Leptospira interrogans Endostatin-Like Outer Membrane Proteins Bind Host Fibronectin, Laminin and Regulators of Complement
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{"title"=>"Leptospira interrogans endostatin-like outer membrane proteins bind host fibronectin, laminin and regulators of complement", "type"=>"journal", "authors"=>[{"first_name"=>"Brian", "last_name"=>"Stevenson", "scopus_author_id"=>"7103399193"}, {"first_name"=>"Henry A.", "last_name"=>"Choy", "scopus_author_id"=>"7006232592"}, {"first_name"=>"Marija", "last_name"=>"Pinne", "scopus_author_id"=>"8079831100"}, {"first_name"=>"Matthew L.", "last_name"=>"Rotondi", "scopus_author_id"=>"24173805500"}, {"first_name"=>"M. Clarke", "last_name"=>"Miller", "scopus_author_id"=>"35618993500"}, {"first_name"=>"Edward", "last_name"=>"DeMoll", "scopus_author_id"=>"6603337079"}, {"first_name"=>"Peter", "last_name"=>"Kraiczy", "scopus_author_id"=>"6701585923"}, {"first_name"=>"Anne E.", "last_name"=>"Cooley", "scopus_author_id"=>"15724540200"}, {"first_name"=>"Trevor P.", "last_name"=>"Creamer", "scopus_author_id"=>"7003634547"}, {"first_name"=>"Marc A.", "last_name"=>"Suchard", "scopus_author_id"=>"6603887291"}, {"first_name"=>"Catherine A.", "last_name"=>"Brissette", "scopus_author_id"=>"21233613200"}, {"first_name"=>"Ashutosh", "last_name"=>"Verma", "scopus_author_id"=>"23111822000"}, {"first_name"=>"David A.", "last_name"=>"Haake", "scopus_author_id"=>"7006383677"}], "year"=>2007, "source"=>"PLoS ONE", "identifiers"=>{"pmid"=>"18000555", "sgr"=>"43149110212", "doi"=>"10.1371/journal.pone.0001188", "scopus"=>"2-s2.0-43149110212", "pui"=>"351638064", "isbn"=>"1932-6203 (Electronic)\\r1932-6203 (Linking)", "issn"=>"19326203"}, "id"=>"836f02a4-36e8-3da4-bf0c-3956c6d52a42", "abstract"=>"The pathogenic spirochete Leptospira interrogans disseminates throughout its hosts via the bloodstream, then invades and colonizes a variety of host tissues. Infectious leptospires are resistant to killing by their hosts' alternative pathway of complement-mediated killing, and interact with various host extracellular matrix (ECM) components. The LenA outer surface protein (formerly called LfhA and Lsa24) was previously shown to bind the host ECM component laminin and the complement regulators factor H and factor H-related protein-1. We now demonstrate that infectious L. interrogans contain five additional paralogs of lenA, which we designated lenB, lenC, lenD, lenE and lenF. All six genes encode domains predicted to bear structural and functional similarities with mammalian endostatins. Sequence analyses of genes from seven infectious L. interrogans serovars indicated development of sequence diversity through recombination and intragenic duplication. LenB was found to bind human factor H, and all of the newly-described Len proteins bound laminin. In addition, LenB, LenC, LenD, LenE and LenF all exhibited affinities for fibronectin, a distinct host extracellular matrix protein. These characteristics suggest that Len proteins together facilitate invasion and colonization of host tissues, and protect against host immune responses during mammalian infection.", "link"=>"http://www.mendeley.com/research/leptospira-interrogans-endostatinlike-outer-membrane-proteins-bind-host-fibronectin-laminin-regulato", "reader_count"=>65, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>7, "Researcher"=>13, "Student > Doctoral Student"=>6, "Student > Ph. D. Student"=>12, "Student > Postgraduate"=>4, "Student > Master"=>7, "Other"=>2, "Student > Bachelor"=>7, "Lecturer"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>5}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>7, "Researcher"=>13, "Student > Doctoral Student"=>6, "Student > Ph. D. Student"=>12, "Student > Postgraduate"=>4, "Student > Master"=>7, "Other"=>2, "Student > Bachelor"=>7, "Lecturer"=>1, "Lecturer > Senior Lecturer"=>1, "Professor"=>5}, "reader_count_by_subject_area"=>{"Unspecified"=>1, "Environmental Science"=>2, "Biochemistry, Genetics and Molecular Biology"=>3, "Nursing and Health Professions"=>1, "Agricultural and Biological Sciences"=>34, "Medicine and Dentistry"=>7, "Veterinary Science and Veterinary Medicine"=>9, "Chemistry"=>2, "Social Sciences"=>1, "Immunology and Microbiology"=>5}, "reader_count_by_subdiscipline"=>{"Medicine and Dentistry"=>{"Medicine and Dentistry"=>7}, "Chemistry"=>{"Chemistry"=>2}, "Social Sciences"=>{"Social Sciences"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>5}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>34}, "Nursing and Health Professions"=>{"Nursing and Health Professions"=>1}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>3}, "Unspecified"=>{"Unspecified"=>1}, "Environmental Science"=>{"Environmental Science"=>2}, "Veterinary Science and Veterinary Medicine"=>{"Veterinary Science and Veterinary Medicine"=>9}}, "reader_count_by_country"=>{"Reunion"=>1, "United States"=>2, "Sri Lanka"=>1, "Egypt"=>1, "Brazil"=>6, "Spain"=>1}, "group_count"=>2}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/942865"], "description"=>"<p>Oligonucleotide primers used to amplify and clone <i>len</i> loci.