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  1. Article ; Online: The expression and function of HSV ICP47 and its promoter in mice.

    Velusamy, Thilaga / Singh, Navneet / Croft, Sarah / Smith, Stewart / Tscharke, David C

    Journal of virology

    2023  Volume 97, Issue 11, Page(s) e0110723

    Abstract: Importance: Immune evasion and latency are key mechanisms that underlie the success of herpesviruses. In each case, interactions between viral and host proteins are required and due to co-evolution, not all mechanisms are preserved across host species, ... ...

    Abstract Importance: Immune evasion and latency are key mechanisms that underlie the success of herpesviruses. In each case, interactions between viral and host proteins are required and due to co-evolution, not all mechanisms are preserved across host species, even if infection is possible. This is highlighted by the herpes simplex virus (HSV) protein immediate early-infected cell protein (ICP)47, which inhibits the detection of infected cells by killer T cells and acts with high efficiency in humans, but poorly, if at all in mouse cells. Here, we show that ICP47 retains modest but detectable function in mouse cells, but in an
    MeSH term(s) Animals ; Mice ; Herpes Simplex/metabolism ; Immediate-Early Proteins/metabolism ; Immune Evasion ; Promoter Regions, Genetic ; Simplexvirus/genetics ; Simplexvirus/metabolism ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Latency
    Chemical Substances ICP47 protein, Herpes simplex virus ; Immediate-Early Proteins ; Viral Proteins
    Language English
    Publishing date 2023-10-30
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80174-4
    ISSN 1098-5514 ; 0022-538X
    ISSN (online) 1098-5514
    ISSN 0022-538X
    DOI 10.1128/jvi.01107-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 609: 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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  2. Article ; Online: Multi-targeted loss of the antigen presentation molecule MR1 during HSV-1 and HSV-2 infection.

    Samer, Carolyn / McWilliam, Hamish E G / McSharry, Brian P / Velusamy, Thilaga / Burchfield, James G / Stanton, Richard J / Tscharke, David C / Rossjohn, Jamie / Villadangos, Jose A / Abendroth, Allison / Slobedman, Barry

    iScience

    2024  Volume 27, Issue 2, Page(s) 108801

    Abstract: The major histocompatibility complex (MHC), Class-I-related (MR1) molecule presents microbiome-synthesized metabolites to Mucosal-associated invariant T (MAIT) cells, present at sites of herpes simplex virus (HSV) infection. During HSV type 1 (HSV-1) ... ...

    Abstract The major histocompatibility complex (MHC), Class-I-related (MR1) molecule presents microbiome-synthesized metabolites to Mucosal-associated invariant T (MAIT) cells, present at sites of herpes simplex virus (HSV) infection. During HSV type 1 (HSV-1) infection there is a profound and rapid loss of MR1, in part due to expression of unique short 3 protein. Here we show that virion host shutoff RNase protein downregulates MR1 protein, through loss of MR1 transcripts. Furthermore, a third viral protein, infected cell protein 22, also downregulates MR1, but not classical MHC-I molecules. This occurs early in the MR1 trafficking pathway through proteasomal degradation. Finally, HSV-2 infection results in the loss of MR1 transcripts, and intracellular and surface MR1 protein, comparable to that seen during HSV-1 infection. Thus HSV coordinates a multifaceted attack on the MR1 antigen presentation pathway, potentially protecting infected cells from MAIT cell T cell receptor-mediated detection at sites of primary infection and reactivation.
    Language English
    Publishing date 2024-01-04
    Publishing country United States
    Document type Journal Article
    ISSN 2589-0042
    ISSN (online) 2589-0042
    DOI 10.1016/j.isci.2024.108801
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: CRISPR/Cas9-Based Genome Editing of HSV.

    Velusamy, Thilaga / Gowripalan, Anjali / Tscharke, David C

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

    2019  Volume 2060, Page(s) 169–183

    Abstract: The CRISPR/Cas9 gene editing system is a robust and versatile technology that has revolutionized our capacity for genome engineering and is applicable in a wide range of organisms, including large dsDNA viruses. Here we provide an efficient methodology ... ...

