{"title":"Thoughts on mRNA Vaccine Response.","authors":"Thomas Kieber-Emmons","doi":"10.1089/mab.2023.29013.editorial","DOIUrl":"https://doi.org/10.1089/mab.2023.29013.editorial","url":null,"abstract":"","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"42 1","pages":"1-2"},"PeriodicalIF":0.0,"publicationDate":"2023-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9414621","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Epitope Mapping of an Anti-Mouse CCR2 Monoclonal Antibody (C<sub>2</sub>Mab-6) Using Enzyme-Linked Immunosorbent Assay.","authors":"Tomohiro Tanaka, Hiroyuki Suzuki, Teizo Asano, Guanjie Li, Ren Nanamiya, Nami Tateyama, Yu Isoda, Yuki Okada, Hiyori Kobayashi, Takeo Yoshikawa, Mika K Kaneko, Yukinari Kato","doi":"10.1089/mab.2022.0020","DOIUrl":"https://doi.org/10.1089/mab.2022.0020","url":null,"abstract":"<p><p>CC chemokine receptor type-2 (CCR2) is a member of the G protein-coupled receptors, and is mainly expressed on cell surface of immune cells. CCR2 binds to its ligand, C-C motif chemokine 2 (also named as monocyte chemoattractant protein-1), which involves in the tumor progression by modulating the tumor microenvironment. Therefore, the monoclonal antibody (mAb) targeting CCR2 could be one of the strategies for cancer treatment. In this study, we investigated the critical epitope of C<sub>2</sub>Mab-6, an anti-mouse CCR2 (mCCR2) mAb developed by N-terminal peptides immunization. We first performed enzyme-linked immunosorbent assay (ELISA) using N-terminal peptides of mCCR2 and demonstrated that C<sub>2</sub>Mab-6 recognizes 1-19 amino acids of mCCR2. We further performed ELISA using 20 alanine-substituted peptides of mCCR2. C<sub>2</sub>Mab-6 lost the reaction to the alanine-substituted peptides of D3A, N4A, M6A, P8A, Q9A, and F10A. These results indicate that the binding epitope of C<sub>2</sub>Mab-6 includes Asp3, Asn4, Met6, Pro8, Gln9, and Phe10 of mCCR2.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"339-342"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10799059","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Hiroki Kawabata, Tomokazu Ohishi, Hiroyuki Suzuki, Teizo Asano, Manabu Kawada, Hiroyoshi Suzuki, Mika K Kaneko, Yukinari Kato
{"title":"A Defucosylated Mouse Anti-CD10 Monoclonal Antibody (31-mG<sub>2a</sub>-f) Exerts Antitumor Activity in a Mouse Xenograft Model of Renal Cell Cancers.","authors":"Hiroki Kawabata, Tomokazu Ohishi, Hiroyuki Suzuki, Teizo Asano, Manabu Kawada, Hiroyoshi Suzuki, Mika K Kaneko, Yukinari Kato","doi":"10.1089/mab.2021.0049","DOIUrl":"https://doi.org/10.1089/mab.2021.0049","url":null,"abstract":"<p><p>CD10 is a cell surface metalloendopeptidase that cleaves and degrades many secreted physiologically active peptides by its enzymatic activity. Although CD10 expression has been found in various types of cells, its expression is increased in several cancers, including renal cancer. In this study, the antitumor activity of a novel anti-human CD10 monoclonal antibody (mAb) was investigated. A defucosylated mouse IgG<sub>2a</sub> version of C<sub>10</sub>Mab-31 (31-mG<sub>2a</sub>-f) was created from an anti-CD10 mAb, C<sub>10</sub>Mab-31 (IgG<sub>1</sub>, kappa). Both C<sub>10</sub>Mab-31 and 31-mG<sub>2a</sub>-f specifically reacted with endogenous CD10 in renal cancer cells, VMRC-RCW, with the dissociation constant (<i>K</i><sub>D</sub>) values of 6.3 × 10<sup>-9</sup> M and 1.1 × 10<sup>-9</sup> M, respectively, indicating high binding affinity. To further examine the anti-CD10 mAb-mediated effector functions, the antibody-dependent cellular cytotoxicity (ADCC) and complement-dependent cytotoxicity (CDC) were examined. The 31-mG<sub>2a</sub>-f significantly exhibited ADCC and CDC against VMRC-RCW cells <i>in vitro</i>. Furthermore, 31-mG<sub>2a</sub>-f exhibited antitumor activities in mouse xenografts of VMRC-RCW cells. These results suggest that 31-mG<sub>2a</sub>-f exerts antitumor activities against CD10-expressing renal cancers and could be a valuable therapeutic candidate for treating them.