The Experts below are selected from a list of 42 Experts worldwide ranked by ideXlab platform
P.a.l. Kongshavn - One of the best experts on this subject based on the ideXlab platform.
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Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody
International journal for parasitology, 1992Co-Authors: K. T. Y. Shaw, I.t. Shaw, P. Ryan, Mary M. Stevenson, P.a.l. KongshavnAbstract:Abstract Shaw K. T. Y. , Shaw I. T. , Ryan P. , Stevenson M. M. and Kongshavn P. A. L. 1992. Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody. International Journal for Parasitology 22 : 603–612. Trypanosoma musculi obtained from normal or irradiated (900 rad) hosts or from in vitro cultures were lysed and analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Similar protein banding patterns with a molecular weight (mol. wt) range from 34 to 68 kDa were observed between the two bloodstream forms. In comparison, lysates of cultured parasites showed a unique banding pattern of antigens within the same mol. wt range. Western blot of bloodstream form lysates, probed with immune plasma (IP), revealed a wide range of parasite proteins. However, when probed with the IgG2a-enriched fraction of IP, a major band of approximately 66 kDa was detected on the blot. Several bands of higher mol. wt were also observed. When anti- T. musculi monoclonal antibodies were used to probe the blot, the 66 kDa protein was again recognized. Using indirect fluorescence, live bloodstream form parasites were analysed by flow cytometry and the p66 protein was determined to be a surface molecule. Finally, lysates of 35 S-methionine-labelled trypanosomes were immunoprecipitated with Sepharose linked anti- T. musculi monoclonal antibodies and the eluted ligand analysed by SDS-PAGE and autoradiographed. The 66 kDa band was identified, therefore confirming that this protein was of parasite origin.
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Cells within the vascular system capable of mediating trypanocidal activity in vitro.
Infection and immunity, 1991Co-Authors: K. T. Y. Shaw, Y. Mawji, M. M. Stevenson, P.a.l. KongshavnAbstract:Cure of Trypanosoma musculi infection involves an effector mechanism mediated by Immunoglobulin G2a Antibody, C3, and an unidentified effector cell. In the present study, experiments were designed to identify the cell(s) within the vascular system that may be responsible for cure of trypanosomiasis. The ability of various cell populations to mediate killing of trypanosomes in the presence of C3 and immune plasma (IP) was tested in vitro. Blood-derived platelets or leukocytes or Bio-Gel-elicited macrophages or neutrophils were incubated at various concentrations with T. musculi, C3, and IP diluted up to 1 in 8. Trypanocidal activity was dependent upon the presence and concentration of IP and on the number of cells in the wells. Macrophages, neutrophils, and platelets were shown to kill with different potencies. With a 2:1 cell-to-parasite ratio, both macrophages and neutrophils reduced parasite numbers by 2 log, while platelets at a 40:1 ratio mediated a 1 log decrease. In addition, even in the absence of C3, the phagocytes were capable of killing trypanosomes while platelet trypanocidal activity was abrogated. The time course of trypanocidal activity was monitored for macrophages and neutrophils. The number of parasites decreased by 0.5 log by 4 h and 1 to 2 log by 8 h and by 20 h was reduced to zero. Cultured monolayers of endothelial cells were also tested for trypanocidal activity and shown to kill the parasites in the presence of IP and C3. The level of trypanocidal activity was dependent on the concentration of IP.
K. T. Y. Shaw - One of the best experts on this subject based on the ideXlab platform.
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Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody
International journal for parasitology, 1992Co-Authors: K. T. Y. Shaw, I.t. Shaw, P. Ryan, Mary M. Stevenson, P.a.l. KongshavnAbstract:Abstract Shaw K. T. Y. , Shaw I. T. , Ryan P. , Stevenson M. M. and Kongshavn P. A. L. 1992. Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody. International Journal for Parasitology 22 : 603–612. Trypanosoma musculi obtained from normal or irradiated (900 rad) hosts or from in vitro cultures were lysed and analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Similar protein banding patterns with a molecular weight (mol. wt) range from 34 to 68 kDa were observed between the two bloodstream forms. In comparison, lysates of cultured parasites showed a unique banding pattern of antigens within the same mol. wt range. Western blot of bloodstream form lysates, probed with immune plasma (IP), revealed a wide range of parasite proteins. However, when probed with the IgG2a-enriched fraction of IP, a major band of approximately 66 kDa was detected on the blot. Several bands of higher mol. wt were also observed. When anti- T. musculi monoclonal antibodies were used to probe the blot, the 66 kDa protein was again recognized. Using indirect fluorescence, live bloodstream form parasites were analysed by flow cytometry and the p66 protein was determined to be a surface molecule. Finally, lysates of 35 S-methionine-labelled trypanosomes were immunoprecipitated with Sepharose linked anti- T. musculi monoclonal antibodies and the eluted ligand analysed by SDS-PAGE and autoradiographed. The 66 kDa band was identified, therefore confirming that this protein was of parasite origin.
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Cells within the vascular system capable of mediating trypanocidal activity in vitro.
