Cancer Associated Aberrant Protein O-Glycosylation Can Modify Antigen Processing and Immune Response
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{"title"=>"Cancer Associated Aberrant Protein O-Glycosylation Can Modify Antigen Processing and Immune Response", "type"=>"journal", "authors"=>[{"first_name"=>"Caroline B.", "last_name"=>"Madsen", "scopus_author_id"=>"55327417700"}, {"first_name"=>"Cecilie", "last_name"=>"Petersen", "scopus_author_id"=>"57198055008"}, {"first_name"=>"Kirstine", "last_name"=>"Lavrsen", "scopus_author_id"=>"55326897300"}, {"first_name"=>"Mikkel", "last_name"=>"Harndahl", "scopus_author_id"=>"14028174700"}, {"first_name"=>"Søren", "last_name"=>"Buus", "scopus_author_id"=>"55625990000"}, {"first_name"=>"Henrik", "last_name"=>"Clausen", "scopus_author_id"=>"35496835400"}, {"first_name"=>"Anders E.", "last_name"=>"Pedersen", "scopus_author_id"=>"7202801558"}, {"first_name"=>"Hans H.", "last_name"=>"Wandall", "scopus_author_id"=>"6603953096"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84870044166", "sgr"=>"84870044166", "issn"=>"19326203", "doi"=>"10.1371/journal.pone.0050139", "pmid"=>"23189185", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "pui"=>"366134099"}, "id"=>"952a8359-533c-3a37-ae0d-6e9eeb3836ad", "abstract"=>"Aberrant glycosylation of mucins and other extracellular proteins is an important event in carcinogenesis and the resulting cancer associated glycans have been suggested as targets in cancer immunotherapy. We assessed the role of O-linked GalNAc glycosylation on antigen uptake, processing, and presentation on MHC class I and II molecules. The effect of GalNAc O-glycosylation was monitored with a model system based on ovalbumin (OVA)-MUC1 fusion peptides (+/- glycosylation) loaded onto dendritic cells co-cultured with IL-2 secreting OVA peptide-specific T cell hybridomas. To evaluate the in vivo response to a cancer related tumor antigen, Balb/c or B6.Cg(CB)-Tg(HLA-A/H2-D)2Enge/J (HLA-A2 transgenic) mice were immunized with a non-glycosylated or GalNAc-glycosylated MUC1 derived peptide followed by comparison of T cell proliferation, IFN-γ release, and antibody induction. GalNAc-glycosylation promoted presentation of OVA-MUC1 fusion peptides by MHC class II molecules and the MUC1 antigen elicited specific Ab production and T cell proliferation in both Balb/c and HLA-A2 transgenic mice. In contrast, GalNAc-glycosylation inhibited the presentation of OVA-MUC1 fusion peptides by MHC class I and abolished MUC1 specific CD8+ T cell responses in HLA-A2 transgenic mice. GalNAc glycosylation of MUC1 antigen therefore facilitates uptake, MHC class II presentation, and antibody response but might block the antigen presentation to CD8+ T cells.", "link"=>"http://www.mendeley.com/research/cancer-associated-aberrant-protein-oglycosylation-modify-antigen-processing-immune-response", "reader_count"=>34, "reader_count_by_academic_status"=>{"Unspecified"=>1, "Professor > Associate Professor"=>4, "Researcher"=>8, "Student > Ph. D. Student"=>4, "Student > Master"=>8, "Other"=>2, "Student > Bachelor"=>4, "Professor"=>3}, "reader_count_by_user_role"=>{"Unspecified"=>1, "Professor > Associate Professor"=>4, "Researcher"=>8, "Student > Ph. D. Student"=>4, "Student > Master"=>8, "Other"=>2, "Student > Bachelor"=>4, "Professor"=>3}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Biochemistry, Genetics and Molecular Biology"=>3, "Medicine and Dentistry"=>5, "Agricultural and Biological Sciences"=>21, "Chemistry"=>1, "Computer Science"=>1, "Immunology and Microbiology"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>5}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>2}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>21}, "Computer Science"=>{"Computer Science"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}}, "reader_count_by_country"=>{"Turkey"=>1, "Uruguay"=>1}, "group_count"=>1}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/287856", "https://ndownloader.figshare.com/files/287907"], "description"=>"<div><p>Aberrant glycosylation of mucins and other extracellular proteins is an important event in carcinogenesis and the resulting cancer associated glycans have been suggested as targets in cancer immunotherapy. We assessed the role of O-linked GalNAc glycosylation on antigen uptake, processing, and presentation on MHC class I and II molecules. The effect of GalNAc O-glycosylation was monitored with a model system based on ovalbumin (OVA)-MUC1 fusion peptides (+/− glycosylation) loaded onto dendritic cells co-cultured with IL-2 secreting OVA peptide-specific T cell hybridomas. To evaluate the <em>in vivo</em> response to a cancer