Adhesion of Trypanosoma cruzi Trypomastigotes to Fibronectin or Laminin Modifies Tubulin and Paraflagellar Rod Protein Phosphorylation
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{"title"=>"Adhesion of Trypanosoma cruzi Trypomastigotes to Fibronectin or Laminin Modifies Tubulin and Paraflagellar Rod Protein Phosphorylation", "type"=>"journal", "authors"=>[{"first_name"=>"Eliciane C.", "last_name"=>"Mattos", "scopus_author_id"=>"14014487800"}, {"first_name"=>"Robert I.", "last_name"=>"Schumacher", "scopus_author_id"=>"57197569707"}, {"first_name"=>"Walter", "last_name"=>"Colli", "scopus_author_id"=>"7005133721"}, {"first_name"=>"Maria Julia M.", "last_name"=>"Alves", "scopus_author_id"=>"35592777500"}], "year"=>2012, "source"=>"PLoS ONE", "identifiers"=>{"scopus"=>"2-s2.0-84867121286", "pmid"=>"23056443", "sgr"=>"84867121286", "doi"=>"10.1371/journal.pone.0046767", "issn"=>"19326203", "pui"=>"365784439"}, "id"=>"7200658a-df99-3c03-bfa3-cea70f49b537", "abstract"=>"BACKGROUND: The unicellular parasite Trypanosoma cruzi is the causative agent of Chagaś disease in humans. Adherence of the infective stage to elements of the extracellular matrix (ECM), as laminin and fibronectin, is an essential step in host cell invasion. Although members of the gp85/TS, as Tc85, were identified as laminin and fibronectin ligands, the signaling events triggered on the parasite upon binding to these molecules are largely unexplored.\\n\\nMETHODOLOGY/PRINCIPAL FINDINGS: Viable infective parasites were incubated with laminin, fibronectin or bovine serum albumin for different periods of time and the proteins were separated by bidimensional gels. The phosphoproteins were envisaged by specific staining and the spots showing phosphorylation levels significantly different from the control were excised and identified by MS/MS. The results of interest were confirmed by immunoblotting or immunoprecipitation and the localization of proteins in the parasite was determined by immunofluorescence. Using a host cell-free system, our data indicate that the phosphorylation contents of T. cruzi proteins encompassing different cellular functions are modified upon incubation of the parasite with fibronectin or laminin.\\n\\nCONCLUSIONS/SIGNIFICANCE: Herein it is shown, for the first time, that paraflagellar rod proteins and α-tubulin, major structural elements of the parasite cytoskeleton, are predominantly dephosphorylated during the process, probably involving the ERK1/2 pathway. It is well established that T. cruzi binds to ECM elements during the cell infection process. The fact that laminin and fibronectin induce predominantly dephosphorylation of the main cytoskeletal proteins of the parasite suggests a possible correlation between cytoskeletal modifications and the ability of the parasite to internalize into host cells.", "link"=>"http://www.mendeley.com/research/adhesion-trypanosoma-cruzi-trypomastigotes-fibronectin-laminin-modifies-tubulin-paraflagellar-rod-pr", "reader_count"=>22, "reader_count_by_academic_status"=>{"Unspecified"=>2, "Student > Doctoral Student"=>5, "Researcher"=>1, "Student > Ph. D. Student"=>6, "Student > Master"=>5, "Student > Bachelor"=>2, "Professor"=>1}, "reader_count_by_user_role"=>{"Unspecified"=>2, "Student > Doctoral Student"=>5, "Researcher"=>1, "Student > Ph. D. Student"=>6, "Student > Master"=>5, "Student > Bachelor"=>2, "Professor"=>1}, "reader_count_by_subject_area"=>{"Unspecified"=>2, "Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>15, "Medicine and Dentistry"=>1, "Physics and Astronomy"=>1, "Chemistry"=>2}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>1}, "Chemistry"=>{"Chemistry"=>2}, "Physics and Astronomy"=>{"Physics and Astronomy"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>15}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Unspecified"=>{"Unspecified"=>2}}, "group_count"=>1}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/564282"], "description"=>"<p>(<b>A</b>) Representative immunoblotting of immunoprecipitated α-tubulin phosphorylated (p-α-tubulin) during the times indicated. (<b>B</b>) Quantitation of 3 independent experiments as described in (<b>A</b>); asterisk represents a comparison between the 5 min and 120 min points by the Student's t-test with p<0.001, indicating a progressive α-tubulin dephosphorylation. (<b>C</b>) Representative immunoblotting of phosphorylated (pS, pT, pY, top) and total (bottom) soluble (S) and insoluble (INS) immunoprecipitated α-tubulin from trypomastigotes incubated for 2h with BSA, laminin (L) or fibronectin (F). (<b>D</b>) Calculation of the phosphorylation ratio relative to BSA from the experiments in (<b>C</b>); ratio: relative intensity of phosphorylated-tubulin treatment/control (BSA); on the left, 49.1 corresponds to the molecular mass standard in kDa.