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Article: Broadly Neutralizing Antibodies for Influenza: Passive Immunotherapy and Intranasal Vaccination.

Biswas, Mrityunjoy / Yamazaki, Tatsuya / Chiba, Joe / Akashi-Takamura, Sachiko

2020 Volume 8, Issue 3

Abstract: Influenza viruses cause annual epidemics and occasional pandemics. The high diversity of viral envelope proteins permits viruses to escape host immunity. Therefore, the development of a universal vaccine and broadly neutralizing antibodies (bnAbs) is ... ...

Abstract	Influenza viruses cause annual epidemics and occasional pandemics. The high diversity of viral envelope proteins permits viruses to escape host immunity. Therefore, the development of a universal vaccine and broadly neutralizing antibodies (bnAbs) is essential for controlling various mutant viruses. Here, we review some potentially valuable bnAbs for influenza; one is a novel passive immunotherapy using a variable domain of heavy chain-only antibody (V
Keywords	covid19
Language	English
Publishing date	2020-07-29
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines8030424
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Article: Neutralizing Anti-Hemagglutinin Monoclonal Antibodies Induced by Gene-Based Transfer Have Prophylactic and Therapeutic Effects on Influenza Virus Infection.

Yamazaki, Tatsuya / Chiba, Joe / Akashi-Takamura, Sachiko

Vaccines

2018 Volume 6, Issue 3

Abstract: Hemagglutinin (HA) of influenza virus is a major target for vaccines. HA initiates the internalization of the virus into the host cell by binding to host sialic acid receptors; therefore, inhibition of HA can significantly prevent influenza virus ... ...

Abstract	Hemagglutinin (HA) of influenza virus is a major target for vaccines. HA initiates the internalization of the virus into the host cell by binding to host sialic acid receptors; therefore, inhibition of HA can significantly prevent influenza virus infection. However, the high diversity of HA permits the influenza virus to escape from host immunity. Moreover, the vaccine efficacy is poor in some high-risk populations (e.g., elderly or immunocompromised patients). Passive immunization with anti-HA monoclonal antibodies (mAbs) is an attractive therapy; however, this method has high production costs and requires repeated inoculations. To address these issues, several methods for long-term expression of mAb against influenza virus have been developed. Here, we provide an overview of methods using plasmid and viral adeno-associated virus (AAV) vectors that have been modified for higher expression of neutralizing antibodies in the host. We also examine two methods of injection, electro-transfer and hydrodynamic injection. Our results show that antibody gene transfer is effective against influenza virus infection even in immunocompromised mice, and antibody expression was detected in the serum and upper respiratory tract. We also demonstrate this method to be effective following influenza virus infection. Finally, we discuss the perspective of passive immunization with antibody gene transfer for future clinical trials.
Language	English
Publishing date	2018-06-26
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2703319-3
ISSN	2076-393X
ISSN	2076-393X
DOI	10.3390/vaccines6030035
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Article ; Online: DNA immunization using

Takatsuka, Shogo / Yamada, Hiroyuki / Haniuda, Kei / Ichihashi, Marina / Chiba, Joe / Kitamura, Daisuke

Bio-protocol

2019 Volume 9, Issue 4, Page(s) e3174

Abstract: Membrane proteins such as cytokine receptors and G protein-coupled receptors can be drug targets. Recently, we have generated specific monoclonal antibodies (mAbs) against the mouse IL-9 receptor (IL-9R) and found that IL-9R on memory B cells have ... ...

Abstract	Membrane proteins such as cytokine receptors and G protein-coupled receptors can be drug targets. Recently, we have generated specific monoclonal antibodies (mAbs) against the mouse IL-9 receptor (IL-9R) and found that IL-9R on memory B cells have critical roles in T-dependent immune response. So far, most antibodies against cell surface proteins have been generated by immunization of animals with recombinant proteins produced in
Language	English
Publishing date	2019-02-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2833269-6
ISSN	2331-8325 ; 2331-8325
ISSN (online)	2331-8325
ISSN	2331-8325
DOI	10.21769/BioProtoc.3174
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Article ; Online: An anti-perfringolysin O monoclonal antibody cross-reactive with streptolysin O protects against streptococcal toxic shock syndrome.

