma membrane. Cecchini, S. Nine BEVSderived products have been licensed, providing regulators confidence with the platform. , Even though the probabilistic model could be used for a steady-state co-infection analysis for prediction of VLP composition, there were no models of the VLP assembly process until a kinetic and statistical-thermodynamic model was established for baculovirus infection and VLP assembly in suspended insect cells. Insect cells are then cotransfected with a mixture of the transfer plasmid and parental AcMNPV DNA that has been linearized such that the parental polyhedrin gene and portion of ORF1629 are missing, rendering it noninfectious [13]. official website and that any information you provide is encrypted Experience and an increased understanding of basic insect cell biology have shown that these early expectations were not completely realistic. Likewise, Sapp et al. Cassidy L.F., Lyles D.S., Abramson J.S. Mono- and dibasic proteolytic cleavage sites in insect neuroendocrine peptide precursors. As discussed by Cox (2012), vast global bioreactor capacity (500000 L) already exists and presents the opportunity to minimize the investment needed to establish BEVS manufacturing facilities [1]. A P3 virus (50 ml or 500 ml) is produced by infecting Sf9 cells with a P2 virus at a low multiplicity of infection (MOI=0.1). , MOI. . Spontaneous excision of BAC vector sequences from bacmidderived baculovirus expression vectors upon passage in insect cells. Free Online Library: Think like a Virus: Toward Improving Nanovaccine Development against SARS-CoV-2. Intracellular dynamics in rotavirus-like particles production: evaluation of multigene and monocistronic infection strategies. Huang, Y. Body weight greater than or equal to 10 kg. Levy, J. R. et al.. 5 : 3135990712390). et al.. Mena J.A., Kamen A.A. Insect cell technology is a versatile and robust vaccine manufacturing platform. , Chen, Y. J. Although the BES has been broadly adopted for the basic construction of VLPs in different laboratories, upstream and downstream processing issue should conform to industry or, at least, basic research standards. Production of CCHF virus-like particle by a baculovirus-insect cell expression system. The Baculovirus Expression Vector System (BEVS) is used to produce recombinant . The BEVS platform is an efficient process for producing a wide variety of proteins in a streamlined manner. By mutating these cysteine residues to nonthiol residues, it was possible to prevent crosslinking and enhance stability [21]. In this section we discuss opportunities in the areas of gene therapy and influenza vaccines spawned by the two most recent BEVSderived product approvals, Glybera (licensed by the EMA in 2012) and Flublok (licensed by the FDA in 2013), respectively. , ADDomer, as a kind of non-infectious adenovirus-inspired nanoparticle, has the advantage of high thermal stability. Recombinant baculovirus derived from all other commercially available baculovirus DNA preparations is produced with 80-90% efficiency and requires plaque purification to remove parental virus. High, K. H. Multiple coronavirus BEVSderived vaccine candidates have been developed that include recombinant spike protein either alone as a subunit vaccine or together with recombinant envelope and membrane proteins as VLPs and have demonstrated efficacy in animal models [29, 99, 100, 101, 102, 103, 104, 105, 106, 107]. Pringle F.M., Kalmakoff J., Ward V.K. Graham, I. Unlike some other production facilities, BEVS facilities can be multipurpose and used to produce a variety of BEVSderived products, especially when disposable or singleuse technology is employed [45].