</p>", "links"=>[], "tags"=>["adhesion", "trypomastigotes", "fibronectin"], "article_id"=>234779, "categories"=>["Biotechnology", "Biochemistry", "Cell Biology", "Microbiology", "Immunology"], "users"=>["Eliciane C. Mattos", "Robert I. Schumacher", "Walter Colli", "Maria Julia M. Alves"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0046767.g003", "stats"=>{"downloads"=>0, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phosphorylation_status_of_945_tubulin_upon_adhesion_of_trypomastigotes_to_laminin_fibronectin_or_BSA_/234779", "title"=>"Phosphorylation status of α-tubulin upon adhesion of trypomastigotes to laminin, fibronectin or BSA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-04 01:19:39"}
  • {"files"=>["https://ndownloader.figshare.com/files/564176"], "description"=>"<p>Incubation was for 2 h: (<b>A</b>) Phosphorylated proteins were stained with Pro-Q Diamond. (<b>B</b>) total protein profile developed with colloidal Coomassie blue staining; molecular mass markers (kDa) are shown on the ordinates; spots with variation in phosphorylation status are circled in red. (<b>C</b>) profile of phosphorylated and dephosphorylated spots upon 2 h incubation. (<b>D</b>) functional distribution of proteins from C.</p>", "links"=>[], "tags"=>["proteins", "modified", "adhesion", "laminin"], "article_id"=>234665, "categories"=>["Biotechnology", "Biochemistry", "Cell Biology", "Microbiology", "Immunology"], "users"=>["Eliciane C. Mattos", "Robert I. Schumacher", "Walter Colli", "Maria Julia M. Alves"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0046767.g002", "stats"=>{"downloads"=>0, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Trypomastigote_proteins_modified_by_phosphorylation_dephosphorylation_upon_adhesion_to_laminin_or_fibronectin_/234665", "title"=>"Trypomastigote proteins modified by phosphorylation/dephosphorylation upon adhesion to laminin or fibronectin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-04 01:17:45"}
  • {"files"=>["https://ndownloader.figshare.com/files/564344"], "description"=>"<p>(<b>A</b>) Representative immunoblotting of phosphorylated (pS, pT, pY) and PAR proteins immunoprecipitated during the incubation time. (<b>B</b>) Quantitation of 3 independent experiments as described in (<b>A</b>); asterisk represents a comparison between the 5 min and 120 min points by the Student's t-test with p<0.05, indicating a progressive PAR dephosphorylation. (<b>C</b>) Representative immunoblotting of phosphorylated (pS, pT, pY, top) and total (bottom) soluble (S) and insoluble (INS) immunoprecipitated PAR proteins from trypomastigotes incubated for 2 h with BSA, laminin (L) or fibronectin (F). (<b>D</b>) Calculation of the phosphorylation ratio relative to BSA from the experiments in (<b>C</b>); ratio: relative intensity of phosphorylated-PAR treatment/control (BSA); on the left, 80 corresponds to the molecular mass standard in kDa.</p>", "links"=>[], "tags"=>["par", "proteins", "incubation", "trypomastigotes", "fibronectin"], "article_id"=>234837, "categories"=>["Biotechnology", "Biochemistry", "Cell Biology", "Microbiology", "Immunology"], "users"=>["Eliciane C. Mattos", "Robert I. Schumacher", "Walter Colli", "Maria Julia M. Alves"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0046767.g004", "stats"=>{"downloads"=>3, "page_views"=>5, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phosphorylation_status_of_PAR_proteins_upon_incubation_of_trypomastigotes_to_laminin_fibronectin_or_BSA_/234837", "title"=>"Phosphorylation status of PAR proteins upon incubation of trypomastigotes to laminin, fibronectin or BSA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-04 01:20:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/563984"], "description"=>"<p>Incubation was for 2 h: (<b>A</b>) Localization of phosphoproteins is shown by the reactivity with anti-pS, -pT, -pY antibodies (red); nucleus and kinetoplast stained with DAPI (blue) and DIC images were also shown; white bars represent 3.2 µm. (<b>B</b>) Quantitation of parasite modifications (arrows) due to treatment with fibronectin and laminin, respectively, as compared to BSA treatment is shown; 6 fields with approximately 40 parasites each have been examined; asterisks represent a p<0.001 when experimental points were compared with the control by the Student's t-test.