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  • 1
    Online Resource
    Online Resource
    Nef-mediated MHC class I down-regulation unmasks clonal differences in virus suppression by SIV-specific CD8+ T cells independent of IFN-γ and CD107a responses
    Elsevier BV ; 2009
    In:  Virology Vol. 391, No. 1 ( 2009-08), p. 130-139
    Details
    In: Virology, Elsevier BV, Vol. 391, No. 1 ( 2009-08), p. 130-139
    Type of Medium: Online Resource
    ISSN: 0042-6822
    URL: Article
    DOI: 10.1016/j.virol.2009.06.008
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2009
    detail.hit.zdb_id: 1471925-3
    SSG: 12
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  • 2
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    Online Resource
    The Mamu B⁎17-restricted SIV Nef IW9 to TW9 mutation abrogates correct epitope processing and presentation without loss of replicative fitness
    Elsevier BV ; 2008
    In:  Virology Vol. 375, No. 1 ( 2008-05), p. 307-314
    Details
    In: Virology, Elsevier BV, Vol. 375, No. 1 ( 2008-05), p. 307-314
    Type of Medium: Online Resource
    ISSN: 0042-6822
    URL: Article
    DOI: 10.1016/j.virol.2008.02.005
    RVK:
    WA 15000
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2008
    detail.hit.zdb_id: 1471925-3
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  • 3
    Online Resource
    Online Resource
    Quantitation of HLA Class II Protein Incorporated into Human Immunodeficiency Type 1 Virions Purified by Anti-CD45 Immunoaffinity Depletion of Microvesicles
    American Society for Microbiology ; 2003
    In:  Journal of Virology Vol. 77, No. 23 ( 2003-12), p. 12699-12709
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 77, No. 23 ( 2003-12), p. 12699-12709
    Abstract: Among the many host cell-derived proteins found in human immunodeficiency virus type 1 (HIV-1), HLA class II (HLA-II) appears to be selectively incorporated onto virions and may contribute to mechanisms of indirect imunopathogenesis in HIV infection and AIDS. However, the amount of HLA-II on the surface of HIV-1 particles has not been reliably determined due to contamination of virus preparations by microvesicles containing host cell proteins, including HLA-II. Even rigorous sucrose density centrifugation is unable to completely separate HIV-1 from microvesicles. CD45, a leukocyte integral membrane protein, is found on microvesicles, yet appears to be excluded from HIV-1 particles. Exploiting this observation, we have developed a CD45-based immunoaffinity depletion method for removing CD45-containing microvesicles that yields highly purified preparations of virions. Examination of CD45-depleted HIV-1 MN by high-pressure liquid chromatography, protein sequencing, and amino acid analyses determined a molar ratio of HLA-II to Gag of 0.04 to 0.05 in the purified virions, corresponding to an estimated average of 50 to 63 native HLA-II complexes (i.e., a dimer of α and β heterodimers) per virion. These values are approximately 5- to 10-fold lower than those previously determined for other virion preparations that contained microvesicles. Our observations demonstrate the utility of CD45 immunoaffinity-based approaches for producing highly purified retrovirus preparations for applications that would benefit from the use of virus that is essentially free of microvesicles.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.77.23.12699-12709.2003
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
    detail.hit.zdb_id: 1495529-5
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  • 4
    Online Resource
    Online Resource
    Preferential Small Intestine Homing and Persistence of CD8 T Cells in Rhesus Macaques Achieved by Molecularly Engineered Expression of CCR9 and Reduced Ex Vivo Manipulation
    American Society for Microbiology ; 2019
    In:  Journal of Virology Vol. 93, No. 21 ( 2019-11)
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 93, No. 21 ( 2019-11)