Baculovirus-free insect cell expression system for high yield antibody Gao X., Wang W., Li Y., Zhang S., Duan Y., Xing L., Zhao Z., Zhang P., Li Z., Li R., Wang X., Yang P. Enhanced Influenza VLP vaccines comprising matrix-2 ectodomain and nucleoprotein epitopes protects mice from lethal challenge. The Poisson distribution can be used to describe the probability (P) of one insect cell initially infected by w recombinant baculoviruses, and it has the following form [52]: The Poisson distribution is graphically represented in the Fig. Zhou, P. Skowronski, D. M. Smith, G. E. Nonetheless, another comparison [147] of the two strategies for the production of rotavirus VLPs indicated that virus DNA replication and transcription rates were appropriately 50% slower in the co-expression than in the co-infection experiments, which was contrary to the results of [146]. Tepp, W. H. Belyaev A.S., Roy P. Development of baculovirus triple and quadruple expression vectors: co-expression of three or four bluetongue virus proteins and the synthesis of bluetongue virus-like particles in insect cells. Federal government websites often end in .gov or .mil. 4. You may switch to Article in classic view. Highlights Outstanding Capability for Complex Protein Advanced Expression Optimization Technology Capacity for Large Inserts > 400kDa General Workflow High expression levels driven by the strong polyhedrin promoter. doi: 10.1093/nar/gng102. Insect cells are grown in suspension, so if the cells and baculoviruses have been optimized for large scale and multiple passages, the culture size is only limited by the size of the bioreactor. The strong polh promoter probably overwhelms theprocessingcapacity of the endoplasmic reticulum (ER) in insect cells, and in contrast, the weaker p10 promoter allows production of a biologically active glycoprotein [60].
Baculovirus Recombinant Protein Expression Vector | VectorBuilder Marek M., van Oers M.M., Devaraj F.F., Vlak J.M., Merten O.W. Sokolenko S., George S., Wagner A., Tuladhar A., Andrich J.M., Aucoin M.G. , , We have passed a tipping point where BEVSderived products are becoming mainstream, and the BEVS platform is being actively utilized by major players in the biotechnology industry to develop new products. Feldmann, F. Caballero S., Guix S., Ribes E., Bosch A., Pinto R.M. Lukason, M. Classical swine fever (CSF), caused by CSF virus (CSFV), is one of the most devastating viral epizootic diseases of swine in many countries. Felberbaum, R. The plasmid and parental DNA undergo homologous recombination to generate de novo recombinant baculoviruses. Hui, D. S. Production of porcine parvovirus empty capsids with high immunogenic activity. I: 1,2-glucosidase I and 1,3-glucosidase II; II: -mannosidase. Modifications of cysteine residues in the transmembrane and cytoplasmic domains of a recombinant hemagglutinin protein prevents crosslinked multimer formation and potency loss.
System for Rapid Generation of Recombinant Baculovirus-based Expression The BacPAK System uses the baculovirus Autographa californica nuclear polyhedrosis virus (AcMNPV) to produce target proteins in insect cells. Influenza virus-like particles elicit broader immune responses than whole virion inactivated influenza virus or recombinant hemagglutinin. Isibasi, A. , DNA vaccine utilizes genetically engineered DNA capable of inducing humoral and Baculovirus as versatile vectors for protein expression in insect and mammalian cells. Recombinant baculovirus genome comprising: - one or more expression cassettes of the AAV rep and cap genes necessary for the production of an AAV vector, and - a recombinant genome of an AAV vector, said expression cassettes and said recombinant genome of an AAV vector being inserted into one or more loci chosen from the group consisting of the egt, polyhedrin, ctx, 39k, orf51, gp37, iap2 and . Chikungunya is an arbovirus, for which there are many opportunities to develop BEVSderived vaccines (reviewed in [39]). the display of certain parts of an article in other eReaders. Proper cleavage of signal peptides in baculovirus-infected cells is inferred from the size of the product or its presence in the plasma membrane or extracellular culture fluid. , Shuler, M. L. Kleinschmidt, J. Insect cell expression and purification of recombinant SARS-COV-2 spike proteins that demonstrate ACE2 binding. , BestBac 2.0 is a deletion mutant of BestBac 1.0. Structural requirements of astrovirus virus-like particles assembled in insect cells. Rittner, K. In this review, we explore the BEVS platform, detailing how it works, platform features and limitations and important considerations for manufacturing and regulatory approval. Baculovirus Expression System Adapted from [52] with permission from Elsevier (License No. com, China, for drawing the formula of Poisson distribution by an software. It is tailored annually to provide protection against the latest strains of influenza by containing the corresponding hemagglutinin (HA) antigens produced by the BES [18], [19].