</p>", "links"=>[], "tags"=>["trypomastigotes", "incubated", "laminin"], "article_id"=>234474, "categories"=>["Biotechnology", "Biochemistry", "Cell Biology", "Microbiology", "Immunology"], "users"=>["Eliciane C. Mattos", "Robert I. Schumacher", "Walter Colli", "Maria Julia M. Alves"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0046767.g001", "stats"=>{"downloads"=>1, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phenotype_of_T_cruzi_trypomastigotes_incubated_with_fibronectin_laminin_or_BSA_/234474", "title"=>"Phenotype of <i>T. cruzi</i> trypomastigotes incubated with fibronectin, laminin or BSA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-04 01:14:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/299546", "https://ndownloader.figshare.com/files/299621"], "description"=>"<div><h3>Background</h3><p>The unicellular parasite <em>Trypanosoma cruzi</em> is the causative agent of Chagaś disease in humans. Adherence of the infective stage to elements of the extracellular matrix (ECM), as laminin and fibronectin, is an essential step in host cell invasion. Although members of the gp85/TS, as Tc85, were identified as laminin and fibronectin ligands, the signaling events triggered on the parasite upon binding to these molecules are largely unexplored.</p> <h3>Methodology/Principal Findings</h3><p>Viable infective parasites were incubated with laminin, fibronectin or bovine serum albumin for different periods of time and the proteins were separated by bidimensional gels. The phosphoproteins were envisaged by specific staining and the spots showing phosphorylation levels significantly different from the control were excised and identified by MS/MS. The results of interest were confirmed by immunoblotting or immunoprecipitation and the localization of proteins in the parasite was determined by immunofluorescence. Using a host cell-free system, our data indicate that the phosphorylation contents of <em>T. cruzi</em> proteins encompassing different cellular functions are modified upon incubation of the parasite with fibronectin or laminin.</p> <h3>Conclusions/Significance</h3><p>Herein it is shown, for the first time, that paraflagellar rod proteins and α-tubulin, major structural elements of the parasite cytoskeleton, are predominantly dephosphorylated during the process, probably involving the ERK1/2 pathway. It is well established that <em>T. cruzi</em> binds to ECM elements during the cell infection process. The fact that laminin and fibronectin induce predominantly dephosphorylation of the main cytoskeletal proteins of the parasite suggests a possible correlation between cytoskeletal modifications and the ability of the parasite to internalize into host cells.</p> </div>", "links"=>[], "tags"=>["adhesion", "trypomastigotes", "fibronectin", "laminin", "modifies", "tubulin", "paraflagellar", "phosphorylation"], "article_id"=>119062, "categories"=>["Biotechnology", "Biochemistry", "Cell Biology", "Microbiology", "Immunology"], "users"=>["Eliciane C. Mattos", "Robert I. Schumacher", "Walter Colli", "Maria Julia M. Alves"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0046767.s001", "https://dx.doi.org/10.1371/journal.pone.0046767.s002"], "stats"=>{"downloads"=>4, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/Adhesion_of_Trypanosoma_cruzi_Trypomastigotes_to_Fibronectin_or_Laminin_Modifies_Tubulin_and_Paraflagellar_Rod_Protein_Phosphorylation/119062", "title"=>"Adhesion of <em>Trypanosoma cruzi</em> Trypomastigotes to Fibronectin or Laminin Modifies Tubulin and Paraflagellar Rod Protein Phosphorylation", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2012-10-04 02:31:02"}
  • {"files"=>["https://ndownloader.figshare.com/files/564418"], "description"=>"<p>(<b>A</b>) Representative immunoblotting of phosphorylated ERK 1/2 (p-ERK 1/2) or GAPDH protein during the times indicated. (<b>B</b>) Calculation of the ERK 1/2 phosphorylation ratio for each experimental point relative to BSA from 2 experiments as in (<b>A</b>); on the left, 49.1 and 34.8 correspond to molecular mass standards in kDa. Asterisks represent a comparison between the 5 min and 120 min points by the Student's t-test with p<0.05 for fibronectin and p<0.2 for laminin.</p>", "links"=>[], "tags"=>["trypomastigotes", "incubated", "fibronectin"], "article_id"=>234913, "categories"=>["Biotechnology", "Biochemistry", "Cell Biology", "Microbiology", "Immunology"], "users"=>["Eliciane C. Mattos", "Robert I. Schumacher", "Walter Colli", "Maria Julia M. Alves"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0046767.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phosphorylation_status_of_ERK1_2_8197_in_trypomastigotes_incubated_with_laminin_fibronectin_or_BSA_/234913", "title"=>"Phosphorylation status of ERK1/2 in trypomastigotes incubated with laminin, fibronectin or BSA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2012-10-04 01:21:53"}

PMC Usage Stats | Further Information

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Relative Metric

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