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"320-327"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10797966","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Development of a Novel Anti-Mouse CCR6 Monoclonal Antibody (C<sub>6</sub>Mab-13) by N-Terminal Peptide Immunization.","authors":"Teizo Asano, Tomohiro Tanaka, Hiroyuki Suzuki, Guanjie Li, Ren Nanamiya, Nami Tateyama, Yu Isoda, Yuki Okada, Hiyori Kobayashi, Takeo Yoshikawa, Mika K Kaneko, Yukinari Kato","doi":"10.1089/mab.2022.0021","DOIUrl":"https://doi.org/10.1089/mab.2022.0021","url":null,"abstract":"<p><p>The CC chemokine receptor 6 (CCR6) is a G protein-coupled receptor family member that is highly expressed in B lymphocytes, certain subsets of effector and memory T cells, and immature dendritic cells. CCR6 has only one chemokine ligand, CCL20. The CCL20-CCR6 axis has been recognized as a therapeutic target for autoimmune diseases and tumor. This study developed specific monoclonal antibodies (mAbs) against mouse CCR6 (mCCR6) using the peptide immunization method. The established anti-mCCR6 mAb, C<sub>6</sub>Mab-13 (rat IgG<sub>1</sub>, kappa), reacted with mCCR6-overexpressed Chinese hamster ovary-K1 (CHO/mCCR6), and mCCR6-endogenously expressed P388 (mouse lymphoid neoplasma) and J774-1 (mouse macrophage-like) cells in flow cytometry. The dissociation constant (<i>K</i><sub>D</sub>) of C<sub>6</sub>Mab-13 for CHO/mCCR6 cells was determined to be 2.8 × 10<sup>-9</sup> M, indicating that C<sub>6</sub>Mab-13 binds to mCCR6 with high affinity. In summary, C<sub>6</sub>Mab-13 is useful for detecting mCCR6-expressing cells through flow cytometry.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"343-349"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10799060","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"What Can We Learn from Research with Monoclonal Antibody 1F7?","authors":"Heinz Kohler","doi":"10.1089/mab.2022.0003","DOIUrl":"https://doi.org/10.1089/mab.2022.0003","url":null,"abstract":"<p><p>1F7 is a monoclonal antibody that recognizes an idiotypic determinant expressed on primate antibodies binding to HIV-1 and hepatitis C proteins. This monoclonal antibody was used as a tool to dissect the immune response in humans infected with HIV-1 and hepatitis B. Furthermore, 1F7 was also used to manipulate the immune response against HIV-1 in macaques. The generation of a monoclonal antibody describing a network suggests similar antibodies could be developed as tools to dissect entangled networks in autoimmune diseases and allergic reactions. This review discusses the body of work done with 1F7 in the light of contemporary immunology.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"350-354"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10509318","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Can Endemic Human Coronaviruses Be a COVID-19 Vaccine Approach?","authors":"Thomas Kieber-Emmons","doi":"10.1089/mab.2022.29012.editorial","DOIUrl":"https://doi.org/10.1089/mab.2022.29012.editorial","url":null,"abstract":"","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"301-302"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10758291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Masaki Saito, Hiroyuki Suzuki, Tomohiro Tanaka, Teizo Asano, Mika K Kaneko, Yukinari Kato
{"title":"Development of an Anti-Mouse CCR8 Monoclonal Antibody (C<sub>8</sub>Mab-1) for Flow Cytometry and Immunocytochemistry.","authors":"Masaki Saito, Hiroyuki Suzuki, Tomohiro Tanaka, Teizo Asano, Mika K Kaneko, Yukinari Kato","doi":"10.1089/mab.2021.0069","DOIUrl":"https://doi.org/10.1089/mab.2021.0069","url":null,"abstract":"<p><p>It has been widely accepted that monoclonal antibody (mAb) is an effective tool for cancer immunotherapy. The C-C motif chemokine receptor 8 (CCR8) is highly expressed in regulatory T cells and many cancers and is associated with the progression of the cancers. However, its role in cancer progression remains unclear. Thus, the development of mAbs for CCR8 leads to cancer immunotherapy and elucidation of unknown mechanisms of CCR8-dependent cancer progression. In this study, we have developed an anti-mouse CCR8 (mCCR8) mAb (clone C<sub>8</sub>Mab-1, rat IgG<sub>2a</sub>, kappa) using the Cell-Based Immunization and Screening (CBIS) method. We showed that C<sub>8</sub>Mab-1 and its recombinant antibody (recC<sub>8</sub>Mab-1) bind to mCCR8-overexpressed Chinese hamster ovary (CHO)-K1 cells (CHO/mCCR8), but not to the parental CHO-K1 cells, in flow cytometry and immunofluorescence. Moreover, C<sub>8</sub>Mab-1 and recC<sub>8</sub>Mab-1 specifically reacted to P388 (a mouse lymphocyte-like cells) and J774-1 (a mouse macrophage-like cells), which express endogenous mCCR8, in both applications. These results suggest that C<sub>8</sub>Mab-1, developed using the CBIS method, is useful for flow cytometry and immunocytochemistry against exogenous and endogenous mCCR8.