    Abstract: A doptive c ell t ransfer (ACT) is a powerful experimental approach to directly study T-cell-mediated immunity in vivo . In the rhesus macaque AIDS virus model, infusing simian immunodeficiency virus (SIV)-infected animals with CD8 T cells engineered to express anti-SIV T-cell receptor specificities enables direct experimentation to better understand antiviral T-cell immunity in vivo . Limiting factors in ACT experiments include suboptimal trafficking to, and poor persistence in, the secondary lymphoid tissues targeted by AIDS viruses. Previously, we redirected CD8 T cells to B-cell follicles by ectopic expression of the CXCR5 homing protein. Here, we modify peripheral blood mononuclear cell (PBMC)-derived CD8 T cells to express the CCR9 chemokine receptor, which induces preferential homing of the engineered cells to the small intestine, a site of intense early AIDS virus replication and pathology in rhesus macaques. Additionally, we increase in vivo persistence and overall systemic distribution of infused CD8 T cells, especially in secondary lymphoid tissues, by minimizing ex vivo culture/manipulation, thereby avoiding the loss of CD28 + /CD95 + central memory T cells by differentiation in culture. These proof-of-principle results establish the feasibility of preferentially localizing PBMC-derived CD8 T cells to the small intestine and enables the direct experimental ACT-based assessment of the potential role of the quality and timing of effective antiviral CD8 T-cell responses to inhibit viral infection and subsequent replication in small intestine CD4 T cells. More broadly, these results support the engineered expression of homing proteins to direct CD8 T cells to target tissues as a means for both experimental and potential therapeutic advances in T-cell immunotherapies, including cancer. IMPORTANCE A doptive c ell t ransfer (ACT) of T cells engineered with antigen-specific effector properties can deliver targeted immune responses against malignancies and infectious diseases. Current T-cell-based therapeutic ACT relies on circulatory distribution to deliver engineered T cells to their targets, an approach which has proven effective for some leukemias but provided only limited efficacy against solid tumors. Here, engineered expression of the CCR9 homing receptor redirected CD8 T cells to the small intestine in rhesus macaque ACT experiments. Targeted homing of engineered T-cell immunotherapies holds promise to increase the effectiveness of adoptively transferred cells in both experimental and clinical settings.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.00896-19
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2019
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  • 5
    Online Resource
    Online Resource
    Human Cellular Nucleic Acid-Binding Protein Zn 2+ Fingers Support Replication of Human Immunodeficiency Virus Type 1 When They Are Substituted in the Nucleocapsid Protein
    American Society for Microbiology ; 2003
    In:  Journal of Virology Vol. 77, No. 15 ( 2003-08), p. 8524-8531
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 77, No. 15 ( 2003-08), p. 8524-8531
    Abstract: A family of cellular nucleic acid binding proteins (CNBPs) contains seven Zn 2+ fingers that have many of the structural characteristics found in retroviral nucleocapsid (NC) Zn 2+ fingers. The sequence of the NH 2 -terminal NC Zn 2+ finger of the pNL4-3 clone of human immunodeficiency virus type 1 (HIV-1) was replaced individually with sequences from each of the seven fingers from human CNBP. Six of the mutants were normal with respect to protein composition and processing, full-length genomic RNA content, and infectivity. One of the mutants, containing the fifth CNBP Zn 2+ finger (CNBP-5) packaged reduced levels of genomic RNA and was defective in infectivity. There appear to be defects in reverse transcription in the CNBP-5 infections. Models of Zn 2+ fingers were constructed by using computational methods based on available structural data, and atom-atom interactions were determined by the hydropathic orthogonal dynamic analysis of the protein method. Defects in the CNBP-5 mutant could possibly be explained, in part, by restrictions of a set of required atom-atom interactions in the CNBP-5 Zn 2+ finger compared to mutant and wild-type Zn 2+ fingers in NC that support replication. The present study shows that six of seven of the Zn 2+ fingers from the CNBP protein can be used as substitutes for the Zn 2+ finger in the NH 2 -terminal position of HIV-1 NC. This has obvious implications in antiviral therapeutics and DNA vaccines employing NC Zn 2+ finger mutants.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.77.15.8524-8531.2003
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
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  • 6
    Online Resource
    Online Resource
    Dynamic Fluorescent Imaging of Human Immunodeficiency Virus Type 1 Gag in Live Cells by Biarsenical Labeling
    American Society for Microbiology ; 2005
    In:  Journal of Virology Vol. 79, No. 7 ( 2005-04), p. 4055-4065
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 79, No. 7 ( 2005-04), p. 4055-4065