    Abstract The CRISPR/Cas9 gene editing system is a robust and versatile technology that has revolutionized our capacity for genome engineering and is applicable in a wide range of organisms, including large dsDNA viruses. Here we provide an efficient methodology that can be used both for marker-based and for marker-free CRISPR/Cas9-mediated editing of the HSV-1 genome. In our method, Cas9, guide RNAs and a homology-directed repair template are provided to cells by cotransection of plasmids, followed by introduction of the HSV genome by infection. This method offers a great deal of flexibility, facilitating editing of the HSV genome that spans the range from individual nucleotide changes to large deletions and insertions.
    MeSH term(s) Animals ; CRISPR-Cas Systems ; Cell Line ; Gene Editing ; Genome, Viral ; Herpesvirus 1, Human/genetics ; Humans
    Language English
    Publishing date 2019-10-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-9814-2_9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Increasing antigen presentation on HSV-1-infected cells increases lesion size but does not alter neural infection or latency.

    Russell, Tiffany A / Velusamy, Thilaga / Tseng, Yeu-Yang / Tscharke, David C

    The Journal of general virology

    2018  Volume 99, Issue 5, Page(s) 682–692

    Abstract: ... ...

    Abstract CD8
    MeSH term(s) Animals ; Antigen Presentation ; CD8-Positive T-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/virology ; Disease Models, Animal ; Female ; Ganglia, Sensory/virology ; Herpes Simplex/immunology ; Herpesvirus 1, Human/genetics ; Herpesvirus 1, Human/immunology ; Histocompatibility Antigens Class I ; Immunodominant Epitopes/genetics ; Mice ; Mice, Inbred BALB C ; Mice, Inbred C57BL ; Skin/immunology ; Skin/pathology ; Skin/virology ; Specific Pathogen-Free Organisms ; Viral Load ; Virus Latency/immunology
    Chemical Substances Histocompatibility Antigens Class I ; Immunodominant Epitopes
    Language English
    Publishing date 2018-04-05
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 219316-4
    ISSN 1465-2099 ; 0022-1317
    ISSN (online) 1465-2099
    ISSN 0022-1317
    DOI 10.1099/jgv.0.001059
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 610: 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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  5. Article: A mutational analysis of the cytosolic domain of the tomato Cf‐9 disease‐resistance protein shows that membrane‐proximal residues are important for Avr9‐dependent necrosis

    Chakrabarti, Apratim / Velusamy, Thilaga / Tee, Choon Yang / Jones, David A

    Molecular plant pathology. 2016 May, v. 17, no. 4

    2016  

    Abstract: The tomato Cf‐9 gene encodes a membrane‐anchored glycoprotein that imparts race‐specific resistance against the tomato leaf mould fungus Cladosporium fulvum in response to the avirulence protein Avr9. Although the N‐terminal half of the extracellular ... ...

    Abstract The tomato Cf‐9 gene encodes a membrane‐anchored glycoprotein that imparts race‐specific resistance against the tomato leaf mould fungus Cladosporium fulvum in response to the avirulence protein Avr9. Although the N‐terminal half of the extracellular leucine‐rich repeat (eLRR) domain of the Cf‐9 protein determines its specificity for Avr9, the C‐terminal half, including its small cytosolic domain, is postulated to be involved in signalling. The cytosolic domain of Cf‐9 carries several residues that are potential sites for ubiquitinylation or phosphorylation, or signals for endocytic uptake. A targeted mutagenesis approach was employed to investigate the roles of these residues and cellular processes in Avr9‐dependent necrosis triggered by Cf‐9. Our results indicate that the membrane‐proximal region of the cytosolic domain of Cf‐9 plays an important role in Cf‐9‐mediated necrosis, and two amino acids within this region, a threonine (T835) and a proline (P838), are particularly important for Cf‐9 function. An alanine mutation of T835 had no effect on Cf‐9 function, but an aspartic acid mutation, which mimics phosphorylation, reduced Cf‐9 function. We therefore postulate that phosphorylation/de‐phosphorylation of T835 could act as a molecular switch to determine whether Cf‐9 is in a primed or inactive state. Yeast two‐hybrid analysis was used to show that the cytosolic domain of Cf‐9 interacts with the cytosolic domain of tomato VAP27. This interaction could be disrupted by an alanine mutation of P838, whereas interaction with CITRX remained unaffected. We therefore postulate that a proline‐induced kink in the membrane‐proximal region of the cytosolic domain of Cf‐9 may be important for interaction with VAP27, which may, in turn, be important for Cf‐9 function.
    Keywords Passalora fulva ; Solanum lycopersicum var. lycopersicum ; alanine ; aspartic acid ; disease resistance ; fungi ; genes ; glycoproteins ; leaves ; necrosis ; phosphorylation ; proline ; site-directed mutagenesis ; threonine ; tomatoes ; two hybrid system techniques
    Language English
    Dates of publication 2016-05
    Size p. 565-576.
    Publishing place Blackwell Science in collaboration with the British Society of Plant Pathology
    Document type Article
    ZDB-ID 2020755-4
    ISSN 1364-3703 ; 1464-6722
    ISSN (online) 1364-3703
    ISSN 1464-6722
    DOI 10.1111/mpp.12315
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: A mutational analysis of the cytosolic domain of the tomato Cf-9 disease-resistance protein shows that membrane-proximal residues are important for Avr9-dependent necrosis.

