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Thomas August - One of the best experts on this subject based on the ideXlab platform.

  • the enhanced immune response to the hiv gp160 lamp chimeric gene product targeted to the lysosome Membrane Protein Trafficking pathway
    Journal of Biological Chemistry, 1997
    Co-Authors: Albert L Ruff, Frank G Guarnieri, Kevin Staveleyocarroll, Robert F Siliciano, Thomas August
    Abstract:

    Abstract The lysosome-associated Membrane Proteins (LAMP), found in the outer Membrane of lysosomes and also in a multilaminar compartment that contains major histocompatibility complex class II (MHC II) Proteins, are directed to their localization by a cytoplasmic carboxyl-terminal sequence. Our studies of the immune response to LAMP-targeted Proteins has led to the application of a HIV-1 gp160/LAMP chimeric gene as a novel means to enhance the MHC II presentation of gp160. Immunofluorescence microscopy confirmed that the gp160/LAMP Protein had a cellular localization corresponding to that of lysosomes. Pulse-chase analysis confirmed that the rates of synthesis of gp160/LAMP and wild type gp160 were comparable and that both Proteins were processed to gp120 at similar rates. However, the gp160/LAMP was degraded more rapidly than the wild type gp160. MHC II-mediated T cell proliferation assays performed with cloned human cell lines showed that gp160/LAMP stimulated greater responses than did the wild type gp160. Moreover, mice vaccinated with recombinant vaccinia expressing gp160/LAMP had greater gp160-specific lymphoproliferation responses and higher titers of anti-V3 loop antibodies than mice vaccinated with recombinant vaccinia expressing wild type gp160.

  • The Enhanced Immune Response to the HIV gp160/LAMP Chimeric Gene Product Targeted to the Lysosome Membrane Protein Trafficking Pathway
    Journal of Biological Chemistry, 1997
    Co-Authors: Albert L Ruff, Frank G Guarnieri, Robert F Siliciano, Kevin Staveley-o'carroll, Thomas August
    Abstract:

    Abstract The lysosome-associated Membrane Proteins (LAMP), found in the outer Membrane of lysosomes and also in a multilaminar compartment that contains major histocompatibility complex class II (MHC II) Proteins, are directed to their localization by a cytoplasmic carboxyl-terminal sequence. Our studies of the immune response to LAMP-targeted Proteins has led to the application of a HIV-1 gp160/LAMP chimeric gene as a novel means to enhance the MHC II presentation of gp160. Immunofluorescence microscopy confirmed that the gp160/LAMP Protein had a cellular localization corresponding to that of lysosomes. Pulse-chase analysis confirmed that the rates of synthesis of gp160/LAMP and wild type gp160 were comparable and that both Proteins were processed to gp120 at similar rates. However, the gp160/LAMP was degraded more rapidly than the wild type gp160. MHC II-mediated T cell proliferation assays performed with cloned human cell lines showed that gp160/LAMP stimulated greater responses than did the wild type gp160. Moreover, mice vaccinated with recombinant vaccinia expressing gp160/LAMP had greater gp160-specific lymphoproliferation responses and higher titers of anti-V3 loop antibodies than mice vaccinated with recombinant vaccinia expressing wild type gp160.

Jiři Friml - One of the best experts on this subject based on the ideXlab platform.

  • BEX5/RabA1b Regulates trans-Golgi Network-to-Plasma Membrane Protein Trafficking in Arabidopsis
    The Plant Cell, 2012
    Co-Authors: Elena Feraru, Mugurel I Feraru, Rin Asaoka, Tomasz Paciorek, Riet De Rycke, Hirokazu Tanaka, Akihiko Nakano, Jiři Friml
    Abstract:

    Constitutive endocytic recycling is a crucial mechanism allowing regulation of the activity of Proteins at the plasma Membrane and for rapid changes in their localization, as demonstrated in plants for PIN-FORMED (PIN) Proteins, the auxin transporters. To identify novel molecular components of endocytic recycling, mainly exocytosis, we designed a PIN1-green fluorescent Protein fluorescence imaging–based forward genetic screen for Arabidopsis thaliana mutants that showed increased intracellular accumulation of cargos in response to the Trafficking inhibitor brefeldin A (BFA). We identified bex5 (for BFA-visualized exocytic Trafficking defective), a novel dominant mutant carrying a missense mutation that disrupts a conserved sequence motif of the small GTPase, RAS GENES FROM RAT BRAINA1b. bex5 displays defects such as enhanced Protein accumulation in abnormal BFA compartments, aberrant endosomes, and defective exocytosis and transcytosis. BEX5/RabA1b localizes to trans-Golgi network/early endosomes (TGN/EE) and acts on distinct Trafficking processes like those regulated by GTP exchange factors on ADP-ribosylation factors GNOM-LIKE1 and HOPM INTERACTOR7/BFA-VISUALIZED ENDOCYTIC Trafficking DEFECTIVE1, which regulate Trafficking at the Golgi apparatus and TGN/EE, respectively. All together, this study identifies Arabidopsis BEX5/RabA1b as a novel regulator of Protein Trafficking from a TGN/EE compartment to the plasma Membrane.

