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{"title"=>"The murid herpesvirus-4 gL regulates an entry-associated conformation change in gH", "type"=>"journal", "authors"=>[{"first_name"=>"Laurent", "last_name"=>"Gillet", "scopus_author_id"=>"6603465553"}, {"first_name"=>"Susanna", "last_name"=>"Colaco", "scopus_author_id"=>"23967916300"}, {"first_name"=>"Philip G.", "last_name"=>"Stevenson", "scopus_author_id"=>"7102757923"}], "year"=>2007, "source"=>"PLoS ONE", "identifiers"=>{"sgr"=>"50949098291", "pui"=>"352269653", "doi"=>"10.1371/journal.pone.0002811", "pmid"=>"18665235", "scopus"=>"2-s2.0-50949098291", "issn"=>"19326203", "isbn"=>"1932-6203 (Electronic) 1932-6203 (Linking)"}, "id"=>"82d2078b-3a6a-306e-a09d-1c6d3c439be5", "abstract"=>"The glycoprotein H (gH)/gL heterodimer is crucial for herpesvirus membrane fusion. Yet how it functions is not well understood. The Murid Herpesvirus-4 gH, like that of other herpesviruses, adopts its normal virion conformation by associating with gL. However, gH switched back to a gL-independent conformation after virion endocytosis. This switch coincided with a conformation switch in gB and with capsid release. Virions lacking gL constitutively expressed the down-stream form of gH, prematurely switched gB to its down-stream form, and showed premature capsid release with poor infectivity. These data argue that gL plays a key role in regulating a gH and gB functional switch from cell binding to membrane fusion.", "link"=>"http://www.mendeley.com/research/murid-herpesvirus4-gl-regulates-entryassociated-conformation-change-gh", "reader_count"=>12, "reader_count_by_academic_status"=>{"Researcher"=>4, "Student > Ph. D. Student"=>7, "Professor"=>1}, "reader_count_by_user_role"=>{"Researcher"=>4, "Student > Ph. D. Student"=>7, "Professor"=>1}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>7, "Veterinary Science and Veterinary Medicine"=>1, "Immunology and Microbiology"=>3}, "reader_count_by_subdiscipline"=>{"Immunology and Microbiology"=>{"Immunology and Microbiology"=>3}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>7}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>1}}, "group_count"=>0}

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• http://doi.org/10.1371/journal.pone.0030152
• http://doi.org/10.1371/journal.ppat.1004761
• http://doi.org/10.1128/JVI.02123-16
• http://doi.org/10.1128/JVI.00456-12
• http://doi.org/10.1099/vir.0.013300-0
• http://doi.org/10.1016/j.sbi.2009.02.012
• http://doi.org/10.1099/vir.0.040790-0
• http://doi.org/10.1099/vir.0.014266-0
• http://doi.org/10.1128/JVI.06238-11
• http://doi.org/10.1128/JVI.00709-13
• http://doi.org/10.1099/vir.0.008755-0
• http://doi.org/10.1016/j.coviro.2015.07.007
• http://doi.org/10.1371/journal.pone.0083842
• http://doi.org/10.1099/vir.0.023085-0
• http://doi.org/10.1021/bi4008676
• http://doi.org/10.1099/vir.0.005785-0
• http://doi.org/10.1099/vir.0.023481-0
• http://doi.org/10.1099/vir.0.032177-0
• http://doi.org/10.1128/JVI.02942-15

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• 3447751
• 4366105
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• 3353389
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• {"type"=>"COMMENT", "annotationUri"=>"info:doi/10.1371/annotation/51aa3660-c57f-4ce6-b76b-4215689018ce", "title"=>"Corrected Figure 6", "body"=>"Note that the change to this figure makes no difference to the conclusions of the paper. It shows that the findings were similar with different cell types.", "isRemoved"=>false, "created"=>"2008-09-07T15:54:02Z", "lastModified"=>"2008-09-07T15:54:02Z", "creator"=>{"userId"=>"129441"}, "highlightedText"=>"", "competingInterestStatement"=>{"creatorWasPrompted"=>false, "hasCompetingInterests"=>false}, "parentArticle"=>{"doi"=>"info:doi/10.1371/journal.pone.0002811", "state"=>"published", "journals"=>{"PLoSONE"=>{"journalKey"=>"PLoSONE", "eIssn"=>"1932-6203", "title"=>"PLOS ONE"}}}, "replyTreeSize"=>0, "mostRecentActivity"=>"2008-09-07T15:54:02Z", "replies"=>[]}