</p>", "links"=>[], "tags"=>["primers", "clone"], "article_id"=>613253, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.t002", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Oligonucleotide_primers_used_to_amplify_and_clone_len_loci_/613253", "title"=>"Oligonucleotide primers used to amplify and clone <i>len</i> loci.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2007-11-14 00:54:13"}
  • {"files"=>["https://ndownloader.figshare.com/files/465762", "https://ndownloader.figshare.com/files/465958"], "description"=>"<div><p>The pathogenic spirochete <em>Leptospira interrogans</em> disseminates throughout its hosts via the bloodstream, then invades and colonizes a variety of host tissues. Infectious leptospires are resistant to killing by their hosts' alternative pathway of complement-mediated killing, and interact with various host extracellular matrix (ECM) components. The LenA outer surface protein (formerly called LfhA and Lsa24) was previously shown to bind the host ECM component laminin and the complement regulators factor H and factor H-related protein-1. We now demonstrate that infectious <em>L. interrogans</em> contain five additional paralogs of <em>lenA</em>, which we designated <em>lenB, lenC, lenD, lenE</em> and <em>lenF</em>. All six genes encode domains predicted to bear structural and functional similarities with mammalian endostatins. Sequence analyses of genes from seven infectious <em>L. interrogans</em> serovars indicated development of sequence diversity through recombination and intragenic duplication. LenB was found to bind human factor H, and all of the newly-described Len proteins bound laminin. In addition, LenB, LenC, LenD, LenE and LenF all exhibited affinities for fibronectin, a distinct host extracellular matrix protein. These characteristics suggest that Len proteins together facilitate invasion and colonization of host tissues, and protect against host immune responses during mammalian infection.</p></div>", "links"=>[], "tags"=>["endostatin-like", "membrane", "proteins", "laminin", "regulators", "complement"], "article_id"=>151817, "categories"=>["Cancer", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>["https://dx.doi.org/10.1371/journal.pone.0001188.s001", "https://dx.doi.org/10.1371/journal.pone.0001188.s002"], "stats"=>{"downloads"=>3, "page_views"=>28, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Leptospira_interrogans_Endostatin_Like_Outer_Membrane_Proteins_Bind_Host_Fibronectin_Laminin_and_Regulators_of_Complement/151817", "title"=>"<em>Leptospira interrogans</em> Endostatin-Like Outer Membrane Proteins Bind Host Fibronectin, Laminin and Regulators of Complement", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2007-11-14 00:30:17"}
  • {"files"=>["https://ndownloader.figshare.com/files/942598"], "description"=>"<p>Soluble recombinant LenA and LenB were each examined for binding to 1 µg immobilized laminin. (A) Saturable laminin binding by LenB compared to the weaker binding by LenA. Average of two independent experiments (bars equal 1 standard deviation), as representative of additional assays performed with different preparations of Len proteins. Significant differences (P<0.05) between LenA and LenB are indicated by asterisks The mean K<sub>d</sub> for LenB binding is 118 +/− 39 nM (n = 4). (B) Laminin binding by LenA and LenB is dependent on ionic strength. (C) Heparin competes with LenA and LenB for laminin binding. The activity of 1 µM LenA was measured with heparin added to the binding buffer. The higher avidity of LenB was challenged by preincubation of laminin with heparin prior to adding 0.25 µM LenB plus varying concentrations of heparin.</p>", "links"=>[], "tags"=>["lena", "lenb", "binding"], "article_id"=>613003, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g006", "stats"=>{"downloads"=>3, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ELISA_results_of_LenA_and_LenB_binding_to_laminin_/613003", "title"=>"ELISA results of LenA and LenB binding to laminin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:50:03"}
