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  1. Article ; Online: Efficient HIV-1 in vitro reverse transcription: optimal capsid stability is required.

    Burdick, Ryan C / Pathak, Vinay K

    Signal transduction and targeted therapy

    2021  Volume 6, Issue 1, Page(s) 13

    MeSH term(s) Capsid ; Capsid Proteins/genetics ; HIV-1/genetics ; Reverse Transcription ; Virus Uncoating
    Chemical Substances Capsid Proteins
    Language English
    Publishing date 2021-01-12
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 2886872-9
    ISSN 2059-3635 ; 2095-9907
    ISSN (online) 2059-3635
    ISSN 2095-9907
    DOI 10.1038/s41392-020-00458-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: HIV-1 uncoating requires long double-stranded reverse transcription products.

    Burdick, Ryan C / Morse, Michael / Rouzina, Ioulia / Williams, Mark C / Hu, Wei-Shau / Pathak, Vinay K

    Science advances

    2024  Volume 10, Issue 17, Page(s) eadn7033

    Abstract: HIV-1 cores, which contain the viral genome and replication machinery, must disassemble (uncoat) during viral replication. However, the viral and host factors that trigger uncoating remain unidentified. Recent studies show that infectious cores enter the ...

    Abstract HIV-1 cores, which contain the viral genome and replication machinery, must disassemble (uncoat) during viral replication. However, the viral and host factors that trigger uncoating remain unidentified. Recent studies show that infectious cores enter the nucleus and uncoat near the site of integration. Here, we show that efficient uncoating of nuclear cores requires synthesis of a double-stranded DNA (dsDNA) genome >3.5 kb and that the efficiency of uncoating correlates with genome size. Core disruption by capsid inhibitors releases viral DNA, some of which integrates. However, most of the viral DNA is degraded, indicating that the intact core safeguards viral DNA. Atomic force microscopy and core content estimation reveal that synthesis of full-length genomic dsDNA induces substantial internal strain on the core to promote uncoating. We conclude that HIV-1 cores protect viral DNA from degradation by host factors and that synthesis of long double-stranded reverse transcription products is required to trigger efficient HIV-1 uncoating.
    MeSH term(s) HIV-1/physiology ; HIV-1/drug effects ; HIV-1/genetics ; Virus Uncoating ; Humans ; DNA, Viral/genetics ; DNA, Viral/metabolism ; Reverse Transcription ; Virus Replication/drug effects ; Genome, Viral ; Microscopy, Atomic Force ; Capsid/metabolism
    Chemical Substances DNA, Viral
    Language English
    Publishing date 2024-04-24
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.adn7033
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Intranuclear Positions of HIV-1 Proviruses Are Dynamic and Do Not Correlate with Transcriptional Activity.

    Burdick, Ryan C / Deleage, Claire / Duchon, Alice / Estes, Jacob D / Hu, Wei-Shau / Pathak, Vinay K

    mBio

    2022  Volume 13, Issue 1, Page(s) e0325621

    Abstract: The relationship between spatiotemporal distribution of HIV-1 proviruses and their transcriptional activity is not well understood. To elucidate the intranuclear positions of transcriptionally active HIV-1 proviruses, we utilized an RNA ... ...

    Abstract The relationship between spatiotemporal distribution of HIV-1 proviruses and their transcriptional activity is not well understood. To elucidate the intranuclear positions of transcriptionally active HIV-1 proviruses, we utilized an RNA fluorescence
    MeSH term(s) Humans ; Proviruses/genetics ; HIV-1/genetics ; HeLa Cells ; Virus Integration ; In Situ Hybridization, Fluorescence ; HIV Infections ; HIV Seropositivity ; RNA/metabolism
    Chemical Substances RNA (63231-63-0)
    Language English
    Publishing date 2022-01-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, N.I.H., Extramural
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.03256-21
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Potent dual block to HIV-1 infection using lentiviral vectors expressing fusion inhibitor peptide mC46- and Vif-resistant APOBEC3G.

    Delviks-Frankenberry, Krista A / Ojha, Chet R / Hermann, Kip J / Hu, Wei-Shau / Torbett, Bruce E / Pathak, Vinay K

    Molecular therapy. Nucleic acids

    2023  Volume 33, Page(s) 794–809

    Abstract: Gene therapy strategies that effectively inhibit HIV-1 replication are needed to reduce the requirement for lifelong antiviral therapy and potentially achieve a functional cure. We previously designed self-activating lentiviral vectors that efficiently ... ...

