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  1. Article: Targeting of HIV-1 Nef to the centrosome: implications for antigen processing.

    Lacaille, V G / Androlewicz, M J

    Traffic (Copenhagen, Denmark)

    2001  Volume 1, Issue 11, Page(s) 884–891

    Abstract: To gain a better understanding of the intracellular sites of antigen processing we have looked at the localization of human immunodeficiency virus (HIV)-1 Nef protein by confocal microscopic and biochemical means. We found that ubiquitin (Ub)-Nef fusion ... ...

    Abstract To gain a better understanding of the intracellular sites of antigen processing we have looked at the localization of human immunodeficiency virus (HIV)-1 Nef protein by confocal microscopic and biochemical means. We found that ubiquitin (Ub)-Nef fusion proteins were localized to the centrosome in transfected COS-7 cells, and that the colocalization was inhibited by the microtubule-disrupting agent, nocodazole. Interestingly, we found that Ub-Nef trafficking to the centrosome was not dependent upon the metabolic stability of Ub-Nef nor on the inhibition of proteasome activity. We also analyzed the MHC class I antigen processing of a reporter epitope linked to the Ub-Nef fusion proteins and found that Ub-Nef was processed in COS-7 cells. In addition, we show that this processing was inhibited by nocodazole. We suggest that the centrosome may serve as a site of antigen processing in vivo.
    MeSH term(s) Animals ; Antigen Presentation/drug effects ; Base Sequence ; COS Cells ; Centrosome/drug effects ; Centrosome/immunology ; Centrosome/metabolism ; DNA Primers/genetics ; Gene Products, nef/genetics ; Gene Products, nef/immunology ; Gene Products, nef/metabolism ; HIV-1/genetics ; HIV-1/immunology ; HIV-1/metabolism ; Humans ; Nocodazole/pharmacology ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; nef Gene Products, Human Immunodeficiency Virus
    Chemical Substances DNA Primers ; Gene Products, nef ; Recombinant Fusion Proteins ; nef Gene Products, Human Immunodeficiency Virus ; Nocodazole (SH1WY3R615)
    Language English
    Publishing date 2001-01-31
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1483852-7
    ISSN 1600-0854 ; 1398-9219
    ISSN (online) 1600-0854
    ISSN 1398-9219
    DOI 10.1034/j.1600-0854.2000.011107.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5634: Show issues Location:
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  2. Article: Photolabeling the transporter associated with antigen processing.

    Lacaille, V G / Androlewicz, M J

    Methods in molecular biology (Clifton, N.J.)

    2000  Volume 156, Page(s) 143–151

    MeSH term(s) ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP Binding Cassette Transporter, Subfamily B, Member 3 ; ATP-Binding Cassette Transporters/analysis ; ATP-Binding Cassette Transporters/metabolism ; Affinity Labels ; Antigen Presentation ; Azides ; B-Lymphocytes ; Cell Line ; Chromatography, High Pressure Liquid/methods ; Cross-Linking Reagents ; Dimerization ; Electrophoresis, Polyacrylamide Gel/methods ; Humans ; Major Histocompatibility Complex ; Protein Subunits
    Chemical Substances ATP Binding Cassette Transporter, Subfamily B, Member 2 ; ATP Binding Cassette Transporter, Subfamily B, Member 3 ; ATP-Binding Cassette Transporters ; Affinity Labels ; Azides ; Cross-Linking Reagents ; Protein Subunits ; TAP1 protein, human ; TAP2 protein, human (145892-13-3) ; hydroxysuccinimidyl-4-azidobenzoate (53053-08-0)
    Language English
    Publishing date 2000-11-01
    Publishing country United States
    Document type Journal Article
    ISSN 1064-3745
    ISSN 1064-3745
    DOI 10.1385/1-59259-062-4:143
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Antigenic peptide transporter.

    Lacaille, V G / Androlewicz, M J

    Pharmaceutical biotechnology

    1999  Volume 12, Page(s) 289–312

    MeSH term(s) ATP-Binding Cassette Transporters/antagonists & inhibitors ; ATP-Binding Cassette Transporters/metabolism ; Antigen Presentation ; Biological Transport ; Drug Design ; Histocompatibility Antigens Class I/metabolism ; Immediate-Early Proteins/metabolism ; Molecular Mimicry ; Peptides/metabolism ; Viral Envelope Proteins/metabolism ; Viral Proteins
    Chemical Substances ATP-Binding Cassette Transporters ; Histocompatibility Antigens Class I ; ICP47 protein, Herpes simplex virus ; Immediate-Early Proteins ; Peptides ; Viral Envelope Proteins ; Viral Proteins ; glycoprotein D, Human herpesvirus 1
    Language English
    Publishing date 1999
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1078-0467
    ISSN 1078-0467
    DOI 10.1007/0-306-46812-3_11
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Herpes simplex virus inhibitor ICP47 destabilizes the transporter associated with antigen processing (TAP) heterodimer.

