Characterization of monoclonal antibodies against prostate specific antigen produced by genetic immunization

Leinonen, Jari; Niemelä, Pauliina; Lövgren, Janita; Bocchi, Leonardo; Pettersson, Kim; Nevanlinna, Heli; Stenman, Ulf‐Hǎkan

doi:10.1016/j.jim.2004.04.022

Cited by 11 publications

(7 citation statements)

References 56 publications

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“…One interesting finding from literature is that although the delivery approach may be critical for the induction of high-level immune responses for human vaccine development, different DNA delivery approaches have been similarly successful in producing mAbs against a wide range of target antigens. Table 3 lists the mAbs elicited by the gene gun approach; 22,24,[31][32][33][34]37,43,55,57,58 needle injection, including intramuscular 19,20,23,38,41,[44][45][46][48][49][50] or intradermal 21,35,42 injection; and electroporation following intramuscular or intradermal injection. 27,28,39,52,53,56 One unique but less-studied approach is hydrodynamic intravenous delivery.…”

Section: Delivery Approach and Schedule Physical Versus Chemical Delimentioning

confidence: 99%

“…67 Another research group used a similar DNA prime-protein boost approach to generate a higher antibody titer and higher quality mAbs than those observed with protein immunization alone. 36 33 Intracellular (PED/PEA-15) 57 Intracellular (annexin-V) 58 Single transmembrane (CAR) 22 Two-transmembrane (P2X7) 24 GPI anchored enzyme 43 Intracelluar (BCL-6) 31 Intracelluar (MALT1) 32 Single transmembrane (MHCI-related gene A) 34 Parasite lipoprotein 55 Viral envelop (HIV gp120) 37 IM Bacteria toxin (Helicobacter pylori vacuolating cyto toxin) 38 Seven transmembrane, GPCR (TSHR) 19 Viral envelop (HGV E2) 48 Seven transmembrane, GPCR (TSHR) 20 Viral non-structure (Dengue NS1) 41 Viral envelop (H5N1) 49 Secretory protein, enzyme (prostate-specific antigen) 45 Viral surface (HBV preS2/S) 50 Seven transmembrane, GPCR (TSHR) 23 Secretory protein, cytokine (CKLF1) 44 Secretory protein, cytokine (Interferon beta) 46…”

Section: Immune Modulation Molecular Adjuvantsmentioning

confidence: 99%

“…21 Other studies included an additional DNA plasmid immunization by intramuscular or intradermal injection 3-5 days before fusion as a final boost. 42,45,51 Although the numbers of mAbs generated were small (that is, only a few mAbs from each fusion), mAbs with good binding affinity and diversity were reported. 45,51 The final DNA plasmid boost could also be delivered by hydrodynamic injection five days before fusion, and specific mAbs were successfully generated, 25 including some against very difficult targets, such as multi-transmembrane proteins.…”

Section: Role Of Final Boost Immunizationmentioning

confidence: 99%

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DNA immunization as a technology platform for monoclonal antibody induction

Liu¹,

Wang

2016

Emerging Microbes & Infections

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To combat the threat of many emerging infectious diseases, DNA immunization offers a unique and powerful approach to the production of high-quality monoclonal antibodies (mAbs) against various pathogens. Compared with traditional protein-based immunization approaches, DNA immunization is efficient for testing novel immunogen designs, does not require the production or purification of proteins from a pathogen or the use of recombinant protein technology and is effective at generating mAbs against conformation-sensitive targets. Although significant progress in the use of DNA immunization to generate mAbs has been made over the last two decades, the literature does not contain an updated summary of this experience. The current review provides a comprehensive analysis of the literature, including our own work, describing the use of DNA immunization to produce highly functional mAbs, in particular, those against emerging infectious diseases. Critical factors such as immunogen design, delivery approach, immunization schedule, use of immune modulators and the role of final boost immunization are discussed in detail.

