VapD in Xylella fastidiosa Is a Thermostable Protein with Ribonuclease Activity
Publication Date
December 22, 2015
Journal
PLOS ONE
Authors
Juliano S. Mendes, André Da S. Santiago, Marcelo A. S. Toledo, Luciana K. Rosselli Murai, et al
Volume
10
Issue
12
Pages
e0145765
DOI
https://dx.plos.org/10.1371/journal.pone.0145765
Publisher URL
http://journals.plos.org/plosone/article?id=10.1371%2Fjournal.pone.0145765
PubMed
http://www.ncbi.nlm.nih.gov/pubmed/26694028
PubMed Central
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687846
Europe PMC
http://europepmc.org/abstract/MED/26694028
Web of Science
000367092500074
Scopus
84970925794
Mendeley
http://www.mendeley.com/research/vapd-xylella-fastidiosa-thermostable-protein-ribonuclease-activity
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Mendeley | Further Information

{"title"=>"VapD in Xylella fastidiosa is a thermostable protein with ribonuclease activity", "type"=>"journal", "authors"=>[{"first_name"=>"Juliano S.", "last_name"=>"Mendes", "scopus_author_id"=>"54998634900"}, {"first_name"=>"André S.", "last_name"=>"Da Santiago", "scopus_author_id"=>"57189438912"}, {"first_name"=>"Marcelo A.S.", "last_name"=>"Toledo", "scopus_author_id"=>"35742166700"}, {"first_name"=>"Luciana K.", "last_name"=>"Rosselli-Murai", "scopus_author_id"=>"35741543100"}, {"first_name"=>"Marianna T.P.", "last_name"=>"Favaro", "scopus_author_id"=>"37037191100"}, {"first_name"=>"Clelton A.", "last_name"=>"Santos", "scopus_author_id"=>"12753224600"}, {"first_name"=>"Maria Augusta C.", "last_name"=>"Horta", "scopus_author_id"=>"55915590900"}, {"first_name"=>"Aline", "last_name"=>"Crucello", "scopus_author_id"=>"54998020900"}, {"first_name"=>"Lilian L.", "last_name"=>"Beloti", "scopus_author_id"=>"54998020800"}, {"first_name"=>"Fabian", "last_name"=>"Romero", "scopus_author_id"=>"56070841600"}, {"first_name"=>"Ljubica", "last_name"=>"Tasic", "scopus_author_id"=>"6701542482"}, {"first_name"=>"Alessandra A.", "last_name"=>"De Souza", "scopus_author_id"=>"35416079500"}, {"first_name"=>"Anete P.", "last_name"=>"De Souza", "scopus_author_id"=>"7101828170"}], "year"=>2015, "source"=>"PLoS ONE", "identifiers"=>{"issn"=>"19326203", "pmid"=>"26694028", "pui"=>"608045060", "scopus"=>"2-s2.0-84970925794", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "doi"=>"10.1371/journal.pone.0145765", "sgr"=>"84970925794"}, "id"=>"db7c2efe-7c93-3ae0-afaf-eefd003521ec", "abstract"=>"Xylella fastidiosa strain 9a5c is a gram-negative phytopathogen that is the causal agent of citrus variegated chlorosis (CVC), a disease that is responsible for economic losses in Brazilian agriculture. The most well-known mechanism of pathogenicity for this bacterial pathogen is xylem vessel occlusion, which results from bacterial movement and the formation of biofilms. The molecular mechanisms underlying the virulence caused by biofilm formation are unknown. Here, we provide evidence showing that virulence-associated protein D in X. fastidiosa (Xf-VapD) is a thermostable protein with ribonuclease activity. Moreover, protein expression analyses in two X. fastidiosa strains, including virulent (Xf9a5c) and nonpathogenic (XfJ1a12) strains, showed that Xf-VapD was expressed during all phases of development in both strains and that increased expression was observed in Xf9a5c during biofilm growth. This study is an important step toward characterizing and improving our understanding of the biological significance of Xf-VapD and its potential functions in the CVC pathosystem.", "link"=>"http://www.mendeley.com/research/vapd-xylella-fastidiosa-thermostable-protein-ribonuclease-activity", "reader_count"=>12, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Librarian"=>1, "Researcher"=>3, "Student > Doctoral Student"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>4}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Librarian"=>1, "Researcher"=>3, "Student > Doctoral Student"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>4}, "reader_count_by_subject_area"=>{"Unspecified"=>3, "Biochemistry, Genetics and Molecular Biology"=>1, "Agricultural and Biological Sciences"=>7, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>7}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>1}, "Unspecified"=>{"Unspecified"=>3}}, "reader_count_by_country"=>{"Germany"=>1}, "group_count"=>0}

