A method to generate antigen-specific mAb capable of staining formalin-fixed, paraffin-embedded tissue sections

Wang, Xinhui; Campoli, Michael; Cho, Hyun Suk; Ogino, Takeshi; Bandoh, Nobuyuki; Shen, Jijia; Hur, Soo Young; Kageshita, Toshiro; Ferrone, Soldano

doi:10.1016/j.jim.2005.02.006

Cited by 56 publications

(47 citation statements)

References 10 publications

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“…[15][16][17][18] Moreover, this trend was further influenced by use of formalin-fixed, paraffin-embedded tissue and the highly specific antibodies to selected HLA-B epitopes. 19 However, rigorous controls for specificity were possible by correlative identification of antibody staining with appropriate donor and recipient skin cell subpopulations (Supplementary Figure 1).…”

Section: Resultsmentioning

confidence: 99%

Biomarker evaluation of face transplant rejection: association of donor T cells with target cell injury

et al. 2014

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This series of 113 sequential biopsies of full facial transplants provides findings of potential translational significance as well as biological insights that could prompt reexamination of conventional paradigms of effector pathways in skin allograft rejection. Serial biopsies before, during, and after rejection episodes were evaluated for clinicopathological assessment that in selected cases included specific biomarkers for donorversus-recipient T cells. Histologic evidence of rejection included lymphocyte-associated injury to epidermal rete ridges, follicular infundibula, and dermal microvessels. Surprisingly, during active rejection, immune cells spatially associated with target cell injury consisted abundantly or predominantly of lymphocytes of donor origin with an immunophenotype typical of the resident memory T-cell subset. Current dogma assumes that skin allograft rejection is mediated by recipient T cells that attack epidermal targets, and the association of donor T cells with sites of target cell injury raises questions regarding the potential complexity of immune cell interactions in the rejection process. A more histopathologically refined and immune-based biomarker approach to assessment of rejection of facial transplants is now indicated. Modern Pathology (2014) 27, 788-799; doi:10.1038/modpathol.2013.249; published online 17 January 2014Keywords: donor T cell; facial transplant; graft-versus-host disease; skin allograft; T resident memory cells; vascularized composite allotransplantation Recent reports emphasizing the critical therapeutic importance of accurate diagnosis of transplant rejection 1 have stressed the imminent need for more precise clinicopathologic criteria and complementary application of relevant biomarkers. 2 The first systematic studies of any form of human allograft rejection were reported by Gibson and Medawar 3 in their classic description of skin rejection involving wartime aviators. 4 Early clues regarding the immunologic basis of skin graft rejection came from studies by Dvorak et al 5 and Bhan et al 6 that implicated both CD4 þ and CD8 þ T cells. These T-cell populations were presumed to be of recipient origin and considered to be primary effectors of epidermal and dermal microvascular target cell injury. With the recent advent of fullfacial transplantation, 7 detailed and sequential histopathologic surveillance for rejection in a manner seldom feasible for conventional skin allografts has become a necessity. However, existing schemas 8 for histologic recognition and grading of rejection in vascular composite allotransplantation are based primarily on allografts that may express relevant structural and immunological differences from facial tissues, eg, extremities (hand) and

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Section: Resultsmentioning

confidence: 99%

Biomarker evaluation of face transplant rejection: association of donor T cells with target cell injury

et al. 2014

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“…The TAP1-specific mAb NOB-1 and the TAP2-specific mAb NOB-2 are secreted by hybridomas derived from the fusion of murine myeloma cells P3-X63-Ag8.653 with splenocytes from BALB/c mice immunized with partial length TAP1 recombinant fusin protein (amino acids 434-735) and a keyhole limpet hemocianin-conjugated TAP1 peptide (amino acids 717-735) and with partial length TAP2 recombinant protein (amino acids 316-703), respectively. The specificity of the mAbs was assessed by their reactivity with molecules with the size corresponding the immunizing TAP1 and TAP2 when tested in Western blotting with a lysate of the human T2 cells and the mouse myeloma cells P3-X63-AG8.653 (22). The mAb HC-10 which recognizes a determinant expressed on all ß 2 m-free HLA-B and C heavy chains and on ß 2 m-free HLA-A10, -A28, -A29, -A30, -A31, -A32 and -A33 heavy chains were used (23).…”

Section: Methodsmentioning

confidence: 99%

HLA class I antigen and transporter associated with antigen processing downregulation in metastatic lesions of head and neck squamous cell carcinoma as a marker of poor prognosis

Bandoh¹

2010

Oncol Rep

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Abstract. HLA class I antigen processing machinery plays a crucial role in the generation of peptides from endogeneously synthesized proteins and in their presentation to cytotoxic T lymphocytes. The purpose of this study was to analyze the downregulation of HLA class I antigen, transporter associated with antigen processing (TAP) and tapasin in primary and metastatic lesions of head and neck squamous cell carcinoma (HNSCC) and to compare TAP, tapasin and HLA class I antigen downregulation in metastatic lesions with that of primary lesions. We analyzed expression levels of TAP1, TAP2, tapasin and HLA class I antigen in 25 primary and autologous metastatic lesions by staining formalin-fixed, paraffin-embedded tissue sections in the immunoperoxidase reaction. We identified the expression levels of TAP1, TAP2, tapasin and HLA class I antigen were coordinately downregulated in both primary and metastatic lesions and were significantly lower in metastatic lesions than in autologous primary lesions tested. HLA class I antigen downregulation in metastatic lesion was significantly associated with reduced disease-free survival of patients (P<0.05). Multivariate Cox proportional hazards model analysis identified negativity of HLA class I antigen as an independent prognostic marker. HLA class I antigen and TAP are likely to be downregulated in metastatic lesions compared with primary lesions in HNSCC. The higher frequency of HLA class I antigen and TAP downregulation in metastases play a role in the clinical course of the disease.

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“…The following antibodies were produced and characterized as described previously [18][19][20][21][22] : the ␦-specific monoclonal antibody (mAb) SY-5; the MB1-specific mAb SJJ-3; the -specific mAb NB1; the LMP2-specific mAb SY-1; the LMP7-specific mAb HB2; the LMP10-specific mAb TO-7; the TAP1-specific mAb NOB1; the TAP2-specific mAb NOB2; the calnexin-specific mAb TO-5; the calreticulin-specific mAb TO-11; the ERp57-specific mAb TO-2; the tapasin-specific mAb TO-3; and the ␤ 2 -m-specific mAb NAMB-1. They were labeled with fluorescein isothiocyanate (FITC) by the use of the Pierce FITC Antibody Labeling Kit.…”

Section: Protein Expression Analysismentioning

confidence: 99%

Alterations in the antigen processing-presenting machinery of transformed plasma cells are associated with reduced recognition by CD8+ T cells and characterize the progression of MGUS to multiple myeloma

Racanelli

Leone

Frassanito

et al. 2010

Blood

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A method to generate antigen-specific mAb capable of staining formalin-fixed, paraffin-embedded tissue sections

Cited by 56 publications

References 10 publications

Biomarker evaluation of face transplant rejection: association of donor T cells with target cell injury

Biomarker evaluation of face transplant rejection: association of donor T cells with target cell injury

HLA class I antigen and transporter associated with antigen processing downregulation in metastatic lesions of head and neck squamous cell carcinoma as a marker of poor prognosis

Alterations in the antigen processing-presenting machinery of transformed plasma cells are associated with reduced recognition by CD8+ T cells and characterize the progression of MGUS to multiple myeloma

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