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Articles by T Nakashima
Total Records ( 3 ) for T Nakashima
  M Kuroda Morimoto , H Tanaka , N Hayashi , M Nakahira , Y Imai , M Imamura , K Yasuda , S Yumikura Futatsugi , K Matsui , T Nakashima , K Sugimura , H Tsutsui , H Sano and K. Nakanishi
 

We previously reported that intranasal challenge with ovalbumin (OVA) plus IL-18 induces airway hyperresponsiveness (AHR) and eosinophilic airway inflammation in mice with OVA-specific Th1 cells. These two conditions can be prevented by neutralizing anti-IFN- and anti-IL-13 antibodies, respectively. The mice develop AHR and eosinophilic airway inflammation after challenge with OVA plus LPS instead of IL-18 and endogenous IL-18 is known to be involved. In contrast, IL-18 does not facilitate these changes in mice possessing OVA-specific Th2 cells. Here, we investigated whether IL-18 is involved in the development of asthma in mice immunized and challenged with bacterial proteins. Upon intranasal exposure to protein A (SpA) derived from Staphylococcus aureus, mice immunized with SpA exhibited AHR and peribronchial eosinophilic inflammation if IFN- or IL-13 were present, respectively. The CD4+ T cells from draining lymph nodes (DLNs) of the SpA-immunized and -challenged mice produced a robust IFN- and IL-13 in response to immobilized anti-CD3 antibodies. Treatment with neutralizing anti-IL-18 antibodies prevented asthmatic inflammation concomitant with their impaired potential to express IFN- and IL-13. Furthermore, naive mice that received the CD4+ T cells from DLNs of SpA-immunized mice developed airway inflammation depending upon the presence of IL-18. Immunodeficient mice that received human PBMCs, which had been stimulated with SpA in vitro, developed dense peribronchial accumulation of human CD4+ T cells upon SpA challenge. Neutralizing anti-human IL-18 antibodies protected against this airway inflammation. These results suggest the importance of IL-18 for the development of asthmatic inflammation associated with airway exposure to bacterial proteins.

  S Muraoka , Y Ito , M Kamimura , M Baba , N Arima , Y Suda , S Hashiguchi , M Torikai , T Nakashima and K. Sugimura
 

By a biopanning method using cell sorter, we quickly isolated an antibody phage clone (S1T-A3) specific to human T-lymphotropic virus type 1-carrying T-cell line S1T from a human single chain Fv (scFv) antibody phage library. This scFv antibody bound to HTLV-1-carrying T-cell lines including MT-2, MT-4 and M8166 other than S1T, but not to non-HTLV-1-carrying T-cell lymphomas such as Jurkat and MOLT4 cells. Interestingly, this antibody induced the cell death on S1T cells very quickly (< 30 min). We tried to identify the target molecules by western blotting and mass spectrometric analysis, revealing that the target antigen was HLA class II DR. The cell death was induced only in dimmer form of scFv (diabody) and at 15-fold lower concentration than that of a fusion protein of scFv and human IgG Fc [(scFv)2-Fc] or anti HLA-DR mouse whole antibody L243. Thus, S1T-A3 diabody is a small antibody fragment with agonistic activity to induce cell death through HLA-DR. This is the first report elucidating that diabody specific to HLA-DR is effective to induce the cell death in T-cell malignancy especially adult T-cell leukaemic cell line.

  J Yang , R Yoshida , Y Kariya , X Zhang , S Hashiguchi , T Nakashima , Y Suda , A Takada , Y Ito and K. Sugimura
 

The development of new therapeutic targets and strategies to control highly pathogenic avian influenza (HPAI) H5N1 virus infection in humans is urgently needed. Neutralizing recombinant human antibodies would provide important agents for immunotherapy on human H5N1 virus infection and definition of the critical mimotope for vaccine development. In this study, we have characterized an anti-H5-specific scFv clone, 3D1 from the human-scFv-displaying phage library. 3D1 blocked the binding of H5-Fc to MDCK cells in flow cytometry and neutralized H5N1 subtype influenza A viruses in a microneutralization assay. Employing a peptide-displaying phage library, Ph.D-12, the mimotope was determined to be at #128-131 and #204-211 of H5, which are silic acid-binding regions. In consistency with this result, 3D1 binds the recombinant sugar-binding domain (#50G-#272E) produced by a baculovirus vector. The 3D1 antibody employs the germline gene VH1-23. As this antibody is the first human anti-H5 scFv clearly defined on the sugar-binding epitope, it allows us to investigate the influence of amino acid substitutions in this region on the determination of the binding specificity to either sialic acid 2,6-galactose (SA 2,6Gal) or sialic acid 2,3-galactose (SA 2,3Gal) providing new insight for the development of effective H5N1 pandemic vaccines.

 
 
 
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