  • bex5 raba1b regulates trans golgi network to plasma Membrane Protein Trafficking in arabidopsis
    The Plant Cell, 2012
    Co-Authors: Elena Feraru, Mugurel I Feraru, Rin Asaoka, Tomasz Paciorek, Riet De Rycke, Hirokazu Tanaka, Akihiko Nakano, Jiři Friml
    Abstract:

    Constitutive endocytic recycling is a crucial mechanism allowing regulation of the activity of Proteins at the plasma Membrane and for rapid changes in their localization, as demonstrated in plants for PIN-FORMED (PIN) Proteins, the auxin transporters. To identify novel molecular components of endocytic recycling, mainly exocytosis, we designed a PIN1-green fluorescent Protein fluorescence imaging–based forward genetic screen for Arabidopsis thaliana mutants that showed increased intracellular accumulation of cargos in response to the Trafficking inhibitor brefeldin A (BFA). We identified bex5 (for BFA-visualized exocytic Trafficking defective), a novel dominant mutant carrying a missense mutation that disrupts a conserved sequence motif of the small GTPase, RAS GENES FROM RAT BRAINA1b. bex5 displays defects such as enhanced Protein accumulation in abnormal BFA compartments, aberrant endosomes, and defective exocytosis and transcytosis. BEX5/RabA1b localizes to trans-Golgi network/early endosomes (TGN/EE) and acts on distinct Trafficking processes like those regulated by GTP exchange factors on ADP-ribosylation factors GNOM-LIKE1 and HOPM INTERACTOR7/BFA-VISUALIZED ENDOCYTIC Trafficking DEFECTIVE1, which regulate Trafficking at the Golgi apparatus and TGN/EE, respectively. All together, this study identifies Arabidopsis BEX5/RabA1b as a novel regulator of Protein Trafficking from a TGN/EE compartment to the plasma Membrane.

Albert L Ruff - One of the best experts on this subject based on the ideXlab platform.

  • the enhanced immune response to the hiv gp160 lamp chimeric gene product targeted to the lysosome Membrane Protein Trafficking pathway
    Journal of Biological Chemistry, 1997
    Co-Authors: Albert L Ruff, Frank G Guarnieri, Kevin Staveleyocarroll, Robert F Siliciano, Thomas August
    Abstract:

    Abstract The lysosome-associated Membrane Proteins (LAMP), found in the outer Membrane of lysosomes and also in a multilaminar compartment that contains major histocompatibility complex class II (MHC II) Proteins, are directed to their localization by a cytoplasmic carboxyl-terminal sequence. Our studies of the immune response to LAMP-targeted Proteins has led to the application of a HIV-1 gp160/LAMP chimeric gene as a novel means to enhance the MHC II presentation of gp160. Immunofluorescence microscopy confirmed that the gp160/LAMP Protein had a cellular localization corresponding to that of lysosomes. Pulse-chase analysis confirmed that the rates of synthesis of gp160/LAMP and wild type gp160 were comparable and that both Proteins were processed to gp120 at similar rates. However, the gp160/LAMP was degraded more rapidly than the wild type gp160. MHC II-mediated T cell proliferation assays performed with cloned human cell lines showed that gp160/LAMP stimulated greater responses than did the wild type gp160. Moreover, mice vaccinated with recombinant vaccinia expressing gp160/LAMP had greater gp160-specific lymphoproliferation responses and higher titers of anti-V3 loop antibodies than mice vaccinated with recombinant vaccinia expressing wild type gp160.