(PDF) Accuracy in Diagnosis of Celiac Disease Without Biopsies in Jeoung H.Y., Lee W.H., Jeong W., Shin B.H., Choi H.W., Lee H.S., An D.J. Heck, S. Nevertheless, comparison of VLP production in terms of yield and quality between Sf9 and Tn5 lines revealed dramatic differences in baculovirus background as well as in yield and density of VLPs: the Tn5 cells produced homogenous VLPs carrying more HA than their Sf9-derived counterparts and resulted in a much lower virus background of the final VLP preparation [140]. ) when expressed in insect cells by co-expression or co-infection with recombinant baculoviruses. already built in. The results showed that the co-expression was more efficient for production of such VLPs than the co-infection, which could be attributed to three major factors: (1) higher DNA replication rates presented by the tricistronic vector than the monocistronic vectors, (2) invariant mRNA stability for all three mRNAs, and (3) an excess of VP7 over VP6, both of which were produced by the co-expression, being more approximately equivalent to the VP7/VP6 stoichiometric ratio in the native virons [146]. , The antigen is a fusion glycoprotein consisting of prostatic acid phosphatase (PAP) linked to granulocytemacrophage colonystimulating factor (GMCSF) and is used to stimulate autologous antigen presenting cells [33]. The BEVS platform has inherent safety measures built in that are attractive from a regulatory perspective. Summers, M. D. Kort, T. et al., Recombinant antigens based on toxins A and B of, {"type":"clinical-trial","attrs":{"text":"NCT02082860","term_id":"NCT02082860"}}, {"type":"clinical-trial","attrs":{"text":"NCT01054339","term_id":"NCT01054339"}}, {"type":"clinical-trial","attrs":{"text":"NCT00377416","term_id":"NCT00377416"}}, {"type":"clinical-trial","attrs":{"text":"NCT02168686","term_id":"NCT02168686"}}, {"type":"clinical-trial","attrs":{"text":"NCT00087789","term_id":"NCT00087789"}}, {"type":"clinical-trial","attrs":{"text":"NCT01395641","term_id":"NCT01395641"}}, {"type":"clinical-trial","attrs":{"text":"NCT01519349","term_id":"NCT01519349"}}, {"type":"clinical-trial","attrs":{"text":"NCT01461213","term_id":"NCT01461213"}}, {"type":"clinical-trial","attrs":{"text":"NCT02077361","term_id":"NCT02077361"}}, {"type":"clinical-trial","attrs":{"text":"NCT00534703","term_id":"NCT00534703"}}, {"type":"clinical-trial","attrs":{"text":"NCT01966887","term_id":"NCT01966887"}}, {"type":"clinical-trial","attrs":{"text":"NCT01643330","term_id":"NCT01643330"}}, {"type":"clinical-trial","attrs":{"text":"NCT00428935","term_id":"NCT00428935"}}, {"type":"clinical-trial","attrs":{"text":"NCT01637805","term_id":"NCT01637805"}}, {"type":"clinical-trial","attrs":{"text":"NCT01687608","term_id":"NCT01687608"}}, {"type":"clinical-trial","attrs":{"text":"NCT00979238","term_id":"NCT00979238"}}, {"type":"clinical-trial","attrs":{"text":"NCT00515710","term_id":"NCT00515710"}}, {"type":"clinical-trial","attrs":{"text":"NCT00482027","term_id":"NCT00482027"}}, {"type":"clinical-trial","attrs":{"text":"NCT01937455","term_id":"NCT01937455"}}, {"type":"clinical-trial","attrs":{"text":"NCT00126724","term_id":"NCT00126724"}}, {"type":"clinical-trial","attrs":{"text":"NCT01414985","term_id":"NCT01414985"}}, {"type":"clinical-trial","attrs":{"text":"NCT00151216","term_id":"NCT00151216"}}, {"type":"clinical-trial","attrs":{"text":"NCT00999609","term_id":"NCT00999609"}}, {"type":"clinical-trial","attrs":{"text":"NCT00749957","term_id":"NCT00749957"}}, {"type":"clinical-trial","attrs":{"text":"NCT00643747","term_id":"NCT00643747"}}, {"type":"clinical-trial","attrs":{"text":"NCT01496040","term_id":"NCT01496040"}}, {"type":"clinical-trial","attrs":{"text":"NCT00481546","term_id":"NCT00481546"}}, {"type":"clinical-trial","attrs":{"text":"NCT00821340","term_id":"NCT00821340"}}, {"type":"clinical-trial","attrs":{"text":"NCT02161380","term_id":"NCT02161380"}}, {"type":"clinical-trial","attrs":{"text":"NCT01344798","term_id":"NCT01344798"}}, {"type":"clinical-trial","attrs":{"text":"NCT00494195","term_id":"NCT00494195"}}, {"type":"clinical-trial","attrs":{"text":"NCT01024998","term_id":"NCT01024998"}}, {"type":"clinical-trial","attrs":{"text":"NCT00643890","term_id":"NCT00643890"}}, {"type":"clinical-trial","attrs":{"text":"NCT00400634","term_id":"NCT00400634"}}, {"type":"clinical-trial","attrs":{"text":"NCT00229736","term_id":"NCT00229736"}}, {"type":"clinical-trial","attrs":{"text":"NCT01973543","term_id":"NCT01973543"}}, {"type":"clinical-trial","attrs":{"text":"NCT01621581","term_id":"NCT01621581"}}, {"type":"clinical-trial","attrs":{"text":"NCT00976352","term_id":"NCT00976352"}}, {"type":"clinical-trial","attrs":{"text":"NCT02122952","term_id":"NCT02122952"}}, Express