  • {"files"=>["https://ndownloader.figshare.com/files/942459"], "description"=>"<p>Carbonic anhydrase, soybean trypsin inhibitor and lysozyme were loaded onto the same lane and served as both negative controls and molecular mass standards. Positions of those standards are indicated to the left of the panel (in kDa).</p>", "links"=>[], "tags"=>["binds", "ligand", "affinity", "blot", "recombinant", "lena", "erpc", "proteins", "included", "controls"], "article_id"=>612846, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g004", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_LenB_binds_human_factor_H_Ligand_affinity_blot_analyses_of_recombinant_LenB_with_recombinant_LenA_and_B_burgdorferi_ErpC_proteins_included_as_positive_controls_71_/612846", "title"=>"LenB binds human factor H. Ligand affinity blot analyses of recombinant LenB, with recombinant LenA and <i>B. burgdorferi</i> ErpC proteins included as positive controls [71].", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:47:26"}
  • {"files"=>["https://ndownloader.figshare.com/files/942777"], "description"=>"<p>(A) Saturable binding of LenB to intact fibronectin, with calculated K<sub>d</sub> 106±8 nM (means and standard deviations from three experiments). Significant differences (P<0.05) between LenA and LenB binding are indicated with asterisks. (B) Binding of fibronectin by LenB is not affected by heparin. Fibronectin was preincubated with heparin, then binding by 1 µM LenB was analyzed in the presence of additional heparin. (C) Interaction with the 70-kDa N-terminal fragment of fibronectin (70 kDa) can account for complete LenB binding to intact fibronectin (Fn). (D) High avidity binding of LenB to the NTD of fibronectin, with calculated K<sub>d</sub> 69.5 nM (means and ranges from two experiments). LenB did not appreciably bind the fibronectin GBD.</p>", "links"=>[], "tags"=>["lena", "lenb", "interactions", "fibronectin", "proteolytic"], "article_id"=>613167, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g008", "stats"=>{"downloads"=>2, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ELISA_results_of_LenA_and_LenB_interactions_with_fibronectin_or_its_proteolytic_fragments_/613167", "title"=>"ELISA results of LenA and LenB interactions with fibronectin or its proteolytic fragments.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:52:47"}
  • {"files"=>["https://ndownloader.figshare.com/files/942324"], "description"=>"<p>(A) Circular dichroism spectrum of recombinant LenA. Deconvolution indicated this protein to consist of 36% beta-sheet, 23% turns, and 41% unordered/other structures. (B) Melting analysis of recombinant LenA, indicating a relatively stable protein with a melting point of 53°C (±2°C).</p>", "links"=>[], "tags"=>["recombinant"], "article_id"=>612720, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g003", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Biophysical_analysis_of_recombinant_LenA_/612720", "title"=>"Biophysical analysis of recombinant LenA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:45:20"}
  • {"files"=>["https://ndownloader.figshare.com/files/942259"], "description"=>"<p>Immunoblot of bacterial lysates using polyclonal rabbit antiserum raised against recombinant <i>L. interrogans</i> serovar Pomona LenD. Lanes 1, 2, and 3 contained 0.5 µg of recombinant LenA, LenC, and LenD, respectively, demonstrating the specificity of the antiserum. Lanes 4-11 contained whole-cell lysates from several different species of <i>Leptospira</i>: (4) <i>L. interrogans</i> serovar Copenhageni strain Fiocruz L1-130; (5) <i>L. interrogans</i> serovar Pomona strain PO-01; (6) <i>L. kirschneri</i>; (7) <i>L. noguchii</i>; (8) <i>L. santarosai</i>; (9) <i>L. borgpetersenii</i>; (10) <i>L. weilii</i>; (11) <i>L. biflexa</i>. Locations of molecular size standards (in kDa) are shown to the left. Note that the recombinant LenD protein includes a fusion partner and is not lipidated, so exhibits a different mobility than do the native proteins. (B) LenD localizes to the <i>L. interrogans</i> outer membrane, as assessed by Triton X-114 extraction. <i>L. interrogans</i> serovar Copenhageni LI-130 whole-cell lysate (lane W), the aqueous fraction (lane A, containing periplasmic proteins), the insoluble pellet (lane P, containing cytoplasmic cylinders and intact bacteria) and the detergent fraction (lane D, containing outer membrane proteins) were subjected to immunoblot using polyclonal rabbit antisera raised against LenD and FlaA1, a component of the inner membrane-associated endoflagella.</p>", "links"=>[], "tags"=>["infectious"], "article_id"=>612660, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g002", "stats"=>{"downloads"=>0, "page_views"=>2, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_A_Infectious_Leptospira_species_produce_a_protein_similar_to_L_interrogans_LenD_/612660", "title"=>"(A) Infectious <i>Leptospira</i> species produce a protein similar to <i>L. interrogans</i> LenD.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:44:20"}