  • The Enhanced Immune Response to the HIV gp160/LAMP Chimeric Gene Product Targeted to the Lysosome Membrane Protein Trafficking Pathway
    Journal of Biological Chemistry, 1997
    Co-Authors: Albert L Ruff, Frank G Guarnieri, Robert F Siliciano, Kevin Staveley-o'carroll, Thomas August
    Abstract:

    Abstract The lysosome-associated Membrane Proteins (LAMP), found in the outer Membrane of lysosomes and also in a multilaminar compartment that contains major histocompatibility complex class II (MHC II) Proteins, are directed to their localization by a cytoplasmic carboxyl-terminal sequence. Our studies of the immune response to LAMP-targeted Proteins has led to the application of a HIV-1 gp160/LAMP chimeric gene as a novel means to enhance the MHC II presentation of gp160. Immunofluorescence microscopy confirmed that the gp160/LAMP Protein had a cellular localization corresponding to that of lysosomes. Pulse-chase analysis confirmed that the rates of synthesis of gp160/LAMP and wild type gp160 were comparable and that both Proteins were processed to gp120 at similar rates. However, the gp160/LAMP was degraded more rapidly than the wild type gp160. MHC II-mediated T cell proliferation assays performed with cloned human cell lines showed that gp160/LAMP stimulated greater responses than did the wild type gp160. Moreover, mice vaccinated with recombinant vaccinia expressing gp160/LAMP had greater gp160-specific lymphoproliferation responses and higher titers of anti-V3 loop antibodies than mice vaccinated with recombinant vaccinia expressing wild type gp160.

Elena Feraru - One of the best experts on this subject based on the ideXlab platform.

  • BEX5/RabA1b Regulates trans-Golgi Network-to-Plasma Membrane Protein Trafficking in Arabidopsis
    The Plant Cell, 2012
    Co-Authors: Elena Feraru, Mugurel I Feraru, Rin Asaoka, Tomasz Paciorek, Riet De Rycke, Hirokazu Tanaka, Akihiko Nakano, Jiři Friml
    Abstract:

    Constitutive endocytic recycling is a crucial mechanism allowing regulation of the activity of Proteins at the plasma Membrane and for rapid changes in their localization, as demonstrated in plants for PIN-FORMED (PIN) Proteins, the auxin transporters. To identify novel molecular components of endocytic recycling, mainly exocytosis, we designed a PIN1-green fluorescent Protein fluorescence imaging–based forward genetic screen for Arabidopsis thaliana mutants that showed increased intracellular accumulation of cargos in response to the Trafficking inhibitor brefeldin A (BFA). We identified bex5 (for BFA-visualized exocytic Trafficking defective), a novel dominant mutant carrying a missense mutation that disrupts a conserved sequence motif of the small GTPase, RAS GENES FROM RAT BRAINA1b. bex5 displays defects such as enhanced Protein accumulation in abnormal BFA compartments, aberrant endosomes, and defective exocytosis and transcytosis. BEX5/RabA1b localizes to trans-Golgi network/early endosomes (TGN/EE) and acts on distinct Trafficking processes like those regulated by GTP exchange factors on ADP-ribosylation factors GNOM-LIKE1 and HOPM INTERACTOR7/BFA-VISUALIZED ENDOCYTIC Trafficking DEFECTIVE1, which regulate Trafficking at the Golgi apparatus and TGN/EE, respectively. All together, this study identifies Arabidopsis BEX5/RabA1b as a novel regulator of Protein Trafficking from a TGN/EE compartment to the plasma Membrane.

  • bex5 raba1b regulates trans golgi network to plasma Membrane Protein Trafficking in arabidopsis
    The Plant Cell, 2012
    Co-Authors: Elena Feraru, Mugurel I Feraru, Rin Asaoka, Tomasz Paciorek, Riet De Rycke, Hirokazu Tanaka, Akihiko Nakano, Jiři Friml
    Abstract:

    Constitutive endocytic recycling is a crucial mechanism allowing regulation of the activity of Proteins at the plasma Membrane and for rapid changes in their localization, as demonstrated in plants for PIN-FORMED (PIN) Proteins, the auxin transporters. To identify novel molecular components of endocytic recycling, mainly exocytosis, we designed a PIN1-green fluorescent Protein fluorescence imaging–based forward genetic screen for Arabidopsis thaliana mutants that showed increased intracellular accumulation of cargos in response to the Trafficking inhibitor brefeldin A (BFA). We identified bex5 (for BFA-visualized exocytic Trafficking defective), a novel dominant mutant carrying a missense mutation that disrupts a conserved sequence motif of the small GTPase, RAS GENES FROM RAT BRAINA1b. bex5 displays defects such as enhanced Protein accumulation in abnormal BFA compartments, aberrant endosomes, and defective exocytosis and transcytosis. BEX5/RabA1b localizes to trans-Golgi network/early endosomes (TGN/EE) and acts on distinct Trafficking processes like those regulated by GTP exchange factors on ADP-ribosylation factors GNOM-LIKE1 and HOPM INTERACTOR7/BFA-VISUALIZED ENDOCYTIC Trafficking DEFECTIVE1, which regulate Trafficking at the Golgi apparatus and TGN/EE, respectively. All together, this study identifies Arabidopsis BEX5/RabA1b as a novel regulator of Protein Trafficking from a TGN/EE compartment to the plasma Membrane.