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Figshare

• {"files"=>["https://ndownloader.figshare.com/files/925884"], "description"=>"1<p>infected mice/total exposed.</p><p>Mice were infected significantly better by wild-type MuHV-4 than by either the gL⁻DEL or gL⁻STOP mutants at 10 p.f.u./mouse (p<0.02 by Fisher's exact test) and 1 p.f.u./mouse (p<0.05). The revertant was not significantly different to wild-type. Comparison between 1 p.f.u. and 10 p.f.u. suggested that the <i>in vivo</i> infectivity of gL knockout virions is about 1/10 that of the wild-type.</p>", "links"=>[], "tags"=>["virology/animal models of infection", "virology/host invasion and cell entry", "virology/immune evasion"], "article_id"=>596333, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.t001", "stats"=>{"downloads"=>2, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Low_dose_in_vivo_infection_by_gL_and_gL_8722_MuHV_4_/596333", "title"=>"Low dose <i>in vivo</i> infection by gL⁺ and gL⁻ MuHV-4.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-21 09:56:03"}
• {"files"=>["https://ndownloader.figshare.com/files/924694"], "description"=>"<p>A. NMuMG cells were exposed to MuHV-4 virions (3 p.f.u./cell, 2 h, 4°C), washed ×3 with PBS and either fixed immediately (4°C) or after a further 2 h incubation at 37°C (37°C). The cells were then stained for gH (MG-9B10), gH/gL (T2C12, 7E5) or gN (3F7) as an invariant control. Glycoprotein staining is green; nuclei are counterstained with DAPI (blue). The data are representative of 5 experiments, and similar results were obtained with 3 other gH-specific/gH/gL-specific mAb pairs. Single cells are shown for optimal resolution. In this as in subsequent figures, each individual cell is fully representative of at least 75% of the total examined (n>100). B. Cells were infected as in A, then stained for LAMP-1 (red) plus either gH (mAb MG-9B10) or gH/gL (mAb 7E5) (green). Co-localization is yellow. The arrow indicates residual gH/gL staining that does not colocalize with LAMP-1.</p>", "links"=>[], "tags"=>["antigenicity"], "article_id"=>595144, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g001", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Glycoprotein_H_changes_its_antigenicity_after_endocytosis_/595144", "title"=>"Glycoprotein H changes its antigenicity after endocytosis.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:49:11"}
• {"files"=>["https://ndownloader.figshare.com/files/925072"], "description"=>"<p>NMuMG cells were exposed to gL⁺ or gL⁻ MuHV-4 virions (3 h, 37°C), then washed ×3 in PBS. Equivalent samples were then either fixed, permeabilized and stained for gN with mAb 3F7 to determine virion uptake by flow cytometry; or incubated for a further 3 h or 15 h, after which viral eGFP expression was assayed by flow cytometry of intact cells. Each point shows the result for 10,000 cells. Equivalent results - the infectivity of gL⁻ viruses was <1% that of gL⁺ viruses for an equivalent level of cell binding - were obtained in a repeat experiment.</p>", "links"=>[], "tags"=>["virions", "post-binding", "nmumg"], "article_id"=>595522, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g003", "stats"=>{"downloads"=>4, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_gL_8722_virions_show_a_post_binding_deficit_in_NMuMG_cell_infection_/595522", "title"=>"gL⁻ virions show a post-binding deficit in NMuMG cell infection.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:51:21"}
• {"files"=>["https://ndownloader.figshare.com/files/925455"], "description"=>"<p>BHK-21 cells were treated as indicated for 2 h, then infected with gL- (gL⁻DEL, gL⁻DEL-STOP) or gL⁺ (wild-type, revertant) MuHV-4 (1 p.f.u./cell). Drug treatment was maintained throughout the course of infection. Infection rates were determined by flow cytometric assay of viral eGFP expression after 18 h. Each point shows the result for 10,000 cells. Equivalent results were obtained in a repeat experiment.</p>", "links"=>[], "tags"=>["muhv-4", "remains", "endocytosis", "lysosomal"], "article_id"=>595901, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g005", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_gL_deficient_MuHV_4_remains_dependent_on_endocytosis_and_lysosomal_acidification_/595901", "title"=>"gL-deficient MuHV-4 remains dependent on endocytosis and lysosomal acidification.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:53:34"}
• {"files"=>["https://ndownloader.figshare.com/files/925911"], "description"=>"1<p>As defined by recognition or not of denatured protein on immunoblots.</p>", "links"=>[], "tags"=>["virology/animal models of infection", "virology/host invasion and cell entry", "virology/immune evasion"], "article_id"=>596363, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.t002", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_MAbs_used_in_this_study_/596363", "title"=>"MAbs used in this study.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-02-21 09:56:12"}