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"333-338"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10797964","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Development of Monoclonal Antibody 281-mG<sub>2a</sub>-f Against Golden Hamster Podoplanin.","authors":"Ren Nanamiya, Hiroyuki Suzuki, Junko Takei, Guanjie Li, Nohara Goto, Hiroyuki Harada, Masaki Saito, Tomohiro Tanaka, Teizo Asano, Mika K Kaneko, Yukinari Kato","doi":"10.1089/mab.2021.0058","DOIUrl":"https://doi.org/10.1089/mab.2021.0058","url":null,"abstract":"<p><p>Golden (Syrian) hamster (<i>Mesocricetus auratus</i>) is a small animal model of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infections. Pathological analyses of the tissues are required to understand the pathogenesis of SARS-CoV-2 and the evaluation of therapeutic modalities, including neutralizing monoclonal antibodies (mAbs). However, mAbs that recognize the golden hamster-derived antigens and distinguish specific cell types, such as the pneumocytes, are limited. Podoplanin (PDPN) is an essential marker of lung type I alveolar epithelial cells, kidney podocytes, and lymphatic endothelial cells. In this study, an anti-Chinese hamster (<i>Cricetulus griseus</i>) PDPN mAb PMab-281 (IgG<sub>3</sub>, kappa) was established using the Cell-Based Immunization and Screening (CBIS) method. A defucosylated mouse IgG<sub>2a</sub> version of PMab-281 (281-mG<sub>2a</sub>-f) was also developed. The 281-mG<sub>2a</sub>-f strongly recognized both the Chinese hamster and the golden hamster PDPN using flow cytometry and could detect lung type I alveolar epithelial cells, lymphatic endothelial cells, and Bowman's capsules in the kidney from the golden hamster using immunohistochemistry. These results suggest the usefulness of 281-mG<sub>2a</sub>-f for analyzing the golden hamster-derived tissues and cells for SARS-CoV-2 research.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"311-319"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10797967","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Development of a Sensitive Anti-Human CCR9 Monoclonal Antibody (C<sub>9</sub>Mab-11) by N-Terminal Peptide Immunization.","authors":"Tomohiro Tanaka, Hiroyuki Suzuki, Yu Isoda, Teizo Asano, Takuro Nakamura, Miyuki Yanaka, Saori Handa, Nozomi Takahashi, Saori Okuno, Takeo Yoshikawa, Guanjie Li, Ren Nanamiya, Nohara Goto, Nami Tateyama, Yuki Okada, Hiyori Kobayashi, Mika K Kaneko, Yukinari Kato","doi":"10.1089/mab.2022.0027","DOIUrl":"https://doi.org/10.1089/mab.2022.0027","url":null,"abstract":"<p><p>The C-C chemokine receptor 9 (CCR9) belongs to the G-protein-coupled receptor superfamily, and is highly expressed on the T cells and intestinal cells. CCR9 regulates various immune responses by binding to the C-C chemokine ligand, CCL25, and is involved in inflammatory diseases and tumors. Therefore, the development of sensitive monoclonal antibodies (mAbs) for CCR9 is necessary for treatment and diagnosis. In this study, we established a specific anti-human CCR9 (hCCR9) mAb; C<sub>9</sub>Mab-11 (mouse IgG<sub>2a</sub>, kappa), using the synthetic peptide immunization method. C<sub>9</sub>Mab-11 reacted with hCCR9-overexpressed Chinese hamster ovary-K1 (CHO/hCCR9) and hCCR9-endogenously expressed MOLT-4 (human T-lymphoblastic leukemia) cells in flow cytometry. The dissociation constant (<i>K</i><sub>D</sub>) of C<sub>9</sub>Mab-11 for CHO/hCCR9 and MOLT-4 cells were determined to be 1.2 × 10<sup>-9</sup> M and 4.9 × 10<sup>-10</sup> M, respectively, indicating that C<sub>9</sub>Mab-11 possesses a high affinity for both exogenously and endogenously hCCR9-expressing cells. Furthermore, C<sub>9</sub>Mab-11 clearly detected hCCR9 protein in CHO/hCCR9 cells using western blot analysis. In summary, C<sub>9</sub>Mab-11 can be a useful tool for analyzing hCCR9-related biological responses.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"303-310"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10818553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A Monoclonal Antibody Targeting C-Terminal Domain of Transmissible Gastroenteritis Virus Spike Protein.","authors":"Na Liu, Yaoming Li","doi":"10.1089/mab.2022.0030","DOIUrl":"https://doi.org/10.1089/mab.2022.0030","url":null,"abstract":"<p><p>The structure and function of the C-terminus domain (CTD) of porcine transmissible gastroenteritis virus (TGEV) spike protein remain largely unknown, thereby a specific monoclonal antibody (MAb) allows us to fully understand this domain. In this study, we developed a murine MAb against CTD of TGEV spike protein, as evidenced by the results of indirect fluorescent assay, Western blotting, and fluorescence-activated cell sorter. Further study showed that the MAb is able to exclusively recognize a 12-residue peptide (FKNVSDGVIYSV) derived from CTD of TGEV spike protein. This MAb can be used to elucidate the potential function of CTD of TGEV spike in virus attachment and entry, and warrants further intensive investigation.</p>","PeriodicalId":53514,"journal":{"name":"Monoclonal Antibodies in Immunodiagnosis and Immunotherapy","volume":"41 6","pages":"328-332"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10456888","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}