    Chakrabarti, Apratim / Velusamy, Thilaga / Tee, Choon Yang / Jones, David A

    Molecular plant pathology

    2015  Volume 17, Issue 4, Page(s) 565–576

    Abstract: The tomato Cf-9 gene encodes a membrane-anchored glycoprotein that imparts race-specific resistance against the tomato leaf mould fungus Cladosporium fulvum in response to the avirulence protein Avr9. Although the N-terminal half of the extracellular ... ...

    Abstract The tomato Cf-9 gene encodes a membrane-anchored glycoprotein that imparts race-specific resistance against the tomato leaf mould fungus Cladosporium fulvum in response to the avirulence protein Avr9. Although the N-terminal half of the extracellular leucine-rich repeat (eLRR) domain of the Cf-9 protein determines its specificity for Avr9, the C-terminal half, including its small cytosolic domain, is postulated to be involved in signalling. The cytosolic domain of Cf-9 carries several residues that are potential sites for ubiquitinylation or phosphorylation, or signals for endocytic uptake. A targeted mutagenesis approach was employed to investigate the roles of these residues and cellular processes in Avr9-dependent necrosis triggered by Cf-9. Our results indicate that the membrane-proximal region of the cytosolic domain of Cf-9 plays an important role in Cf-9-mediated necrosis, and two amino acids within this region, a threonine (T835) and a proline (P838), are particularly important for Cf-9 function. An alanine mutation of T835 had no effect on Cf-9 function, but an aspartic acid mutation, which mimics phosphorylation, reduced Cf-9 function. We therefore postulate that phosphorylation/de-phosphorylation of T835 could act as a molecular switch to determine whether Cf-9 is in a primed or inactive state. Yeast two-hybrid analysis was used to show that the cytosolic domain of Cf-9 interacts with the cytosolic domain of tomato VAP27. This interaction could be disrupted by an alanine mutation of P838, whereas interaction with CITRX remained unaffected. We therefore postulate that a proline-induced kink in the membrane-proximal region of the cytosolic domain of Cf-9 may be important for interaction with VAP27, which may, in turn, be important for Cf-9 function.
    MeSH term(s) Amino Acid Motifs ; Amino Acid Sequence ; Amino Acids/metabolism ; Cell Membrane/chemistry ; Cladosporium/physiology ; Cytosol/chemistry ; DNA Mutational Analysis ; Disease Resistance ; Fungal Proteins/metabolism ; Lycopersicon esculentum/metabolism ; Lycopersicon esculentum/microbiology ; Mutation/genetics ; Necrosis ; Plant Diseases/microbiology ; Plant Proteins/chemistry ; Plant Proteins/genetics ; Protein Binding ; Protein Domains ; Sequence Alignment ; Structure-Activity Relationship ; Two-Hybrid System Techniques
    Chemical Substances Amino Acids ; Fungal Proteins ; Plant Proteins ; AVR9 protein, Cladosporium fulvum (138880-27-0)
    Language English
    Publishing date 2015-10-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2020755-4
    ISSN 1364-3703 ; 1464-6722
    ISSN (online) 1364-3703
    ISSN 1464-6722
    DOI 10.1111/mpp.12315
    Database MEDical Literature Analysis and Retrieval System OnLINE

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