    Abstract Gene therapy strategies that effectively inhibit HIV-1 replication are needed to reduce the requirement for lifelong antiviral therapy and potentially achieve a functional cure. We previously designed self-activating lentiviral vectors that efficiently delivered and expressed a Vif-resistant mutant of APOBEC3G (A3G-D128K) to T cells, which potently inhibited HIV-1 replication and spread with no detectable virus. Here, we developed vectors that express A3G-D128K, membrane-associated fusion inhibitor peptide mC46, and O
    Language English
    Publishing date 2023-08-11
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2662631-7
    ISSN 2162-2531
    ISSN 2162-2531
    DOI 10.1016/j.omtn.2023.08.007
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Structural Insights into APOBEC3-Mediated Lentiviral Restriction.

    Delviks-Frankenberry, Krista A / Desimmie, Belete A / Pathak, Vinay K

    Viruses

    2020  Volume 12, Issue 6

    Abstract: Mammals have developed clever adaptive and innate immune defense mechanisms to protect against invading bacterial and viral pathogens. Human innate immunity is continuously evolving to expand the repertoire of restriction factors and one such family of ... ...

    Abstract Mammals have developed clever adaptive and innate immune defense mechanisms to protect against invading bacterial and viral pathogens. Human innate immunity is continuously evolving to expand the repertoire of restriction factors and one such family of intrinsic restriction factors is the APOBEC3 (A3) family of cytidine deaminases. The coordinated expression of seven members of the A3 family of cytidine deaminases provides intrinsic immunity against numerous foreign infectious agents and protects the host from exogenous retroviruses and endogenous retroelements. Four members of the A3 proteins-A3G, A3F, A3H, and A3D-restrict HIV-1 in the absence of virion infectivity factor (Vif); their incorporation into progeny virions is a prerequisite for cytidine deaminase-dependent and -independent activities that inhibit viral replication in the host target cell. HIV-1 encodes Vif, an accessory protein that antagonizes A3 proteins by targeting them for polyubiquitination and subsequent proteasomal degradation in the virus producing cells. In this review, we summarize our current understanding of the role of human A3 proteins as barriers against HIV-1 infection, how Vif overcomes their antiviral activity, and highlight recent structural and functional insights into A3-mediated restriction of lentiviruses.
    MeSH term(s) APOBEC Deaminases/chemistry ; APOBEC Deaminases/physiology ; Animals ; Base Sequence ; Humans ; Lentivirus/immunology ; Lentivirus/metabolism ; Lentivirus Infections/immunology ; Lentivirus Infections/metabolism ; Protein Structure, Tertiary ; Structure-Activity Relationship
    Chemical Substances APOBEC Deaminases (EC 3.5.4.5) ; APOBEC3 proteins, human (EC 3.5.4.5)
    Language English
    Publishing date 2020-05-27
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12060587
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Development of a Cell-Based Luciferase Complementation Assay for Identification of SARS-CoV-2 3CL

    Rawson, Jonathan M O / Duchon, Alice / Nikolaitchik, Olga A / Pathak, Vinay K / Hu, Wei-Shau

    Viruses

    2021  Volume 13, Issue 2

    Abstract: The 3C-like protease ( ... ...

    Abstract The 3C-like protease (3CL
    MeSH term(s) Antiviral Agents/metabolism ; Antiviral Agents/pharmacology ; Cell Survival/drug effects ; Coronavirus 3C Proteases/antagonists & inhibitors ; Coronavirus 3C Proteases/genetics ; Coronavirus 3C Proteases/metabolism ; Drug Evaluation, Preclinical ; HEK293 Cells ; Humans ; Lentivirus/genetics ; Luciferases/genetics ; Luciferases/metabolism ; Protease Inhibitors/metabolism ; Protease Inhibitors/pharmacology ; SARS-CoV-2/enzymology
    Chemical Substances Antiviral Agents ; Protease Inhibitors ; Luciferases (EC 1.13.12.-) ; 3C-like proteinase, SARS-CoV-2 (EC 3.4.22.-) ; Coronavirus 3C Proteases (EC 3.4.22.28)
    Language English
    Publishing date 2021-01-24
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 2516098-9
    ISSN 1999-4915 ; 1999-4915
    ISSN (online) 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v13020173
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: HIV-1 cores retain their integrity until minutes before uncoating in the nucleus.