related tumor antigen, Balb/c or B6.Cg(CB)-Tg(HLA-A/H2-D)2Enge/J (HLA-A2 transgenic) mice were immunized with a non-glycosylated or GalNAc-glycosylated MUC1 derived peptide followed by comparison of T cell proliferation, IFN-γ release, and antibody induction. GalNAc-glycosylation promoted presentation of OVA-MUC1 fusion peptides by MHC class II molecules and the MUC1 antigen elicited specific Ab production and T cell proliferation in both Balb/c and HLA-A2 transgenic mice. In contrast, GalNAc-glycosylation inhibited the presentation of OVA-MUC1 fusion peptides by MHC class I and abolished MUC1 specific CD8+ T cell responses in HLA-A2 transgenic mice. GalNAc glycosylation of MUC1 antigen therefore facilitates uptake, MHC class II presentation, and antibody response but might block the antigen presentation to CD8+ T cells.</p> </div>", "links"=>[], "tags"=>["cancer", "aberrant", "o-glycosylation", "antigen", "response"], "article_id"=>116711, "categories"=>["Cancer", "Biochemistry", "Immunology"], "users"=>["Caroline B. Madsen", "Cecilie Petersen", "Kirstine Lavrsen", "Mikkel Harndahl", "Søren Buus", "Henrik Clausen", "Anders E. Pedersen", "Hans H. Wandall"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0050139.s001", "https://dx.doi.org/10.1371/journal.pone.0050139.s002"], "stats"=>{"downloads"=>7, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Cancer_Associated_Aberrant_Protein_O_Glycosylation_Can_Modify_Antigen_Processing_and_Immune_Response__/116711", "title"=>"Cancer Associated Aberrant Protein O-Glycosylation Can Modify Antigen Processing and Immune Response", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-11-26 01:51:51"}
  • {"files"=>["https://ndownloader.figshare.com/files/537605"], "description"=>"<p>A) O-glycan synthesis overview. B) IL-2 production from OVA specific CD4+ T cell hybridoma (BO.97.10) co-cultured with bone marrow derived DCs pulsed with two peptide variants with and without 2 and 4 glycan residues (GalNAc). Full length OVA used as a positive control. Individually cultured T cells and DCs had an OD value equal to the background.</p>", "links"=>[], "tags"=>["glycosylation", "enhances", "activation", "antigen"], "article_id"=>208093, "categories"=>["Cancer", "Biochemistry", "Immunology"], "users"=>["Caroline B. Madsen", "Cecilie Petersen", "Kirstine Lavrsen", "Mikkel Harndahl", "Søren Buus", "Henrik Clausen", "Anders E. Pedersen", "Hans H. Wandall"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050139.g001", "stats"=>{"downloads"=>1, "page_views"=>28, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_glycosylation_enhances_the_activation_of_antigen_specific_CD4_T_cell_hybridoma_/208093", "title"=>"Peptide glycosylation enhances the activation of antigen specific CD4+ T cell hybridoma.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-26 02:14:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/538028"], "description"=>"<p>A) DC uptake of uncoated fluorescent beads, MUC1-fluorescent beads, or GalNAc MUC1 fluorescent beads. DCs without beads were used as reference. B) The uptake of MUC2 fusion peptide +/−GalNAc was evaluated by flow cytometry after 48 hrs of peptide pulsing. Unstained DCs (purple filled) and DCs with no peptide load (green) were used as a background control. C) Evaluation of the surface expression by flow cytometry of SIINFEKL in the H2kb peptide binding groove. DCs were pulsed with the MUC2 fusion peptide (highest concentration from D) with GalNAc (green line) and without GalNAc (purple filled) 48 hrs before the staining. D) IL-2 production from SIINFEKL specific CD8+ T cell hybridoma (RF 33.70) co-cultured with bone marrow derived DCs pulsed <i>in vitro</i> for two days with MUC2 fusion peptide both with and without glycosylation in a concentration gradient. Full length OVA was used as a positive control. Representative data of at least two independent experiments is shown. E, F) Confocal imaging of DC internalized GalNAc MUC2 fusion (E, green) and MUC2 fusion (F, green) co-stained with endosomal marker EEA-1 (red) and lysosomal marker LAMP-2 (red).</p>", "links"=>[], "tags"=>["peptide", "glycosylation", "increases", "uptake", "inhibits", "activation", "antigen"], "article_id"=>208511, "categories"=>["Cancer", "Biochemistry", "Immunology"], "users"=>["Caroline B. Madsen", "Cecilie Petersen", "Kirstine Lavrsen", "Mikkel Harndahl", "Søren Buus", "Henrik Clausen", "Anders E. Pedersen", "Hans H. Wandall"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050139.g004", "stats"=>{"downloads"=>4, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Increased_density_of_peptide_glycosylation_increases_uptake_but_inhibits_activation_of_antigen_specific_CD8_T_cell_hybridoma_/208511", "title"=>"Increased density of peptide glycosylation increases uptake but inhibits activation of antigen specific CD8+ T cell hybridoma.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-26 02:21:51"}