Scopus | Further Information

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/2614618"], "description"=>"<p>(A) The prediction of the 3D structure of Xf-VapD was performed using Phyre V 2.0 (red cartoon). A model was obtained with 66% of the Xf-VapD sequence and 100% confidence using the single highest scoring template. The structure was edited using PyMol. On the right, the amino acid sequence is shown with the respective secondary structure and confidence. The amino acid residues highlighted in red correspond to the area in the red cartoon shown in the 3D structure. (B) The neighbor-joining consensus tree inferred for the amino acid sequences of VapD. The values above the branches indicate the Bayesian posterior probabilities for the amino acids (PPaa) and nucleotides (PPnt). The values below the branches indicate the results of the neighbor-joining method for the amino acids (BSaa) and nucleotides (BSnt) following 1,000 bootstrap replicates. The minus symbol (‒) indicates that no support was reached for this node. The groups are the same as those in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0145765#pone.0145765.g001\" target=\"_blank\">Fig 1</a>.</p>", "links"=>[], "tags"=>["biofilm", "protein expression analyses", "cvc", "mechanism", "Xf 9a", "formation", "xylem vessel occlusion", "Ribonuclease Activity Xylella fastidiosa strain 9", "XfJ 1a strains"], "article_id"=>1628848, "categories"=>["Biological Sciences"], "users"=>["Juliano S. Mendes", "André da S. Santiago", "Marcelo A. S. Toledo", "Luciana K. Rosselli-Murai", "Marianna T. P. Favaro", "Clelton A. Santos", "Maria Augusta C. Horta", "Aline Crucello", "Lilian L. Beloti", "Fabian Romero", "Ljubica Tasic", "Alessandra A. de Souza", "Anete P. de Souza"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0145765.g002", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_and_phylogenetic_analysis_of_Xf_VapD_/1628848", "title"=>"Structural and phylogenetic analysis of Xf-VapD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2016-01-05 14:52:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/2614621"], "description"=>"<p>A chromatogram showing the two steps used in the purification of Xf-VapD: Xf-VapD fused with a trx-tag was obtained first, and then trypsin cleavage was used to remove the trx-tag. On the right, a 12.5% SDS-PAGE is shown for the Xf-VapD purification process. The lanes are as follows: M, protein marker; 1, Xf-VapD fused to trx-tag (31 kDa); 2, Xf-VapD and trx-tag after cleavage with trypsin; 3, totally purified Xf-VapD (16.5 kDa); and 4, trx-tag (~13 kDa). The gel was stained using Coomassie brilliant blue.</p>", "links"=>[], "tags"=>["biofilm", "protein expression analyses", "cvc", "mechanism", "Xf 9a", "formation", "xylem vessel occlusion", "Ribonuclease Activity Xylella fastidiosa strain 9", "XfJ 1a strains"], "article_id"=>1628851, "categories"=>["Biological Sciences"], "users"=>["Juliano S. Mendes", "André da S. Santiago", "Marcelo A. S. Toledo", "Luciana K. Rosselli-Murai", "Marianna T. P. Favaro", "Clelton A. Santos", "Maria Augusta C. Horta", "Aline Crucello", "Lilian L. Beloti", "Fabian Romero", "Ljubica Tasic", "Alessandra A. de Souza", "Anete P. de Souza"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0145765.g003", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Purification_of_recombinant_Xf_VapD_/1628851", "title"=>"Purification of recombinant Xf-VapD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2016-01-05 14:52:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/2614622"], "description"=>"<p>(A) Circular dichroism spectrum (200 nm–260 nm) of the recombinant purified Xf-VapD. The secondary structure of the protein was found to be 69% α-helices, 19% β-sheets, and 12% random coils. (B) Thermal unfolding/refolding of Xf-VapD. At 83°C during the heating phase, 50% of the proteins were unfolded (red marker). The conformational structure of the protein was not restored during the cooling phase.</p>", "links"=>[], "tags"=>["biofilm", "protein expression analyses", "cvc", "mechanism", "Xf 9a", "formation", "xylem vessel occlusion", "Ribonuclease Activity Xylella fastidiosa strain 9", "XfJ 1a strains"], "article_id"=>1628852, "categories"=>["Biological Sciences"], "users"=>["Juliano S. Mendes", "André da S. Santiago", "Marcelo A. S. Toledo", "Luciana K. Rosselli-Murai", "Marianna T. P. Favaro", "Clelton A. Santos", "Maria Augusta C. Horta", "Aline Crucello", "Lilian L. Beloti", "Fabian Romero", "Ljubica Tasic", "Alessandra A. de Souza", "Anete P. de Souza"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0145765.g004", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Secondary_structure_and_thermo_stability_assay_of_Xf_VapD_/1628852", "title"=>"Secondary structure and thermo stability assay of Xf-VapD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2016-01-05 