    Li, Chenglei / Burdick, Ryan C / Nagashima, Kunio / Hu, Wei-Shau / Pathak, Vinay K

    Proceedings of the National Academy of Sciences of the United States of America

    2021  Volume 118, Issue 10

    Abstract: We recently reported that HIV-1 cores that retained >94% of their capsid (CA) protein entered the nucleus and disassembled (uncoated) near their integration site <1.5 h before integration. However, whether the nuclear capsids lost their integrity by ... ...

    Abstract We recently reported that HIV-1 cores that retained >94% of their capsid (CA) protein entered the nucleus and disassembled (uncoated) near their integration site <1.5 h before integration. However, whether the nuclear capsids lost their integrity by rupturing or a small loss of CA before capsid disassembly was unclear. Here, we utilized a previously reported vector in which green fluorescent protein is inserted in HIV-1 Gag (iGFP); proteolytic processing efficiently releases GFP, some of which remains trapped inside capsids and serves as a fluid phase content marker that is released when the capsids lose their integrity. We found that nuclear capsids retained their integrity until shortly before integration and lost their GFP content marker ∼1 to 3 min before loss of capsid-associated mRuby-tagged cleavage and polyadenylation specificity factor 6 (mRuby-CPSF6). In contrast, loss of GFP fused to CA and mRuby-CPSF6 occurred simultaneously, indicating that viral cores retain their integrity until just minutes before uncoating. Our results indicate that HIV-1 evolved to retain its capsid integrity and maintain a separation between macromolecules in the viral core and the nuclear environment until uncoating occurs just before integration. These observations imply that intact HIV-1 capsids are imported through nuclear pores; that reverse transcription occurs in an intact capsid; and that interactions between the preintegration complex and LEDGF/p75, and possibly other host factors that facilitate integration, must occur during the short time period between loss of capsid integrity and integration.
    MeSH term(s) Cell Line ; HIV-1/genetics ; HIV-1/metabolism ; Humans ; Nucleocapsid/genetics ; Nucleocapsid/metabolism ; Virus Internalization ; gag Gene Products, Human Immunodeficiency Virus/genetics ; gag Gene Products, Human Immunodeficiency Virus/metabolism
    Chemical Substances gag Gene Products, Human Immunodeficiency Virus
    Language English
    Publishing date 2021-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2019467118
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1148: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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  8. Article ; Online: Transcription Start Site Heterogeneity and Preferential Packaging of Specific Full-Length RNA Species Are Conserved Features of Primate Lentiviruses.

    Rawson, Jonathan M O / Nikolaitchik, Olga A / Shakya, Saurabh / Keele, Brandon F / Pathak, Vinay K / Hu, Wei-Shau

    Microbiology spectrum

    2022  Volume 10, Issue 4, Page(s) e0105322

    Abstract: HIV-1 must package its RNA genome to generate infectious viruses. Recent studies have revealed that during genome packaging, HIV-1 not only excludes cellular mRNAs, but also distinguishes among full-length viral RNAs. Using NL4-3 and MAL molecular clones, ...