• {"files"=>["https://ndownloader.figshare.com/files/925781"], "description"=>"<p>BHK-21 cells were left uninfected (UI) or infected with gL⁻ (gL⁻STOP, gL⁻DEL) or gL⁺ (wild-type, gL⁻DEL revertant) viruses (2 p.f.u./cell, 18 h). The cells were then trypsinized and stained with secondary antibody only (nil, solid lines) or for gN (mAb 3F7, dotted lines), gH-only (mAb MG-9B10, solid lines), gH/gL (mAb T2C12, dotted lines), the mAb BN-1A7⁺ virion gB conformation (gB vir, dotted lines) or the mAb MG-1A12⁺ pro-fusion gB conformation (gB fus, solid lines). The data are from 1 of 3 equivalent experiments.</p>", "links"=>[], "tags"=>["gb", "conformational", "instability", "muhv-4-infected", "bhk-21"], "article_id"=>596229, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g007", "stats"=>{"downloads"=>0, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_gL_dependent_gB_conformational_instability_in_MuHV_4_infected_BHK_21_cells_/596229", "title"=>"gL-dependent gB conformational instability in MuHV-4-infected BHK-21 cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:55:27"}
• {"files"=>["https://ndownloader.figshare.com/files/924850"], "description"=>"<p>A. MuHV-4 virions were bound to NMuMG cells (2 h, 4°C) with or without bafilomycin (500 nM) or concanamycin A (1 µM). The cells were then washed in PBS to remove unbound virions, further incubated with or without drugs (2 h, 37°C), fixed, permeabilized and stained for gH or gH/gL plus LAMP-1. Nuclei were counterstained with DAPI. B. In a similar experiment, MuHV-4 virions were bound to NMuMG cells (2 h, 4°C) with or without NH₄Cl (100 mM) or chlorpromazine (3 µg/ml). Unbound virus was removed by PBS wash and the cells incubated further (37°C, 2 h), again with or without drug treatment, before fixing, permeabilizing and staining for gH or gH/gL. Although NH₄Cl is generally considered to block endosomal acidification, here it also seemed to block virion endocytosis.</p>", "links"=>[], "tags"=>["conformation"], "article_id"=>595301, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g002", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_gH_gL_conformation_change_is_pH_dependent_/595301", "title"=>"The gH/gL conformation change is pH-dependent.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:50:07"}
• {"files"=>["https://ndownloader.figshare.com/files/925296"], "description"=>"<p>A. NMuMG cells were exposed to wild-type or gL⁻ virions (2 h, 4°C, 3 p.f.u./cell) then washed ×3 in PBS and either fixed immediately (4°C) or first incubated (2 h, 37°C) to allow virion endocytosis (37°C). The cells were then permeabilized and stained for LAMP-1 plus MuHV-4 capsid or glycoprotein antigens as shown. Nuclei were counterstained with DAPI. Colocalization appears as yellow in the merged images. Equivalent data were obtained in 3 further experiments. B. MCCD epithelial cells were incubated with a range of different gL⁻ or gL⁺ viruses (2 h, 4°C, 3 p.f.u./cell), then washed ×3 with PBS and incubated further (2 h, 37°C) to allow virion endocytosis. The cells were then stained for gp150, an abundant virion glycoprotein, with mAb LS-B11 (IgG1) and for ORF65 capsid with mAb MG-12B8 (IgG2a). Nuclei were counterstained with DAPI.</p>", "links"=>[], "tags"=>["virions", "altered", "glycoprotein", "capsid", "distributions", "gb", "conformation"], "article_id"=>595743, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g004", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_gL_8722_virions_show_altered_glycoprotein_and_capsid_distributions_and_gB_conformation_changes_/595743", "title"=>"gL⁻ virions show altered glycoprotein and capsid distributions and gB conformation changes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:52:38"}
• {"files"=>["https://ndownloader.figshare.com/files/925610"], "description"=>"<p>gL⁺ and gL⁻ virions were bound to adherent NIH-3T3 cells (2 h, 4°C). Unbound virions were then removed by PBS wash. The cells were then either fixed (4°C) or first incubated (2 h, 37°C) to allow virion endocytosis and then fixed (37°C). All cells were then permeabilized and stained for MuHV-4 virion components (green) and LAMP-1 (red) as shown. Nuclei were counter-stained with DAPI (blue). In the absence of gL, both capsids and glycoproteins remained peripheral. gB conformation changes were also affected. Notably, MG-1A12⁺ gB appeared in peripheral, LAMP-1⁻ endosomes. Representative cells are shown.</p>", "links"=>[], "tags"=>["virions", "abnormal", "nih-3t3"], "article_id"=>596063, "categories"=>["Medicine", "Infectious Diseases"], "users"=>["Laurent Gillet", "Susanna Colaco", "Philip G. Stevenson"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0002811.g006", "stats"=>{"downloads"=>3, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_gL_deficient_virions_show_abnormal_entry_in_NIH_3T3_fibroblasts_/596063", "title"=>"gL-deficient virions show abnormal entry in NIH-3T3 fibroblasts.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-02-21 09:54:28"}

PMC Usage Stats | Further Information

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Relative Metric

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F1000Prime