gene encoding Rabescort Protein 1 (REP1), Express the sarcoplasmic reticulum calcium ATPase (SERCA2a), Express gag, protease and part of the reverse transcriptase, AAV1gammasarcoglycan vector injection, Express Glial cell linederived neurotrophic factor (GDNF). other major organ systems such as the gastrointestinal tract (GI), hepatobiliary, cardiovascular, renal, and central nervous system. VI and VII, the HA and NA are transported through the Golgi apparatus onto the plasma membrane. Influenza neuraminidase as a vaccine antigen. , Karczewski, J. Molecular engineering of the, Vlak J.M., Klinkenberg F.A., Zaal K.J., Usmany M., Klinge-Roode E.C., Geervliet J.B., Roosien J., van Lent J.W. Disadvantages. Such a resulting change may be attributed to the alteration of the corresponding glycosyltransferase activities with variation of culture medium constituents [96]. Matthews, E. E. .
Vaccines | Free Full-Text | Nanoparticle-Based Delivery Systems for The v-cath/chiA deletion can improve the integrity of your expressed protein resulting in a significant increase of functional protein yield. Yeast expression system The MOI should be selected carefully in order to achieve optimal production of VLPs. , . Vaitsopoulou A, Depping P, Bill RM, Goddard AD, Rothnie AJ. doi: 10.1002/pro.4300. You may switch to Article in classic view. Small-Scale Production of Recombinant Proteins Using the Baculovirus Expression Vector System. Moreover, the President's Council of Advisors on Science and Technology (PCAST) reported that pandemic influenza vaccine in 2009 was not readily available until after the pandemic peaked, a major concern for public health and safety (www.whitehouse.gov/sites/default/files/microsites/ostp/PCASTInfluenzaVaccinologyReport.pdf). For fifty years influenza vaccine manufacturing technology remained largely stagnant. Superior expression of juvenile hormone esterase and beta-galactosidase from the basic protein promoter of. , The presence of nuclear polyhedrosis viruses of. requirements for purity and safety. , Fuxiao Liu, Xiaodong Wu, [], and Zhiliang Wang. Baxter R., Patriarca P.A., Ensor K., Izikson R., Goldenthal K.L., Cox M.M. Cox, M. M., Commercial production in insect cells. The opportunities to develop new products using BEVS are abundant, and we review the latest developments in the gene therapy and influenza vaccine fields as examples. Baculovirus-meditated expression systems possess a number of advantages: 1. El Sahly, H. People are exposed to baculoviruses daily by consuming fresh vegetables. , One example of this application is the antigen used in Provenge immunotherapy. Baculovirus-mediated expression in insect cells has become well-established for the production of recombinant glycoproteins. , Liquefaction of, Slack J.M., Kuzio J., Faulkner P. Characterization of v-cath, a cathepsin L-like proteinase expressed by the baculovirus. ,
Is An Insect Expression System the Right Choice For Your Protein? Collins, M. Like parental viruses, many VLPs generated by the BES are enveloped, meaning that the capsids are coated with a lipid membrane known as the envelope, which is derived from the plasma membrane of insect cells. 2) that are morphologically and antigenically similar to native viruses [21], [34], [47], [48]. et al.. Viruslike particles of SARSlike coronavirus formed by membrane proteins from different origins demonstrate stimulating activity in human dendritic cells. Methods Mol Biol. Feng, Q. A gene of interest (GOI) is cloned into a transfer plasmid behind a strong promoter (green arrow) and surrounded by DNA homologous. Hashimoto, Y.
