The Two-Domain LysX Protein of Mycobacterium tuberculosis Is Required for Production of Lysinylated Phosphatidylglycerol and Resistance to Cationic Antimicrobial Peptides
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{"title"=>"The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides", "type"=>"journal", "authors"=>[{"first_name"=>"Erin", "last_name"=>"Maloney", "scopus_author_id"=>"8531803600"}, {"first_name"=>"Dorota", "last_name"=>"Stankowska", "scopus_author_id"=>"23974940500"}, {"first_name"=>"Jian", "last_name"=>"Zhang", "scopus_author_id"=>"7601343397"}, {"first_name"=>"Marek", "last_name"=>"Fol", "scopus_author_id"=>"6506493128"}, {"first_name"=>"Qi Jian", "last_name"=>"Cheng", "scopus_author_id"=>"37042002300"}, {"first_name"=>"Shichun", "last_name"=>"Lun", "scopus_author_id"=>"7006810174"}, {"first_name"=>"William R.", "last_name"=>"Bishai", "scopus_author_id"=>"7005156752"}, {"first_name"=>"Malini", "last_name"=>"Rajagopalan", "scopus_author_id"=>"7005707191"}, {"first_name"=>"Delphi", "last_name"=>"Chatterjee", "scopus_author_id"=>"35418695500"}, {"first_name"=>"Murty V.", "last_name"=>"Madiraju", "scopus_author_id"=>"7003537701"}], "year"=>2009, "source"=>"PLoS Pathogens", "identifiers"=>{"issn"=>"15537366", "scopus"=>"2-s2.0-70049106239", "sgr"=>"70049106239", "pui"=>"355237352", "isbn"=>"10.1371/journal.ppat.1000534", "pmid"=>"19649276", "doi"=>"10.1371/journal.ppat.1000534"}, "id"=>"a51adb43-076a-30b9-b3fa-a89e0eba3a81", "abstract"=>"The well-recognized phospholipids (PLs) of Mycobacterium tuberculosis (Mtb) include several acidic species such as phosphatidylglycerol (PG), cardiolipin, phosphatidylinositol and its mannoside derivatives, in addition to a single basic species, phosphatidylethanolamine. Here we demonstrate that an additional basic PL, lysinylated PG (L-PG), is a component of the PLs of Mtb H37Rv and that the lysX gene encoding the two-domain lysyl-transferase (mprF)-lysyl-tRNA synthetase (lysU) protein is responsible for L-PG production. The Mtb lysX mutant is sensitive to cationic antibiotics and peptides, shows increased association with lysosome-associated membrane protein-positive vesicles, and it exhibits altered membrane potential compared to wild type. A lysX complementing strain expressing the intact lysX gene, but not one expressing mprF alone, restored the production of L-PG and rescued the lysX mutant phenotypes, indicating that the expression of both proteins is required for LysX function. The lysX mutant also showed defective growth in mouse and guinea pig lungs and showed reduced pathology relative to wild type, indicating that LysX activity is required for full virulence. Together, our results suggest that LysX-mediated production of L-PG is necessary for the maintenance of optimal membrane integrity and for survival of the pathogen upon infection.", "link"=>"http://www.mendeley.com/research/twodomain-lysx-protein-mycobacterium-tuberculosis-required-production-lysinylated-phosphatidylglycer", "reader_count"=>60, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>2, "Librarian"=>1, "Researcher"=>16, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>17, "Student > Postgraduate"=>3, "Student > Master"=>6, "Other"=>1, "Student > Bachelor"=>4, "Lecturer"=>1, "Professor"=>5, "Unspecified"=>1}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>2, "Librarian"=>1, "Researcher"=>16, "Student > Doctoral Student"=>3, "Student > Ph. D. Student"=>17, "Student > Postgraduate"=>3, "Student > Master"=>6, "Other"=>1, "Student > Bachelor"=>4, "Lecturer"=>1, "Professor"=>5, "Unspecified"=>1}, "reader_count_by_subject_area"=>{"Engineering"=>1, "Environmental Science"=>1, "Biochemistry, Genetics and Molecular Biology"=>9, "Agricultural and Biological Sciences"=>32, "Medicine and Dentistry"=>8, "Arts and Humanities"=>1, "Pharmacology, Toxicology and Pharmaceutical Science"=>1, "Chemistry"=>1, "Immunology and Microbiology"=>5, "Unspecified"=>1}, "reader_count_by_subdiscipline"=>{"Engineering"=>{"Engineering"=>1}, "Medicine and Dentistry"=>{"Medicine and Dentistry"=>8}, "Chemistry"=>{"Chemistry"=>1}, "Immunology and Microbiology"=>{"Immunology and Microbiology"=>5}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>32}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>9}, "Environmental Science"=>{"Environmental Science"=>1}, "Pharmacology, Toxicology and Pharmaceutical Science"=>{"Pharmacology, Toxicology and Pharmaceutical Science"=>1}, "Unspecified"=>{"Unspecified"=>1}, "Arts and Humanities"=>{"Arts and Humanities"=>1}}, "reader_count_by_country"=>{"Denmark"=>1, "United Kingdom"=>2, "Germany"=>1, "India"=>2}, "group_count"=>0}