Matsumura, Takayuki / Nishiyama, Ayae / Aiko, Michio / Ainai, Akira / Ikebe, Tadayoshi / Chiba, Joe / Ato, Manabu / Takahashi, Yoshimasa

BMC research notes

2020 Volume 13, Issue 1, Page(s) 419

Abstract: Objective: Streptococcus pyogenes (Group A Streptococcus; GAS) causes a variety of infections that include life-threatening, severe invasive GAS infections, such as streptococcal toxic shock syndrome (STSS), with > 30% mortality rate, despite effective ... ...

Abstract	Objective: Streptococcus pyogenes (Group A Streptococcus; GAS) causes a variety of infections that include life-threatening, severe invasive GAS infections, such as streptococcal toxic shock syndrome (STSS), with > 30% mortality rate, despite effective antibiotics and treatment options. STSS clinical isolates highly express streptolysin O (SLO), a member of a large family of pore-forming toxins called cholesterol-dependent cytolysins (CDCs). SLO is an important toxic factor for GAS and may be an effective therapeutic target for the treatment of STSS. Our aim was to identify a monoclonal antibody (mAb) that reacts with SLO and has therapeutic potential for STSS treatment. Results: We focused on mAbs that had originally been established as neutralizing reagents to perfringolysin O (PFO), another member of the CDC family, as some cross-reactivity with SLO had been reported. Here, we confirmed cross-reactivity of an anti-PFO mAb named HS1 with SLO. In vitro analysis revealed that HS1 mAb sufficiently prevented human neutrophils from being killed by STSS clinical isolates. Furthermore, prophylactic and therapeutic injection of HS1 mAb into C57BL/6 mice significantly improved the survival rate following lethal infection with an STSS clinical isolate. These results highlight the therapeutic potential of HS1 mAb for STSS treatment.
MeSH term(s)	Animals ; Antibodies, Monoclonal ; Bacterial Proteins ; Bacterial Toxins ; Hemolysin Proteins ; Mice ; Mice, Inbred C57BL ; Shock, Septic/drug therapy ; Shock, Septic/prevention & control ; Streptococcal Infections/drug therapy ; Streptococcal Infections/prevention & control ; Streptococcus pyogenes ; Streptolysins
Chemical Substances	Antibodies, Monoclonal ; Bacterial Proteins ; Bacterial Toxins ; Hemolysin Proteins ; Streptolysins ; streptolysin O ; Clostridium perfringens theta-toxin (71329-60-7)
Language	English
Publishing date	2020-09-05
Publishing country	England
Document type	Journal Article
ZDB-ID	2413336-X
ISSN	1756-0500 ; 1756-0500
ISSN (online)	1756-0500
ISSN	1756-0500
DOI	10.1186/s13104-020-05264-2
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Article ; Online: STEAP4 regulates focal adhesion kinase activation and CpG motifs within STEAP4 promoter region are frequently methylated in DU145, human androgen-independent prostate cancer cells.

Tamura, Takahiko / Chiba, Joe

International journal of molecular medicine

2009 Volume 24, Issue 5, Page(s) 599–604

Abstract: The possible roles of STEAP4 in cancer progression have not been reported. In this study, we report that STEAP4 expression is able to inhibit anchorage-independent cell growth. We also demonstrate that STEAP4 associates with focal adhesion kinase (FAK) ... ...