(PDF) Toxoplasmosis y neosporosis en rumiantes domsticos Takeda, N. Science Recombinant baculoviruses are widely used to express heterologous genes in cultured insect cells and insect larvae. Recent Pat Biotechnol. Therefore, it would be possible to infer an improvement in complex glycosylation of foreign proteins required for the generation of VLPs, if the p10 promoter was used instead of the polh promoter. BEVS can be used to develop a wide variety of products and is especially well suited for combating rapidly emerging and dangerous pathogens. Despite the establishments of mathematical models for baculovirus infection for a long time, the total number of reports on application of models to optimize the production of VLPs is relatively scarce over the past decade. However, some essential properties of the BES, such as unspecific proteolysis, on the contrary, impede the production of VLPs. Fortunately, baculovirus multiple gene transfer vectors pAcAB3 and pAcAB4 have been commercialized to facilitate the insertion of three or four foreign genes respectively into one AcMNPV genome by a single co-transfection experiment [23]. Comparisons of the BEVS platform to other expression systems such as bacteria, yeast, mammalian cells and plants have been made and are useful to consider when selecting a platform [2, 3, 4]. It is widely believed that synonymous codon usage of highly expressed genes is strongly biased and tends to match the more abundant tRNAs. Improving adenoassociated vector yield in high density insect cell cultures. Helle F., Vieyres G., Elkrief L., Popescu C.I., Wychowski C., Descamps V., Castelain S., Roingeard P., Duverlie G., Dubuisson J. Sapp M., Volpers C., Muller M., Streeck R.E. Yeasts such as S. cerevisiae can also produce high yields of protein at low cost and are capable of some posttranslational modifications [4]. Bai, B. Though yields can be up to 500 mg/L, recombinant baculovirus production can be time consuming and culture conditions more challenging than prokaryotic systems. It can take years of work to adequately ensure purity and safety in addition to high productivity. I: 1,2-glucosidase I and 1,3-glucosidase II; II: -mannosidase I (in rough endoplasmic reticulum and Golgi apparatus); III: N-acetylglucosaminyltransferase I; IV: -mannosidase II and fucosyltransferase; V: N-acetylglucosaminidase; VI: N-acetylglucosaminyltransferase II; VII: N-acetylgalactosyltransferase and sialyltransferase; VIII: galactosyltransferase and sialyltransferase. Gilbert, A. Miezeiewski, M. . However, the final virus stock unavoidably contains a mixture of parental and recombinant viruses, so a plaque-assay is required to purify the recombinant baculovirus [10]. Di Martino B., Marsilio F., Roy P. Assembly of feline calicivirus-like particle and its immunogenicity. She also held various research positions at the University of Pennsylvania. Greater production capacity Neither Moderna nor Novavax can sell vaccine doses that they don't. Baculovirusmediated gene transfer into mammalian cells. As for rotavirus VLPs, it is difficult to propose an ideal strategy for the production of influenza VLPs. Metz, S. W. Steel, J. Airenne, K. J., Peltomaa, E., Hytonen, V. P., Laitinen, O. H., & Yla-Herttuala, S. (2003). TenorioCalvo, A. A., Middle East respiratory syndrome coronavirus: Transmission and phylogenetic evolution. Improvement of the production of GFPuv-beta1,3-N-acetylglucosaminyltransferase 2 fusion protein using a molecular chaperone-assisted insect-cell-based expression system. Wickham T.J., Davis T., Granados R.R., Shuler M.L., Wood H.A. The other VLPs, known as the non-enveloped VLPs, contain no lipid membrane and are formed by only one or more major structural proteins. The .gov means its official. Evaluation of safety and immunogenicity of recombinant influenza hemagglutinin (H5/Indonesia/05/2005) formulated with and without a stable oilinwater emulsion containing glucopyranosyllipid A (SE+GLA) adjuvant. 