Infection and immunity, 1991Co-Authors: K. T. Y. Shaw, Y. Mawji, M. M. Stevenson, P.a.l. KongshavnAbstract:Cure of Trypanosoma musculi infection involves an effector mechanism mediated by Immunoglobulin G2a Antibody, C3, and an unidentified effector cell. In the present study, experiments were designed to identify the cell(s) within the vascular system that may be responsible for cure of trypanosomiasis. The ability of various cell populations to mediate killing of trypanosomes in the presence of C3 and immune plasma (IP) was tested in vitro. Blood-derived platelets or leukocytes or Bio-Gel-elicited macrophages or neutrophils were incubated at various concentrations with T. musculi, C3, and IP diluted up to 1 in 8. Trypanocidal activity was dependent upon the presence and concentration of IP and on the number of cells in the wells. Macrophages, neutrophils, and platelets were shown to kill with different potencies. With a 2:1 cell-to-parasite ratio, both macrophages and neutrophils reduced parasite numbers by 2 log, while platelets at a 40:1 ratio mediated a 1 log decrease. In addition, even in the absence of C3, the phagocytes were capable of killing trypanosomes while platelet trypanocidal activity was abrogated. The time course of trypanocidal activity was monitored for macrophages and neutrophils. The number of parasites decreased by 0.5 log by 4 h and 1 to 2 log by 8 h and by 20 h was reduced to zero. Cultured monolayers of endothelial cells were also tested for trypanocidal activity and shown to kill the parasites in the presence of IP and C3. The level of trypanocidal activity was dependent on the concentration of IP.
Nirbhay Kumar - One of the best experts on this subject based on the ideXlab platform.
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Purified malaria pigment (hemozoin) enhances dendritic cell maturation and modulates the isotype of antibodies induced by a DNA vaccine.
Infection and immunity, 2002Co-Authors: Cevayir Coban, Ken J Ishii, David J. Sullivan, Nirbhay KumarAbstract:Hemozoin (malaria pigment) has been implicated in the modulation of immune responses during malaria infection. This study was designed to evaluate the effect of purified hemozoin on the in vitro activation of myeloid dendritic cells. Our study also revealed that in addition to enhancing the maturation of dendritic cells, hemozoin also greatly promotes Immunoglobulin G2a Antibody responses when coadministered with a DNA vaccine plasmid encoding Pfs25, a Plasmodium falciparum transmission-blocking antigen.
Mary M. Stevenson - One of the best experts on this subject based on the ideXlab platform.
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Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody
International journal for parasitology, 1992Co-Authors: K. T. Y. Shaw, I.t. Shaw, P. Ryan, Mary M. Stevenson, P.a.l. KongshavnAbstract:Abstract Shaw K. T. Y. , Shaw I. T. , Ryan P. , Stevenson M. M. and Kongshavn P. A. L. 1992. Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody. International Journal for Parasitology 22 : 603–612. Trypanosoma musculi obtained from normal or irradiated (900 rad) hosts or from in vitro cultures were lysed and analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Similar protein banding patterns with a molecular weight (mol. wt) range from 34 to 68 kDa were observed between the two bloodstream forms. In comparison, lysates of cultured parasites showed a unique banding pattern of antigens within the same mol. wt range. Western blot of bloodstream form lysates, probed with immune plasma (IP), revealed a wide range of parasite proteins. However, when probed with the IgG2a-enriched fraction of IP, a major band of approximately 66 kDa was detected on the blot. Several bands of higher mol. wt were also observed. When anti- T. musculi monoclonal antibodies were used to probe the blot, the 66 kDa protein was again recognized. Using indirect fluorescence, live bloodstream form parasites were analysed by flow cytometry and the p66 protein was determined to be a surface molecule. Finally, lysates of 35 S-methionine-labelled trypanosomes were immunoprecipitated with Sepharose linked anti- T. musculi monoclonal antibodies and the eluted ligand analysed by SDS-PAGE and autoradiographed. The 66 kDa band was identified, therefore confirming that this protein was of parasite origin.
P. Ryan - One of the best experts on this subject based on the ideXlab platform.
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Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody
International journal for parasitology, 1992Co-Authors: K. T. Y. Shaw, I.t. Shaw, P. Ryan, Mary M. Stevenson, P.a.l. KongshavnAbstract:Abstract Shaw K. T. Y. , Shaw I. T. , Ryan P. , Stevenson M. M. and Kongshavn P. A. L. 1992. Identification of immunodominant Trypanosoma musculi antigens recognized by monoclonal Antibody and curative Immunoglobulin G2a Antibody. International Journal for Parasitology 22 : 603–612. Trypanosoma musculi obtained from normal or irradiated (900 rad) hosts or from in vitro cultures were lysed and analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Similar protein banding patterns with a molecular weight (mol. wt) range from 34 to 68 kDa were observed between the two bloodstream forms. In comparison, lysates of cultured parasites showed a unique banding pattern of antigens within the same mol. wt range. Western blot of bloodstream form lysates, probed with immune plasma (IP), revealed a wide range of parasite proteins. However, when probed with the IgG2a-enriched fraction of IP, a major band of approximately 66 kDa was detected on the blot. Several bands of higher mol. wt were also observed. When anti- T. musculi monoclonal antibodies were used to probe the blot, the 66 kDa protein was again recognized. Using indirect fluorescence, live bloodstream form parasites were analysed by flow cytometry and the p66 protein was determined to be a surface molecule. Finally, lysates of 35 S-methionine-labelled trypanosomes were immunoprecipitated with Sepharose linked anti- T. musculi monoclonal antibodies and the eluted ligand analysed by SDS-PAGE and autoradiographed. The 66 kDa band was identified, therefore confirming that this protein was of parasite origin.