Abstract	The possible roles of STEAP4 in cancer progression have not been reported. In this study, we report that STEAP4 expression is able to inhibit anchorage-independent cell growth. We also demonstrate that STEAP4 associates with focal adhesion kinase (FAK) and regulate the activity of FAK through Y397 phosphorylation. Furthermore, we show that CpG sequences in STEAP4 promoter region were frequently methylated in DU145, androgen-independent prostate cancer cells. Demethylation treatment induced STEAP4 expression in DU145, suggesting the possibility that STEAP4 expression in cancer cells is in part epigenetically regulated. Collectively, these data demonstrate a novel function of STEAP4 and that STEAP4 may play an important role in tumor malignancy.
MeSH term(s)	Androgens/metabolism ; Cell Line, Tumor ; CpG Islands/genetics ; DNA Methylation ; Down-Regulation/genetics ; Enzyme Activation ; Focal Adhesion Protein-Tyrosine Kinases/metabolism ; Gene Expression Regulation, Neoplastic ; Humans ; Male ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Promoter Regions, Genetic/genetics ; Prostatic Neoplasms/enzymology ; Prostatic Neoplasms/genetics ; Prostatic Neoplasms/pathology ; Protein Binding ; Tumor Stem Cell Assay
Chemical Substances	Androgens ; Membrane Proteins ; Phosphotyrosine (21820-51-9) ; Oxidoreductases (EC 1.-) ; STEAP4 protein, human (EC 1.16.1.-) ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2)
Language	English
Publishing date	2009-09-04
Publishing country	Greece
Document type	Journal Article
ZDB-ID	1444428-8
ISSN	1791-244X ; 1107-3756
ISSN (online)	1791-244X
ISSN	1107-3756
DOI	10.3892/ijmm_00000270
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Zs.A 4942: Show issues

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Article ; Online: Production of antibodies against multipass membrane proteins expressed in human tumor cells using dendritic cell immunization.

Tamura, Takahiko / Chiba, Joe

Journal of biomedicine & biotechnology

2009 Volume 2009, Page(s) 673098

Abstract: Antibody mediated therapeutic strategies against human malignant tumors have been widely authorized and clinically applied to cancer patients. In order to develop methods to generate antibodies reactive to the extracellular domains of multipass plasma ... ...

Abstract	Antibody mediated therapeutic strategies against human malignant tumors have been widely authorized and clinically applied to cancer patients. In order to develop methods to generate antibodies reactive to the extracellular domains of multipass plasma membrane proteins specifically expressed in malignant tumors, we examined the use of dendritic cells (DCs) for immunization. DCs were transduced with genes encoding the human six transmembrane epithelial antigen of prostate 1 (STEAP1), STEAP4, and seven transmembrane prostate specific G-protein coupled receptor (PSGR). Mice were immunized with these DCs and followed by repeated booster immunization with plasmids expressing each protein. The immunized mice produced significant amounts of antibodies against these proteins. Our results suggest that DC immunization is an effective method to produce antibodies reactive to extracellular regions of plasma membrane proteins with multiple-transmembrane domains, and may be useful to develop antibody mediated antitumor therapies.
MeSH term(s)	Animals ; Antibodies, Neoplasm/biosynthesis ; Antigens, Neoplasm/immunology ; Dendritic Cells/immunology ; Dendritic Cells/metabolism ; Humans ; Immunization ; Membrane Proteins/immunology ; Mice ; Mice, Inbred BALB C ; Neoplasm Proteins/immunology ; Oxidoreductases/immunology ; Receptors, Odorant/immunology ; Tumor Cells, Cultured
Chemical Substances	Antibodies, Neoplasm ; Antigens, Neoplasm ; Membrane Proteins ; Neoplasm Proteins ; OR51E2 protein, human ; Receptors, Odorant ; Oxidoreductases (EC 1.-) ; STEAP1 protein, human (EC 1.16.1.-) ; STEAP4 protein, human (EC 1.16.1.-)
Language	English
Publishing date	2009-04-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2052552-7
ISSN	1110-7251 ; 1110-7243
ISSN (online)	1110-7251
ISSN	1110-7243
DOI	10.1155/2009/673098
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Zs.A 5540: Show issues

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Article: Anti-WASP intrabodies inhibit inflammatory responses induced by Toll-like receptors 3, 7, and 9, in macrophages

Sakuma, Chisato / Sato, Mitsuru / Oshima, Takuma / Takenouchi, Takato / Chiba, Joe / Kitani, Hiroshi

Biochemical and biophysical research communications. 2015 Feb. 27, v. 458

2015

Abstract: Wiskott-Aldrich syndrome protein (WASP) is an adaptor molecule in immune cells. Recently, we showed that the WASP N-terminal domain interacted with the SH3 domain of Bruton's tyrosine kinase (Btk), and that the complex formed by WASP and Btk was ... ...