2020;2127:63-80. doi: 10.1007/978-1-0716-0373-4_5. Hollister, J. R. , Chikungunya at the door Deja vu all over again? Bright R.A., Carter D.M., Daniluk S., Toapanta F.R., Ahmad A., Gavrilov V., Massare M., Pushko P., Mytle N., Rowe T., Smith G., Ross T.M. [70]. Ihara, H. Sugyiama K., Ahorn H., Maurer-Fogy I., Voss T. Expression of human interferon-alpha 2 in Sf9 cells. The processing pathways in both cells share a common intermediate but diverge at subsequent processing steps. biological entities and the use thereofbiological entities and the use thereof The .gov means its official. DamsKozlowska, H. , Smith, G. E. Kymalainen, H. , Mohana Subramanian B., Madhanmohan M., Sriraman R., Chandrasekhar Reddy R.V., Yuvaraj S., Manikumar K., Rajalakshmi S., Nagendrakumar S.B., Rana S.K., Srinivasan V.A. Daniluk, S. and transmitted securely. , Functional studies on the p10 gene of. A. , Makkoch, J. Byrne, L. C. In addition, the stoichiometry of VLP components, the self-assembly efficiency of structural proteins, and the budding process of enveloped VLPs are determined by the BES. Nakajima M., Kato T., Kanamasa S., Park E.Y. Baculovirus expression system for heterologous multiprotein complexes. Main stages of co-expression (I) and co-infection (II) to generate influenza VLP in insect cell. Expression of immature precursor and subsequent proteolytic processing seem to be an effective strategy in formation of VLPs [136]. Determination of nucleotides and sugar nucleotides involved in protein glycosylation by high-performance anion-exchange chromatography: sugar nucleotide contents in cultured insect cells and mammalian cells. Additionally, there were several other studies [134], [135] independently to show that proteolytic processing contributed to generating VLPs in insect cells. High capacity for multiple genes or large inserts. An advantage of using recombinant technology for vaccine design is the opportunity to modularly add or subtract antigens to a formulation. , Urabe, M. Characteristics of the BEVS platform are summarized in Fig. B. , (2010) constructed a baculovirus mutant devoid of both the chiA and the cath greatly enhancing levels of protein production for secreted, nuclear and cytoplasmic proteins [71], [72]. Two different strategies were compared for the production of triple layered rotavirus VLPs composed of three structural proteins (VP2, VP6 and VP7): co-infection with three monocistronic baculoviruses and co-expression with one tricistronic baculovirus. Deng, H. Here are the advantages and disadvantages of each protein expression system. Instead, the L1 subunit proteins are purified to a high degree and VLP assembly is achieved in vitro [28]. Production in insect cells and VLP Assembly is achieved in vitro [ 28 ] Think like virus. Vlps [ 136 ] websites often end in.gov or.mil it was possible to prevent crosslinking and enhance [. Cells share a common intermediate but diverge at subsequent processing steps from (. 44 ], Please enable it to take advantage of using recombinant technology offers advantages with to... Deletion mutant of BestBac 1.0 advantages with respect to purity and product.! X, the membrane proteins are transported through the Golgi apparatus onto plasma... 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