  • {"files"=>["https://ndownloader.figshare.com/files/537866"], "description"=>"<p>A) Serum reactivity to different mucin glycoforms from Balb/c mice immunized with degMUC1+/− GalNAc by ELISA. Data are representative of a minimum of 4 Balb/c mice immunized with each antigen. (B) T cell proliferation from mice Balb/c mice or (C) HLA-A2 mice immunized with GalNAc degMUC1 (white bars) and non-glycosylated degMUC1 (grey bars) for each peptide used for <i>in vitro</i> re-stimulation (100 ug/ml) as indicated on the x-axis. D) Lymphocytes from immunized HLA-A2 mice pulsed with the 9 mer degMUC1 peptide, ALGSTAPPV, with and without glycosylation. DegMUC1 specific CD8+ T cells were selected based on anti-CD8 Ab (x-axis) and anti-IFNγ Ab (y-axis) after 4 hrs of Golgi stop treatment. E) Spleen cells after 24 days of re-stimulation with the non-glycosylated ALGSTAPPV peptide. All T cell data is generated from spleen or lymph nodes from at least 4 mice, but in most cases 6 mice.</p>", "links"=>[], "tags"=>["degmuc1", "wt", "hla-a2", "transgenic"], "article_id"=>208351, "categories"=>["Cancer", "Biochemistry", "Immunology"], "users"=>["Caroline B. Madsen", "Cecilie Petersen", "Kirstine Lavrsen", "Mikkel Harndahl", "Søren Buus", "Henrik Clausen", "Anders E. Pedersen", "Hans H. Wandall"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050139.g003", "stats"=>{"downloads"=>1, "page_views"=>15, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_In_vivo_response_to_degMUC1_in_WT_Balb_c_and_HLA_A2_transgenic_mice_/208351", "title"=>"<i>In vivo</i> response to degMUC1 in WT Balb/c and HLA-A2 transgenic mice.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-26 02:19:11"}
  • {"files"=>["https://ndownloader.figshare.com/files/537707"], "description"=>"<p>IL-2 production from OVA specific CD8+ T cell hybridoma (RF 33.70) co-cultured with bone marrow derived DCs (A) or CD11c+ DCs purified from mouse spleen (B). DCs were pulsed with two peptide variants with and without 2 and 4 glycan residues (GalNAc). Full length OVA was used as a positive control. Individually cultured T cells and DCs had an OD value equal to the background. C, D) Surface expression by flow cytometry of SIINFEKL in the H2kb peptide binding groove on DCs after pulsing with the two peptide variants (non-glycosylated peptide (thin purple dashed line), peptide with 2 GalNAcs (thick green line), or 4 GalNAcs (pink line)). E) Surface expression of SIINFEKL in the H2kb peptide binding groove on DCs without pulsing (blue line) and after pulsing with OVA control (purple line). Gray histograms represent cells stained only with secondary antibody.</p>", "links"=>[], "tags"=>["glycosylation", "inhibits", "activation", "antigen"], "article_id"=>208193, "categories"=>["Cancer", "Biochemistry", "Immunology"], "users"=>["Caroline B. Madsen", "Cecilie Petersen", "Kirstine Lavrsen", "Mikkel Harndahl", "Søren Buus", "Henrik Clausen", "Anders E. Pedersen", "Hans H. Wandall"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050139.g002", "stats"=>{"downloads"=>3, "page_views"=>21, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_glycosylation_inhibits_activation_of_antigen_specific_CD8_T_cell_hybridoma_/208193", "title"=>"Peptide glycosylation inhibits activation of antigen specific CD8+ T cell hybridoma.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-11-26 02:16:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/538153"], "description"=>"<p>1 and 2 (H2-Kb restricted fusion), 3 and 4 (I-Ab restricted fusion). Underlining indicate sites of glycosylation. Internal (I), terminal (T), N-Acetylgalactosamine (GalNAc).</p>", "links"=>[], "tags"=>["sequences", "dc", "hybridoma"], "article_id"=>208639, "categories"=>["Cancer", "Biochemistry", "Immunology"], "users"=>["Caroline B. Madsen", "Cecilie Petersen", "Kirstine Lavrsen", "Mikkel Harndahl", "Søren Buus", "Henrik Clausen", "Anders E. Pedersen", "Hans H. Wandall"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0050139.t001", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Peptide_sequences_for_DC_T_cell_hybridoma_co_culture_/208639", "title"=>"Peptide sequences for DC T cell hybridoma co-culture.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2012-11-26 02:23:59"}

PMC Usage Stats | Further Information

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Relative Metric

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