14:52:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/2614623"], "description"=>"<p>(A) The lanes contain one positive control, two negative controls, and the Xf-VapD samples that were treated at 37°C and 90°C. The values are shown in RFU/time units. The curves show that Xf-VapD demonstrated ribonuclease activity at both 37°C, and after heating to 90°C. (B) Lane 1 contains RNA alone, and lanes 2 to 5 contain RNA with Xf-VapD (1 μM, 5 μM, 10 μM and 20 μM, respectively). (C) Lane 1 contains dsDNA (2 kb) alone, and lanes 2 to 3 contain dsDNA (2 kb) with Xf-VapD (20 μM and 50 μM, respectively). (D) Lane 1 contains dsDNA (20 bp) alone, and lanes 2 to 3 contain dsDNA (20 bp) with Xf-VapD (20 μM and 50 μM, respectively). (E) Lane 1 contains ssDNA (26 nt) alone, and lane 2 contains ssDNA (26 nt) with Xf-VapD (50 μM).</p>", "links"=>[], "tags"=>["biofilm", "protein expression analyses", "cvc", "mechanism", "Xf 9a", "formation", "xylem vessel occlusion", "Ribonuclease Activity Xylella fastidiosa strain 9", "XfJ 1a strains"], "article_id"=>1628853, "categories"=>["Biological Sciences"], "users"=>["Juliano S. Mendes", "André da S. Santiago", "Marcelo A. S. Toledo", "Luciana K. Rosselli-Murai", "Marianna T. P. Favaro", "Clelton A. Santos", "Maria Augusta C. Horta", "Aline Crucello", "Lilian L. Beloti", "Fabian Romero", "Ljubica Tasic", "Alessandra A. de Souza", "Anete P. de Souza"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0145765.g005", "stats"=>{"downloads"=>0, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Enzymatic_activity_assay_of_Xf_VapD_/1628853", "title"=>"Enzymatic activity assay of Xf-VapD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2016-01-05 14:52:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/2614628"], "description"=>"<p>(A) Strain 9a5c in planktonic and biofilm growth. (B) Strain J1a12 in planktonic growth. The band values were obtained using ImageJ software. The values above the bars indicate the average of three biological replicates. The error bars indicate the standard errors of the means. The asterisk (*) indicates a significant difference compared to the days of growth indicated in the brackets (Student’s <i>t</i>-test, <i>p</i><0.05).</p>", "links"=>[], "tags"=>["biofilm", "protein expression analyses", "cvc", "mechanism", "Xf 9a", "formation", "xylem vessel occlusion", "Ribonuclease Activity Xylella fastidiosa strain 9", "XfJ 1a strains"], "article_id"=>1628855, "categories"=>["Biological Sciences"], "users"=>["Juliano S. Mendes", "André da S. Santiago", "Marcelo A. S. Toledo", "Luciana K. Rosselli-Murai", "Marianna T. P. Favaro", "Clelton A. Santos", "Maria Augusta C. Horta", "Aline Crucello", "Lilian L. Beloti", "Fabian Romero", "Ljubica Tasic", "Alessandra A. de Souza", "Anete P. de Souza"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0145765.g006", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Western_blot_analyses_of_Xf_VapD_expression_in_X_fastidiosa_cells_/1628855", "title"=>"Western blot analyses of Xf-VapD expression in <i>X</i>. <i>fastidiosa</i> cells.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2016-01-05 14:52:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/2614616"], "description"=>"<p>Group 1: The <i>X</i>. <i>fastidiosa</i> strains 9a5c and Ann-1 (Xf9a5c and XfAnn-1, respectively), <i>G</i>. <i>anatis</i> (Ga), <i>A</i>. <i>actinomycetemcomitans</i> (Aa), and <i>N</i>. <i>meningitides</i> (Nm). Group 2: <i>E</i>. <i>coli</i> (Ec), <i>X</i>. <i>campestris</i> (Xc), and <i>H</i>. <i>influenza</i> (Hi). Group 3: <i>H</i>. <i>pylori</i> (Hp) and <i>R</i>. <i>equi</i> (Re). The identity values for Xf-VapD are shown in parentheses at the end of each sequence.</p>", "links"=>[], "tags"=>["biofilm", "protein expression analyses", "cvc", "mechanism", "Xf 9a", "formation", "xylem vessel occlusion", "Ribonuclease Activity Xylella fastidiosa strain 9", "XfJ 1a strains"], "article_id"=>1628846, "categories"=>["Biological Sciences"], "users"=>["Juliano S. Mendes", "André da S. Santiago", "Marcelo A. S. Toledo", "Luciana K. Rosselli-Murai", "Marianna T. P. Favaro", "Clelton A. Santos", "Maria Augusta C. Horta", "Aline Crucello", "Lilian L. Beloti", "Fabian Romero", "Ljubica Tasic", "Alessandra A. de Souza", "Anete P. de Souza"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0145765.g001", "stats"=>{"downloads"=>1, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Multiple_sequence_alignments_to_VapD_proteins_/1628846", "title"=>"Multiple sequence alignments to VapD proteins.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2016-01-05 14:52:32"}

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Relative Metric

{"start_date"=>"2015-01-01T00:00:00Z", "end_date"=>"2015-12-31T00:00:00Z", "subject_areas"=>[]}
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