Axel Martinelli - One of the best experts on this subject based on the ideXlab platform.

  • artemisinin resistance in rodent malaria mutation in the ap2 adaptor μ chain suggests involvement of endocytosis and Membrane Protein Trafficking
    Malaria Journal, 2013
    Co-Authors: Gisela Henriques, Axel Martinelli, Louise Rodrigues, Katarzyna Modrzynska, Richard Fawcett, Douglas R Houston
    Abstract:

    Background: The control of malaria, caused by Plasmodium falciparum, is hampered by the relentless evolution of drug resistance. Because artemisinin derivatives are now used in the most effective anti-malarial therapy, resistance to artemisinin would be catastrophic. Indeed, studies suggest that artemisinin resistance has already appeared in natural infections. Understanding the mechanisms of resistance would help to prolong the effective lifetime of these drugs. Genetic markers of resistance are therefore required urgently. Previously, a mutation in a de-ubiquitinating enzyme was shown to confer artemisinin resistance in the rodent malaria parasite Plasmodium chabaudi. Methods: Here, for a mutant P. chabaudi malaria parasite and its immediate progenitor, the in vivo artemisinin resistance phenotypes and the mutations arising using Illumina whole-genome re-sequencing were compared. Results: An increased artemisinin resistance phenotype is accompanied by one non-synonymous substitution. The mutated gene encodes the μ-chain of the AP2 adaptor complex, a component of the endocytic machinery. Homology models indicate that the mutated residue interacts with a cargo recognition sequence. In natural infections of the human malaria parasite P. falciparum, 12 polymorphisms (nine SNPs and three indels) were identified in the orthologous gene. Conclusion: An increased artemisinin-resistant phenotype occurs along with a mutation in a functional element of the AP2 adaptor Protein complex. This suggests that endocytosis and Trafficking of Membrane Proteins may be involved, generating new insights into possible mechanisms of resistance. The genotypes of this adaptor Protein can be evaluated for its role in artemisinin responses in human infections of P. falciparum.

  • Artemisinin resistance in rodent malaria - mutation in the AP2 adaptor μ-chain suggests involvement of endocytosis and Membrane Protein Trafficking
    Malaria Journal, 2013
    Co-Authors: Gisela Henriques, Axel Martinelli, Louise Rodrigues, Katarzyna Modrzynska, Richard Fawcett, Douglas R Houston, Sofia T. Borges, Umberto D'alessandro, Halidou Tinto, Corine Karema
    Abstract:

    The control of malaria, caused by Plasmodium falciparum, is hampered by the relentless evolution of drug resistance. Because artemisinin derivatives are now used in the most effective anti-malarial therapy, resistance to artemisinin would be catastrophic. Indeed, studies suggest that artemisinin resistance has already appeared in natural infections. Understanding the mechanisms of resistance would help to prolong the effective lifetime of these drugs. Genetic markers of resistance are therefore required urgently. Previously, a mutation in a de-ubiquitinating enzyme was shown to confer artemisinin resistance in the rodent malaria parasite Plasmodium chabaudi. Here, for a mutant P. chabaudi malaria parasite and its immediate progenitor, the in vivo artemisinin resistance phenotypes and the mutations arising using Illumina whole-genome re-sequencing were compared. An increased artemisinin resistance phenotype is accompanied by one non-synonymous substitution. The mutated gene encodes the μ-chain of the AP2 adaptor complex, a component of the endocytic machinery. Homology models indicate that the mutated residue interacts with a cargo recognition sequence. In natural infections of the human malaria parasite P. falciparum, 12 polymorphisms (nine SNPs and three indels) were identified in the orthologous gene. An increased artemisinin-resistant phenotype occurs along with a mutation in a functional element of the AP2 adaptor Protein complex. This suggests that endocytosis and Trafficking of Membrane Proteins may be involved, generating new insights into possible mechanisms of resistance. The genotypes of this adaptor Protein can be evaluated for its role in artemisinin responses in human infections of P. falciparum.