    Lacaille, V G / Androlewicz, M J

    The Journal of biological chemistry

    1998  Volume 273, Issue 28, Page(s) 17386–17390

    Abstract: Chemical cross-linking of the transporter associated with antigen processing (TAP) heterodimer was used to determine whether the herpes simplex virus inhibitor of TAP, ICP47, induces a conformational change in TAP. Cross-linking of TAP in cellular ... ...

    Abstract Chemical cross-linking of the transporter associated with antigen processing (TAP) heterodimer was used to determine whether the herpes simplex virus inhibitor of TAP, ICP47, induces a conformational change in TAP. Cross-linking of TAP in cellular membranes produced a major species of approximately 220 kDa which was comprised solely of TAP.1 and TAP.2 and most likely represents the TAP heterodimer. Interestingly, prior treatment of TAP-containing membranes with TAP peptide substrates stimulated the formation of the cross-linked TAP heterodimer, whereas pretreatment of membranes with ICP47 completely blocked the formation of the cross-linked heterodimer. These data suggest that suitable substrates for TAP stabilize the TAP heterodimer, whereas ICP47 destabilizes the heterodimer. The results indicate that subtle conformational changes occur in the TAP heterodimer upon the binding of peptides and the inhibitor ICP47 and that ICP47 has a deleterious effect on TAP heterodimer structure, in addition to its role as a potent blocker of substrate binding to TAP.
    MeSH term(s) ATP-Binding Cassette Transporters/antagonists & inhibitors ; Amino Acid Sequence ; Animals ; Cell Line ; Dimerization ; Immediate-Early Proteins/metabolism ; Iodine Radioisotopes ; Spodoptera ; Viral Proteins
    Chemical Substances ATP-Binding Cassette Transporters ; ICP47 protein, Herpes simplex virus ; Immediate-Early Proteins ; Iodine Radioisotopes ; Viral Proteins
    Language English
    Publishing date 1998-07-10
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.273.28.17386
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Binding and transport of melanoma-specific antigenic peptides by the transporter associated with antigen processing.

    Chang, S A / Lacaille, V G / Guttoh, D S / Androlewicz, M J

    Molecular immunology

    1996  Volume 33, Issue 15, Page(s) 1165–1169

    Abstract: To gain insight into how tumor antigens are generated and presented, a panel of peptides corresponding to melanoma-specific T cell epitopes were tested for their transport capacity by the transporter associated with antigen processing (TAP). The melanoma ...

    Abstract To gain insight into how tumor antigens are generated and presented, a panel of peptides corresponding to melanoma-specific T cell epitopes were tested for their transport capacity by the transporter associated with antigen processing (TAP). The melanoma epitopes exhibited differential capacities to be transported by TAP in streptolysin O-permeabilized cells, as well as differential competition for peptide binding to TAP. The data indicate that some melanoma-specific epitopes are good substrates for TAP, while others are poor substrates for TAP. One of the epitopes, derived from tyrosinase, was transported into the endoplasmic reticulum (ER), in spite of being a poor competitor for reporter peptide transport and for peptide binding. These results suggest that the melanoma antigens follow distinct pathways for presentation, along the MHC class I pathway.
    MeSH term(s) ATP Binding Cassette Transporter, Subfamily B, Member 3 ; ATP-Binding Cassette Transporters/immunology ; Amino Acid Sequence ; Antigen Presentation ; Antigens, Neoplasm/metabolism ; Epitopes ; Humans ; Major Histocompatibility Complex/immunology ; Melanoma/immunology ; Peptides/chemistry ; Protein Binding
    Chemical Substances ATP Binding Cassette Transporter, Subfamily B, Member 3 ; ATP-Binding Cassette Transporters ; Antigens, Neoplasm ; Epitopes ; Peptides ; TAP2 protein, human (145892-13-3)
    Language English
    Publishing date 1996-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 424427-8
    ISSN 1872-9142 ; 0161-5890
    ISSN (online) 1872-9142
    ISSN 0161-5890
    DOI 10.1016/s0161-5890(96)00082-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 166: Show issues Location:
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