Abstract	Wiskott-Aldrich syndrome protein (WASP) is an adaptor molecule in immune cells. Recently, we showed that the WASP N-terminal domain interacted with the SH3 domain of Bruton's tyrosine kinase (Btk), and that the complex formed by WASP and Btk was important for TLR2 and TLR4 signaling in macrophages. Several other studies have shown that Btk played important roles in modulating innate immune responses through TLRs in immune cells. Here, we evaluated the significance of the interaction between WASP and Btk in TLR3, TLR7, and TLR9 signaling. We established bone marrow–derived macrophage cell lines from transgenic (Tg) mice that expressed intracellular antibodies (intrabodies) that specifically targeted the WASP N-terminal domain. One intrabody comprised the single-chain variable fragment and the other comprised the light-chain variable region single domain of an anti-WASP N-terminal monoclonal antibody. Both intrabodies inhibited the specific interaction between WASP and Btk, which impaired the expression of TNF-α, IL-6, and IL-1β in response to TLR3, TLR7, or TLR9 stimulation. Furthermore, the intrabodies inhibited the phosphorylation of both nuclear factor (NF)-κB and WASP in response to TLR3, TLR7, or TLR9 stimulation, in the Tg bone marrow-derived macrophages. These results suggested that WASP plays important roles in TLR3, TLR7, and TLR9 signaling by associating with Btk in macrophages.
Keywords	Toll-like receptor 2 ; Toll-like receptor 3 ; Toll-like receptor 4 ; Toll-like receptor 7 ; Toll-like receptor 9 ; genetically modified organisms ; inflammation ; innate immunity ; interleukin-1beta ; interleukin-6 ; macrophages ; mice ; monoclonal antibodies ; phosphorylation ; tumor necrosis factor-alpha ; tyrosine
Language	English
Dates of publication	2015-0227
Size	p. 28-33.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2015.01.049
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Article ; Online: A Novel Gene Delivery Vector of Agonistic Anti-Radioprotective 105 Expressed on Cell Membranes Shows Adjuvant Effect for DNA Immunization Against Influenza.

Yamazaki, Tatsuya / Biswas, Mrityunjoy / Kosugi, Kouyu / Nagashima, Maria / Inui, Masanori / Tomono, Susumu / Takagi, Hidekazu / Ichimonji, Isao / Nagaoka, Fumiaki / Ainai, Akira / Hasegawa, Hideki / Chiba, Joe / Akashi-Takamura, Sachiko

Frontiers in immunology

2020 Volume 11, Page(s) 606518

Abstract: Radioprotective 105 (RP105) (also termed CD180) is an orphan and unconventional Toll-like receptor (TLR) that lacks an intracellular signaling domain. The agonistic anti-RP105 monoclonal antibody (mAb) can cross-link RP105 on B cells, resulting in the ... ...