  • {"files"=>["https://ndownloader.figshare.com/files/942532"], "description"=>"<p>Asterisks indicate positions of relatively weak signals corresponding to binding of laminin by LenA and LenB. Smaller bands seen in some lanes correspond with protein degradation products, indicating that at least some of the larger Len proteins can bind laminin even when partially truncated. Bovine serum albumin (BSA) was included in all blots as a negative control. Positions of molecular mass standards are indicated to the left (in kDa).</p>", "links"=>[], "tags"=>["affinity", "blot", "recombinant", "len", "proteins", "purified"], "article_id"=>612920, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g005", "stats"=>{"downloads"=>7, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ligand_affinity_blot_analyses_of_recombinant_Len_proteins_with_purified_laminin_/612920", "title"=>"Ligand affinity blot analyses of recombinant Len proteins with purified laminin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:48:40"}
  • {"files"=>["https://ndownloader.figshare.com/files/942690"], "description"=>"<p>Prolonged film exposures indicated binding of fibronectin by LenB and LenD, but increased background signal made it impossible to produce a clear figure (see <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0001188#pone.0001188.s002\" target=\"_blank\">Fig. S2</a>). No indication of LenA binding to fibronectin was observed at any exposure. Bovine serum albumin (BSA) was included in all blots as a negative control. Positions of molecular mass standards are indicated to the left (in kDa).</p>", "links"=>[], "tags"=>["affinity", "blot", "recombinant", "len", "proteins", "purified"], "article_id"=>613082, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g007", "stats"=>{"downloads"=>1, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Ligand_affinity_blot_analyses_of_recombinant_Len_proteins_using_purified_fibronectin_/613082", "title"=>"Ligand affinity blot analyses of recombinant Len proteins using purified fibronectin.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:51:22"}
  • {"files"=>["https://ndownloader.figshare.com/files/942908"], "description"=>"a<p>GenBank and TIGR assigned different identifying numbers to many ORFs of <i>L. interrogans</i> serovar Lai strain 56601.</p>", "links"=>[], "tags"=>["numbers", "genes", "contained", "completed", "genomes"], "article_id"=>613295, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.t001", "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ORF_numbers_of_len_genes_contained_in_completed_genomes_of_L_interrogans_/613295", "title"=>"ORF numbers of <i>len</i> genes contained in completed genomes of <i>L. interrogans</i>.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2007-11-14 00:54:55"}
  • {"files"=>["https://ndownloader.figshare.com/files/942111"], "description"=>"<p>(A) Schematic of Len proteins, with individual Len-motifs indicated by grey rectangles. LenC, LenD, LenE and LenF each consist of 2 Len-motifs, bridged by proline-rich linkers. (B) Alignment of predicted amino acid sequences of representative proteins: serovar Lai LenA (LenA, Lai), serovar Bratislava LenB (LenB, Brat), serovar Bratislava LenC-1 (LenC, Brat), serovar Canicola LenC-2 (LenC, Can), serovar Pomona LenD (LenD, Pom), serovar Grippotyphosa LenE (LenE, Gripp), serovar Pomona LenF-1 (LenF,. Pom), and serovar Hardjo LenF-1 (LenF, Har). Sequences of the proteins possessing two Len-motifs (LenC, LenD, LenE and LenF) were divided in the middle, after the well-conserved internal CVEQ sequence, to permit alignment of each Len-motif, and the amino- and carboxy-terminal Len-motifs are indicated by “-N” and “-C”, respectively. An alignment of these same proteins, undivided, is presented in <a href=\"http://www.plosone.org/article/info:doi/10.1371/journal.pone.0001188#pone.0001188.s001\" target=\"_blank\">Figure S1</a>. Identical amino acids found in the majority of proteins are boxed and shaded. Cysteine residues that may serve as amino-terminal lipidation sites are circled. (C) Unrooted phylogenetic tree of predicted amino acid sequences of each identified Len protein. Bootstrap values of each major node are indicated. (D) Alignment of sequences located 5′ of <i>lenA</i> and <i>lenB</i> genes. Identical nucleotides are boxed and shaded.