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  • {"files"=>["https://ndownloader.figshare.com/files/889577"], "description"=>"<p>THP-1-derived macrophages were infected with <i>Mtb</i> strains; at the indicated times following infection, the macrophages were lysed, and the <i>Mtb</i> viability was determined. The white bars represent Rv-80lys; the dashed bars represent Rv-82med; the grey bars represent Rv-81ami; and the black bars represent Rv-03. Data are mean±standard error from three independent experiments, and the Mann-Whitney Rank Sum Test was used for data analyses.</p>", "links"=>[], "tags"=>["viability"], "article_id"=>560030, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g005", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_viability_of_lysX_in_macrophages_/560030", "title"=>"The viability of <i>lysX</i> in macrophages.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 00:00:30"}
  • {"files"=>["https://ndownloader.figshare.com/files/889886"], "description"=>"<p>Panel A: C57BL/6 female mouse lungs were infected with <i>lysX</i> (triangles) and WT (dark diamonds) strains via an aerosol route. The mean CFU counts were obtained from lung homogenates of at least three mice per group and plated on Middlebrook 7H10 agar plates. All plates were incubated at 37°C for at least three weeks before colonies were counted. Panel B: Guinea pigs (Hartley strain) were infected with <i>lysX</i> (open symbols) or WT (dark symbols) strains via an aerosol route. Five guinea pigs were sacrificed at days 1, 21 and 42 days after infection, and the survival of <i>Mtb</i> strains in the entire lung homogenate was determined by plating on agar medium as described above. Panels C, D: Gross pathology of the lungs infected with the Rv-80lys and Rv-03 <i>Mtb</i> strains. Lungs from mouse -C- and guinea pig -D- were excised, stored in 10% formalin, embedded, and stained with hematoxylin and eosin for histopathological analysis. Note the presence of tubercles on the surface of the lungs for Rv-03 compared to Rv-80lys. Panels E, F: Histopathology of mouse -E- and guinea pig -F- lungs infected with the Rv-80lys and Rv-03 <i>Mtb</i> strains. Hematoxylin-eosin staining confirmed that the lungs infected with Rv-03, but not those infected with Rv-80lys, had extensive inflammation in both species and showed caseating granulomas in guinea pigs.</p>", "links"=>[], "tags"=>["wt", "strains"], "article_id"=>560332, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g008", "stats"=>{"downloads"=>0, "page_views"=>1, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Growth_of_lysX_and_WT_strains_in_vivo_/560332", "title"=>"Growth of <i>lysX</i> and WT strains in vivo.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 00:05:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/889507"], "description"=>"<p>The relative membrane potential was calculated using the average mean fluorescence intensity (the ratio between the average red fluorescence and the average green fluorescence). The graph shows the average of four experiments. Wild type and <i>lysX</i> mutant strains were incubated with 3 µM DiOC<sub>2</sub>(3) for 5 h in either the presence (+) or absence (−) of 100 µM CCCP. The bars represent the mean±standard error. * Represents <i>P</i><0.002 versus Rv-03 and Rv-81ami (Student-Newman-Keuls Method), whereas # refers to <i>P</i> = 0.001 compared to untreated with CCCP.</p>", "links"=>[], "tags"=>["membrane"], "article_id"=>559957, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g004", "stats"=>{"downloads"=>2, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Determination_of_the_membrane_potential_of_Mtb_strains_/559957", "title"=>"Determination of the membrane potential of <i>Mtb</i> strains.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 02:45:57"}