    Abstract: Human immunodeficiency virus type 1 (HIV-1) Gag is the primary structural protein of the virus and is sufficient for particle formation. We utilized the recently developed biarsenical-labeling method to dynamically observe HIV-1 Gag within live cells by adding a tetracysteine tag (C-C-P-G-C-C) to the C terminus of Gag in both Pr55 Gag expression and full-length proviral constructs. Membrane-permeable biarsenical compounds FlAsH and ReAsH covalently bond to this tetracysteine sequence and specifically fluoresce, effectively labeling Gag in the cell. Biarsenical labeling readily and specifically detected a tetracysteine-tagged HIV-1 Gag protein (Gag-TC) in HeLa, Mel JuSo, and Jurkat T cells by deconvolution fluorescence microscopy. Gag-TC was localized primarily at or near the plasma membrane in all cell types examined. Fluorescent two-color analysis of Gag-TC in HeLa cells revealed that nascent Gag was present mostly at the plasma membrane in distinct regions. Intracellular imaging of a Gag-TC myristylation mutant observed a diffuse signal throughout the cell, consistent with the role of myristylation in Gag localization to the plasma membrane. In contrast, mutation of the L-domain core sequence did not appreciably alter the localization of Gag, suggesting that the PTAP L domain functions at the site of budding rather than as a targeting signal. Taken together, our results show that Gag concentrates in specific plasma membrane areas rapidly after translation and demonstrate the utility of biarsenical labeling for visualizing the dynamic localization of Gag.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.79.7.4055-4065.2005
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2005
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  • 7
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    Online Resource
    Analysis and Localization of Cyclophilin A Found in the Virions of Human Immunodeficiency Virus Type 1 MN Strain
    Mary Ann Liebert Inc ; 1995
    In:  AIDS Research and Human Retroviruses Vol. 11, No. 9 ( 1995-09), p. 1003-1006
    Details
    In: AIDS Research and Human Retroviruses, Mary Ann Liebert Inc, Vol. 11, No. 9 ( 1995-09), p. 1003-1006
    Type of Medium: Online Resource
    ISSN: 0889-2229 , 1931-8405
    URL: Article
    DOI: 10.1089/aid.1995.11.1003
    RVK:
    XA 10000
    Language: English
    Publisher: Mary Ann Liebert Inc
    Publication Date: 1995
    detail.hit.zdb_id: 1475767-9
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  • 8
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    Online Resource
    Retroviruses Have Differing Requirements for Proteasome Function in the Budding Process
    American Society for Microbiology ; 2003
    In:  Journal of Virology Vol. 77, No. 6 ( 2003-03-15), p. 3384-3393
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 77, No. 6 ( 2003-03-15), p. 3384-3393
    Abstract: Proteasome inhibitors reduce the budding of human immunodeficiency virus types 1 (HIV-1) and 2, simian immunodeficiency virus, and Rous sarcoma virus. To investigate this effect further, we examined the budding of other retroviruses from proteasome inhibitor-treated cells. The viruses tested differed in their Gag organization, late (L) domain usage, or assembly site from those previously examined. We found that proteasome inhibition decreased the budding of murine leukemia virus (plasma membrane assembly, PPPY L domain) and Mason-Pfizer monkey virus (cytoplasmic assembly, PPPY L domain), similar to the reduction observed for HIV-1. Thus, proteasome inhibitors can affect the budding of a virus that assembles within the cytoplasm. However, the budding of mouse mammary tumor virus (MMTV; cytoplasmic assembly, unknown L domain) was unaffected by proteasome inhibitors, similar to the proteasome-independent budding previously observed for equine infectious anemia virus (plasma membrane assembly, YPDL L domain). Examination of MMTV particles detected Gag-ubiquitin conjugates, demonstrating that an interaction with the ubiquitination system occurs during assembly, as previously found for other retroviruses. For all of the cell lines tested, the inhibitor treatment effectively inactivated proteasomes, as measured by the accumulation of polyubiquitinated proteins. The ubiquitination system was also inhibited, as evidenced by the loss of monoubiquitinated histones from treated cells. These results and those from other viruses show that proteasome inhibitors reduce the budding of viruses that utilize either a PPPY- or PTAP-based L domain and that this effect does not depend on the assembly site or the presence of monoubiquitinated Gag in the virion.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.77.6.3384-3393.2003
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2003
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  • 9