</p>", "links"=>[], "tags"=>["len", "proteins"], "article_id"=>612508, "categories"=>["Infectious Diseases", "Microbiology"], "users"=>["Brian Stevenson", "Henry A. Choy", "Marija Pinne", "Matthew L. Rotondi", "M. Clarke Miller", "Edward DeMoll", "Peter Kraiczy", "Anne E. Cooley", "Trevor P. Creamer", "Marc A. Suchard", "Catherine A. Brissette", "Ashutosh Verma", "David A. Haake"], "doi"=>"https://dx.doi.org/10.1371/journal.pone.0001188.g001", "stats"=>{"downloads"=>0, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Relationships_between_Len_proteins_and_genes_/612508", "title"=>"Relationships between Len proteins and genes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2007-11-14 00:41:48"}

PMC Usage Stats | Further Information

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  • {"unique-ip"=>"9", "full-text"=>"10", "pdf"=>"5", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2016", "month"=>"10"}
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  • {"unique-ip"=>"10", "full-text"=>"12", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"3", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2016", "month"=>"12"}
  • {"unique-ip"=>"10", "full-text"=>"6", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"3", "year"=>"2017", "month"=>"1"}
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  • {"unique-ip"=>"4", "full-text"=>"4", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"3"}
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  • {"unique-ip"=>"7", "full-text"=>"8", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2017", "month"=>"12"}
  • {"unique-ip"=>"5", "full-text"=>"4", "pdf"=>"1", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"1"}
  • {"unique-ip"=>"10", "full-text"=>"9", "pdf"=>"2", "abstract"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"5", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"3"}
  • {"unique-ip"=>"5", "full-text"=>"5", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"1"}
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  • {"unique-ip"=>"6", "full-text"=>"4", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"2", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"9"}
  • {"unique-ip"=>"12", "full-text"=>"10", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"12"}
  • {"unique-ip"=>"16", "full-text"=>"19", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2018", "month"=>"11"}
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  • {"unique-ip"=>"6", "full-text"=>"7", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"3"}
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  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2019", "month"=>"9"}
  • {"unique-ip"=>"8", "full-text"=>"6", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"9", "supp-data"=>"1", "cited-by"=>"0", "year"=>"2019", "month"=>"10"}
  • {"unique-ip"=>"9", "full-text"=>"7", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2019", "month"=>"12"}
  • {"unique-ip"=>"16", "full-text"=>"19", "pdf"=>"4", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"1", "supp-data"=>"4", "cited-by"=>"0", "year"=>"2020", "month"=>"2"}
  • {"unique-ip"=>"13", "full-text"=>"12", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"2", "cited-by"=>"0", "year"=>"2020", "month"=>"3"}
  • {"unique-ip"=>"10", "full-text"=>"12", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"4"}
  • {"unique-ip"=>"12", "full-text"=>"11", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"5"}
  • {"unique-ip"=>"9", "full-text"=>"9", "pdf"=>"1", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"6"}
  • {"unique-ip"=>"7", "full-text"=>"7", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"7"}
  • {"unique-ip"=>"7", "full-text"=>"9", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"8"}
  • {"unique-ip"=>"4", "full-text"=>"5", "pdf"=>"0", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"9"}
  • {"unique-ip"=>"9", "full-text"=>"11", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"10"}
  • {"unique-ip"=>"5", "full-text"=>"3", "pdf"=>"2", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"11"}
  • {"unique-ip"=>"7", "full-text"=>"6", "pdf"=>"3", "scanned-summary"=>"0", "scanned-page-browse"=>"0", "figure"=>"0", "supp-data"=>"0", "cited-by"=>"0", "year"=>"2020", "month"=>"12"}
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Relative Metric

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