Abstract	Radioprotective 105 (RP105) (also termed CD180) is an orphan and unconventional Toll-like receptor (TLR) that lacks an intracellular signaling domain. The agonistic anti-RP105 monoclonal antibody (mAb) can cross-link RP105 on B cells, resulting in the proliferation and activation of B cells. Anti-RP105 mAb also has a potent adjuvant effect, providing higher levels of antigen-specific antibodies compared to alum. However, adjuvanticity is required for the covalent link between anti-RP105 mAb and the antigen. This is a possible obstacle to immunization due to the link between anti-RP105 mAb and some antigens, especially multi-transmembrane proteins. We have previously succeeded in inducing rapid and potent recombinant mAbs in mice using antibody gene-based delivery. To simplify the covalent link between anti-RP105 mAb and antigens, we generated genetic constructs of recombinant anti-RP105 mAb (αRP105) bound to the transmembrane domain of the IgG-B cell receptor (TM) (αRP105-TM), which could enable the anti-RP105 mAb to link the antigen
MeSH term(s)	Adjuvants, Immunologic/genetics ; Adjuvants, Immunologic/pharmacology ; Animals ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Antibodies, Monoclonal/pharmacology ; Antigens, CD/genetics ; Antigens, CD/immunology ; Antigens, CD/metabolism ; Antigens, Surface/genetics ; Antigens, Surface/metabolism ; B-Lymphocytes/drug effects ; B-Lymphocytes/immunology ; B-Lymphocytes/metabolism ; Cell Membrane/drug effects ; Cell Membrane/immunology ; Cell Membrane/metabolism ; Cell Proliferation/drug effects ; Coculture Techniques ; Gene Transfer Techniques ; Genetic Vectors ; HEK293 Cells ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Hemagglutinin Glycoproteins, Influenza Virus/pharmacology ; Humans ; Hybridomas ; Immunization ; Influenza Vaccines/genetics ; Influenza Vaccines/immunology ; Influenza Vaccines/pharmacology ; Lymphocyte Activation/drug effects ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Mice, Inbred BALB C ; Mice, Knockout ; Orthomyxoviridae Infections/immunology ; Orthomyxoviridae Infections/metabolism ; Orthomyxoviridae Infections/prevention & control ; Orthomyxoviridae Infections/virology ; Rats ; Receptors, IgG/genetics ; Receptors, IgG/immunology ; Spleen/drug effects ; Spleen/immunology ; Spleen/metabolism ; Vaccines, DNA/pharmacology
Chemical Substances	Adjuvants, Immunologic ; Antibodies, Monoclonal ; Antigens, CD ; Antigens, Surface ; H1N1 virus hemagglutinin ; Hemagglutinin Glycoproteins, Influenza Virus ; Influenza Vaccines ; Ly78 protein, mouse ; Ly86 protein, mouse ; Membrane Glycoproteins ; Receptors, IgG ; Vaccines, DNA
Language	English
Publishing date	2020-12-22
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2020.606518
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Article ; Online: Anti-WASP intrabodies inhibit inflammatory responses induced by Toll-like receptors 3, 7, and 9, in macrophages.

Sakuma, Chisato / Sato, Mitsuru / Oshima, Takuma / Takenouchi, Takato / Chiba, Joe / Kitani, Hiroshi