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    Online Resource
    Efficient Incorporation of HLA Class II onto Human Immunodeficiency Virus Type 1 Requires Envelope Glycoprotein Packaging
    American Society for Microbiology ; 2000
    In:  Journal of Virology Vol. 74, No. 8 ( 2000-04-15), p. 3918-3923
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 74, No. 8 ( 2000-04-15), p. 3918-3923
    Abstract: HLA class II DR is one of the most abundant cell surface proteins incorporated onto human immunodeficiency virus type 1 (HIV-1) during budding. The mechanism for HLA class II protein incorporation is not known and may involve a viral protein. To determine whether Env affects HLA class II protein incorporation, HIV-1 virions, either with or without Env on their surface, were produced from HLA class II-expressing cells and analyzed by whole-virus immunoprecipitation with antisera against HLA class II proteins. HLA class II proteins were detected on virions only when wild-type Env was incorporated, while similar experiments showed that HLA class I proteins were incorporated independent of Env packaging. Therefore, the packaging of HIV-1 Env protein is required for the efficient incorporation of HLA class II but not class I proteins into the virion. Analysis of two Env mutants revealed that the presence of a 43-amino-acid sequence between amino acids 708 and 750 in the gp41 TM cytoplasmic tail was required for efficient incorporation of HLA class II proteins. These data show that HIV-1 actively incorporates HLA class II proteins in a process that, either directly or indirectly, requires Env.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.74.8.3918-3923.2000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 2000
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  • 10
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    Online Resource
    Mutational Analysis of the Hydrophobic Tail of the Human Immunodeficiency Virus Type 1 p6 Gag Protein Produces a Mutant That Fails To Package Its Envelope Protein
    American Society for Microbiology ; 1999
    In:  Journal of Virology Vol. 73, No. 1 ( 1999-01), p. 19-28
    Details
    In: Journal of Virology, American Society for Microbiology, Vol. 73, No. 1 ( 1999-01), p. 19-28
    Abstract: The p6 Gag protein of human immunodeficiency virus type 1 (HIV-1) is produced as the carboxyl-terminal sequence within the Gag polyprotein. The amino acid composition of this protein is high in hydrophilic and polar residues except for a patch of relatively hydrophobic amino acids found in the carboxyl-terminal 16 amino acids. Internal cleavage of p6 Gag between Y 36 and P 37 , apparently by the HIV-1 protease, removes this hydrophobic tail region from approximately 30% of the mature p6 Gag proteins in HIV-1 MN . To investigate the importance of this cleavage and the hydrophobic nature of this portion of p6 Gag , site-directed mutations were made at the minor protease cleavage site and within the hydrophobic tail. The results showed that all of the single-amino-acid-replacement mutants exhibited either reduced or undetectable cleavage at the site yet almost all were nearly as infectious as wild-type virus, demonstrating that processing at this site is not important for viral replication. However, one exception, Y36F, was 300-fold as infectious the wild type. In contrast to the single-substitution mutants, a virus with two substitutions in this region of p6 Gag , Y36S-L41P, could not infect susceptible cells. Protein analysis showed that while the processing of the Gag precursor was normal, the double mutant did not incorporate Env into virus particles. This mutant could be complemented with surface glycoproteins from vesicular stomatitis virus and murine leukemia virus, showing that the inability to incorporate Env was the lethal defect for the Y36S-L41P virus. However, this mutant was not rescued by an HIV-1 Env with a truncated gp41 TM cytoplasmic domain, showing that it is phenotypically different from the previously described MA mutants that do not incorporate their full-length Env proteins. Cotransfection experiments with Y36S-L41P and wild-type proviral DNAs revealed that the mutant Gag dominantly blocked the incorporation of Env by wild-type Gag. These results show that the Y36S-L41P p6 Gag mutation dramatically blocks the incorporation of HIV-1 Env, presumably acting late in assembly and early during budding.
    Type of Medium: Online Resource
    ISSN: 0022-538X , 1098-5514
    URL: Article
    DOI: 10.1128/JVI.73.1.19-28.1999
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1999
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