    Abstract HIV-1 must package its RNA genome to generate infectious viruses. Recent studies have revealed that during genome packaging, HIV-1 not only excludes cellular mRNAs, but also distinguishes among full-length viral RNAs. Using NL4-3 and MAL molecular clones, multiple transcription start sites (TSS) were identified, which generate full-length RNAs that differ by only a few nucleotides at the 5' end. However, HIV-1 selectively packages RNAs containing one guanosine (1G RNA) over RNAs with three guanosines (3G RNA) at the 5' end. Thus, the 5' context of HIV-1 full-length RNA can affect its function. To determine whether the regulation of genome packaging by TSS usage is unique to NL4-3 and MAL, we examined 15 primate lentiviruses including transmitted founder viruses of HIV-1, HIV-2, and several simian immunodeficiency viruses (SIVs). We found that all 15 viruses used multiple TSS to some extent. However, the level of TSS heterogeneity in infected cells varied greatly, even among closely related viruses belonging to the same subtype. Most viruses also exhibited selective packaging of specific full-length viral RNA species into particles. These findings demonstrate that TSS heterogeneity and selective packaging of certain full-length viral RNA species are conserved features of primate lentiviruses. In addition, an SIV strain closely related to the progenitor virus that gave rise to HIV-1 group M, the pandemic pathogen, exhibited TSS usage similar to some HIV-1 strains and preferentially packaged 1G RNA. These findings indicate that multiple TSS usage and selective packaging of a particular unspliced RNA species predate the emergence of HIV-1.
    MeSH term(s) Animals ; HIV-1/genetics ; Lentiviruses, Primate/genetics ; RNA, Viral/genetics ; Transcription Initiation Site ; Virion/genetics
    Chemical Substances RNA, Viral
    Language English
    Publishing date 2022-06-23
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural
    ZDB-ID 2807133-5
    ISSN 2165-0497 ; 2165-0497
    ISSN (online) 2165-0497
    ISSN 2165-0497
    DOI 10.1128/spectrum.01053-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Structural Insights into APOBEC3-Mediated Lentiviral Restriction

    Delviks-Frankenberry, Krista A / Desimmie, Belete A / Pathak, Vinay K

    Viruses. 2020 May 27, v. 12, no. 6

    2020  

    Abstract: Mammals have developed clever adaptive and innate immune defense mechanisms to protect against invading bacterial and viral pathogens. Human innate immunity is continuously evolving to expand the repertoire of restriction factors and one such family of ... ...

    Abstract Mammals have developed clever adaptive and innate immune defense mechanisms to protect against invading bacterial and viral pathogens. Human innate immunity is continuously evolving to expand the repertoire of restriction factors and one such family of intrinsic restriction factors is the APOBEC3 (A3) family of cytidine deaminases. The coordinated expression of seven members of the A3 family of cytidine deaminases provides intrinsic immunity against numerous foreign infectious agents and protects the host from exogenous retroviruses and endogenous retroelements. Four members of the A3 proteins—A3G, A3F, A3H, and A3D—restrict HIV-1 in the absence of virion infectivity factor (Vif); their incorporation into progeny virions is a prerequisite for cytidine deaminase-dependent and -independent activities that inhibit viral replication in the host target cell. HIV-1 encodes Vif, an accessory protein that antagonizes A3 proteins by targeting them for polyubiquitination and subsequent proteasomal degradation in the virus producing cells. In this review, we summarize our current understanding of the role of human A3 proteins as barriers against HIV-1 infection, how Vif overcomes their antiviral activity, and highlight recent structural and functional insights into A3-mediated restriction of lentiviruses.
    Keywords HIV infections ; Human immunodeficiency virus 1 ; antiviral properties ; cytidine ; cytidine deaminase ; defense mechanisms ; humans ; innate immunity ; pathogenicity ; pathogens ; progeny ; proteins ; retrotransposons ; ubiquitination ; virion ; virus replication ; viruses
    Language English
    Dates of publication 2020-0527
    Publishing place Multidisciplinary Digital Publishing Institute
    Document type Article
    ZDB-ID 2516098-9
    ISSN 1999-4915
    ISSN 1999-4915
    DOI 10.3390/v12060587
    Database NAL-Catalogue (AGRICOLA)

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  10. Article ; Online: Authors' reply.

    Singh, Itu / Ahuja, Madhvi / Lavania, Mallika / Pathak, Vinay K / Turankar, Ravindra P / Singh, Vikram / Sengupta, Utpal / Das, Loretta / Kumar, Archana / Saini, Geeta B

    Indian journal of dermatology, venereology and leprology

    2023  Volume 89, Issue 6, Page(s) 872–873

    Language English
    Publishing date 2023-11-07
    Publishing country United States
    Document type Journal Article
    ZDB-ID 416068-x
    ISSN 0973-3922 ; 0019-5162 ; 0378-6323
    ISSN (online) 0973-3922
    ISSN 0019-5162 ; 0378-6323
    DOI 10.25259/IJDVL_1056_2023
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 85: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (1.OG)
    ab Jg. 2022: Lesesaal (EG)

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