Biochemical and biophysical research communications

2015 Volume 458, Issue 1, Page(s) 28–33

Abstract	Wiskott-Aldrich syndrome protein (WASP) is an adaptor molecule in immune cells. Recently, we showed that the WASP N-terminal domain interacted with the SH3 domain of Bruton's tyrosine kinase (Btk), and that the complex formed by WASP and Btk was important for TLR2 and TLR4 signaling in macrophages. Several other studies have shown that Btk played important roles in modulating innate immune responses through TLRs in immune cells. Here, we evaluated the significance of the interaction between WASP and Btk in TLR3, TLR7, and TLR9 signaling. We established bone marrow-derived macrophage cell lines from transgenic (Tg) mice that expressed intracellular antibodies (intrabodies) that specifically targeted the WASP N-terminal domain. One intrabody comprised the single-chain variable fragment and the other comprised the light-chain variable region single domain of an anti-WASP N-terminal monoclonal antibody. Both intrabodies inhibited the specific interaction between WASP and Btk, which impaired the expression of TNF-α, IL-6, and IL-1β in response to TLR3, TLR7, or TLR9 stimulation. Furthermore, the intrabodies inhibited the phosphorylation of both nuclear factor (NF)-κB and WASP in response to TLR3, TLR7, or TLR9 stimulation, in the Tg bone marrow-derived macrophages. These results suggested that WASP plays important roles in TLR3, TLR7, and TLR9 signaling by associating with Btk in macrophages.
MeSH term(s)	Aminoquinolines/pharmacology ; Animals ; Antibodies/genetics ; Antibodies/immunology ; Antibodies/metabolism ; Bone Marrow Cells/cytology ; Cytokines/metabolism ; Inflammation/drug therapy ; Inflammation/immunology ; Inflammation/metabolism ; Macrophages/drug effects ; Macrophages/immunology ; Macrophages/metabolism ; Membrane Glycoproteins/immunology ; Membrane Glycoproteins/metabolism ; Mice, Inbred C57BL ; Mice, Transgenic ; NF-kappa B/metabolism ; Phosphorylation/drug effects ; Poly I-C/pharmacology ; Single-Chain Antibodies/genetics ; Single-Chain Antibodies/immunology ; Single-Chain Antibodies/metabolism ; Toll-Like Receptor 3/immunology ; Toll-Like Receptor 3/metabolism ; Toll-Like Receptor 7/immunology ; Toll-Like Receptor 7/metabolism ; Toll-Like Receptor 9/immunology ; Toll-Like Receptor 9/metabolism ; Wiskott-Aldrich Syndrome Protein/genetics ; Wiskott-Aldrich Syndrome Protein/immunology
Chemical Substances	Aminoquinolines ; Antibodies ; Cytokines ; Membrane Glycoproteins ; NF-kappa B ; Single-Chain Antibodies ; TLR3 protein, mouse ; Tlr7 protein, mouse ; Tlr9 protein, mouse ; Toll-Like Receptor 3 ; Toll-Like Receptor 7 ; Toll-Like Receptor 9 ; WAS protein, human ; Wiskott-Aldrich Syndrome Protein ; Poly I-C (O84C90HH2L) ; imiquimod (P1QW714R7M)
Language	English
Publishing date	2015-02-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2015.01.049
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Article ; Online: Novel ELISA using intracellularly biotinylated antigen for detection of antibody following DNA immunization.

Kimura, Ryuichiro / Yoda, Ayako / Hayashizaki, Yoshihide / Chiba, Joe

Japanese journal of infectious diseases

2010 Volume 63, Issue 1, Page(s) 41–48

Abstract: DNA immunization or vaccination, which refers to the injection of DNA encoding the corresponding antigen proteins, has become an attractive method for inducing the production of antibodies (Abs) in animals, since it does not require proteins as antigens. ...

Abstract	DNA immunization or vaccination, which refers to the injection of DNA encoding the corresponding antigen proteins, has become an attractive method for inducing the production of antibodies (Abs) in animals, since it does not require proteins as antigens. However, a method for detecting Abs produced in response to antigens is still essential for the quantification of Abs in the sera of immunized animals and for the screening of monoclonal antibody (mAb)-producing hybridomas. Here, we report a new system for the evaluation of Abs against antigens that are difficult to purify, by employing intracellular biotinylation of the antigen protein. The antigen tagged with a peptide to be biotinylated (Bio-tag) and codon-optimized bacterial BirA biotin ligase were co-expressed in mammalian cells, and the biotinylated Bio-tagged antigen was captured on a streptavidin-coated plate. Abs against five human nuclear antigens that were difficult to purify as full-length recombinant proteins were detected in the sera of DNA-immunized mice, and IgG mAbs against three of these antigens were selected by ELISA. The results demonstrate that this system employing intracellular biotinylation of the antigen is a powerful technique for stimulating the production of Abs following DNA immunization.
MeSH term(s)	Animals ; Antibodies/blood ; Antigens/metabolism ; Biotinylation ; Cell Line ; Enzyme-Linked Immunosorbent Assay/methods ; Female ; Humans ; Mice ; Mice, Inbred BALB C ; Vaccines, DNA/immunology
Chemical Substances	Antibodies ; Antigens ; Vaccines, DNA
Language	English
Publishing date	2010-01
Publishing country	Japan
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1478383-6
ISSN	1884-2836 ; 1344-6304
ISSN (online)	1884-2836
ISSN	1344-6304
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