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Section: Delivery Approach and Schedule Physical Versus Chemical Delimentioning

confidence: 99%

Section: Immune Modulation Molecular Adjuvantsmentioning

confidence: 99%

Section: Role Of Final Boost Immunizationmentioning

confidence: 99%

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DNA immunization as a technology platform for monoclonal antibody induction

Liu¹,

Wang

2016

Emerging Microbes & Infections

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“…DNA immunization employs an expression plasmid encoding the selected antigen to immunize animals. The transfected tissues of the immunized animal express the antigen which subsequently drives an antibody response [21]–[25]. DNA immunization with sequences coding polypeptide protein regions combines the advantages of both full length protein and peptide and immunization approaches, providing immunogens that comprise relatively large regions of the target protein with the potential for multiple epitopes, faster turn-around, and greater accessibility than full-length protein.…”

Section: Introductionmentioning

confidence: 99%

Impact of Immunization Technology and Assay Application on Antibody Performance – A Systematic Comparative Evaluation

Brown¹,

Joaquim²,

Chambers³

et al. 2011

PLoS ONE

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Antibodies are quintessential affinity reagents for the investigation and determination of a protein's expression patterns, localization, quantitation, modifications, purification, and functional understanding. Antibodies are typically used in techniques such as Western blot, immunohistochemistry (IHC), and enzyme-linked immunosorbent assays (ELISA), among others. The methods employed to generate antibodies can have a profound impact on their success in any of these applications. We raised antibodies against 10 serum proteins using 3 immunization methods: peptide antigens (3 per protein), DNA prime/protein fragment-boost (“DNA immunization”; 3 per protein), and full length protein. Antibodies thus generated were systematically evaluated using several different assay technologies (ELISA, IHC, and Western blot). Antibodies raised against peptides worked predominantly in applications where the target protein was denatured (57% success in Western blot, 66% success in immunohistochemistry), although 37% of the antibodies thus generated did not work in any of these applications. In contrast, antibodies produced by DNA immunization performed well against both denatured and native targets with a high level of success: 93% success in Western blots, 100% success in immunohistochemistry, and 79% success in ELISA. Importantly, success in one assay method was not predictive of success in another. Immunization with full length protein consistently yielded the best results; however, this method is not typically available for new targets, due to the difficulty of generating full length protein. We conclude that DNA immunization strategies which are not encumbered by the limitations of efficacy (peptides) or requirements for full length proteins can be quite successful, particularly when multiple constructs for each protein are used.

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“…(1)(2)(3)(4)(5) Although genetic immunization generally elicits a lower humoral immune response than immunization with protein antigens, its many advantages include defined specificity, expression of the protein in its native conformation, and production of high-avidity antibodies. (6) In addition, the time-consuming and labor-intensive procedures of protein expression and purification are not necessary.…”

Section: Introductionmentioning

confidence: 99%

Monoclonal Anti-Thrombopoietin Antibodies Generated by Genetic Immunization

Lim

Kim²,

Kim³

et al. 2006

Hybridoma

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Thrombopoietin (TPO) is a megakaryocyte growth and differentiation factor that is currently being investigated as a therapeutic for cancer patients undergoing myelosuppressive chemotherapy. We generated monoclonal antibodies (MAbs) specific for human thrombopoietin (hTPO) by genetic immunization using an hTPO expression plasmid and an adjuvant plasmid that encodes mouse granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin-4 (IL-4). All genetically immunized mice exhibited a high humoral immune response. Splenocytes from these mice were used to generate hybridomas. Two MAbs, designated 2B9A10 and 4C16B15 (of IgG1 and IgG3 isotypes, respectively), were subsequently selected and produced. They specifically recognized and precipitated recombinant hTPO produced by mammalian cells and were effective in sandwich enzyme-linked immunosorbent assays (ELISAs) for hTPO quantitation. Our results demonstrate that these MAbs should be useful for purification and quantitation of hTPO in clinical and laboratory settings.

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Characterization of monoclonal antibodies against prostate specific antigen produced by genetic immunization

Cited by 11 publications

References 56 publications

DNA immunization as a technology platform for monoclonal antibody induction

DNA immunization as a technology platform for monoclonal antibody induction

Impact of Immunization Technology and Assay Application on Antibody Performance – A Systematic Comparative Evaluation

Monoclonal Anti-Thrombopoietin Antibodies Generated by Genetic Immunization

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