  • {"files"=>["https://ndownloader.figshare.com/files/889414"], "description"=>"<p>Panel A: The growth and viability of the <i>Mtb lysX</i> strains in 7H9 broth in the absence of antibiotics -i. A-ii: The growth and viability of cultures grown in the presence of 1.0 µg/ml Van. At the indicated times, growth was measured. After 3 days of growth in broth, viability was determined by plating cells on Middlebrook 7H11 agar and determining the CFU. Symbols: Filled diamonds – Rv-03; grey squares – Rv81-ami; white triangles – Rv-80lys; crosses – Rv-82med. The inset shows the viable cell count. Black bars - Rv-03, grey bars - Rv-81ami, white bars - Rv-80lys and dashed bars - Rv82-med. A-iii: The growth and viability of cultures grown in the presence of 100 units/ml PMB. * Represents a <i>P</i> value<0.001 versus Rv-03 and Rv-81ami (Student-Newman-Keuls Method); bars represent means±standard error. Panel B: The growth and viability of <i>Mtb</i> strains in the presence of 1 mg/ml lysozyme -i- or HNP-1 -ii. There was no significant reduction in viability compared to cultures grown without TFA (data not shown). The stars represent P<0.001 versus Rv-03 and Rv-81ami (Student-Newman-Keuls Method). The bars represent the mean±standard error.</p>", "links"=>[], "tags"=>["infectious diseases/bacterial infections", "microbiology", "microbiology/innate immunity", "microbiology/microbial physiology and metabolism", "molecular biology"], "article_id"=>559856, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g003", "stats"=>{"downloads"=>1, "page_views"=>0, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Phenotype_of_lysX_strains_/559856", "title"=>"Phenotype of <i>lysX</i> strains.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 02:44:16"}
  • {"files"=>["https://ndownloader.figshare.com/files/890026"], "description"=>"<p>A- refers to the wild type strain carrying the <i>lysX</i> gene at its native locus. B- refers to the Rv-80 merodiploid (hyg<sup>r</sup>) strain produced by the integration of a plasmid expressing the <i>lysX</i> gene from the amidase promoter. C- refers to a single crossover (SCO, hyg<sup>r</sup>, kan<sup>r</sup>, gm<sup>r</sup>) recombinant produced by integration of the suicide recombination plasmid. D- refers to a mutant double crossover (DCO, hyg<sup>r</sup>, kan<sup>s</sup>, gm<sup>r</sup>) produced following a reciprocal recombination event. E- refers to Rv-80lys (kan<sup>r</sup>, gm<sup>r</sup>) produced following switching of the resident integrated plasmid (hyg<sup>r</sup>) with the incoming pMV306 plasmid (kan<sup>r</sup>). F- refers to Rv-82med (hyg<sup>r</sup>, gm<sup>r</sup>) produced following switching of the resident pMV306 plasmid (kan<sup>r</sup>) with the incoming plasmid expressing the <i>mprF</i> fragment from the amidase promoter (hyg<sup>r</sup>).</p>", "links"=>[], "tags"=>["mutant", "complemented"], "article_id"=>560473, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g009", "stats"=>{"downloads"=>1, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Cartoon_showing_construction_of_the_lysX_mutant_and_complemented_strains_/560473", "title"=>"Cartoon showing construction of the <i>lysX</i> mutant and complemented strains.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 00:07:53"}
  • {"files"=>["https://ndownloader.figshare.com/files/440763", "https://ndownloader.figshare.com/files/440817", "https://ndownloader.figshare.com/files/440856", "https://ndownloader.figshare.com/files/440919", "https://ndownloader.figshare.com/files/440965"], "description"=>"<div><p>The well-recognized phospholipids (PLs) of <em>Mycobacterium tuberculosis</em> (<em>Mtb</em>) include several acidic species such as phosphatidylglycerol (PG), cardiolipin, phosphatidylinositol and its mannoside derivatives, in addition to a single basic species, phosphatidylethanolamine. Here we demonstrate that an additional basic PL, lysinylated PG (L-PG), is a component of the PLs of <em>Mtb</em> H37Rv and that the <em>lysX</em> gene encoding the two-domain lysyl-transferase (<em>mpr</em>F)-lysyl-tRNA synthetase (<em>lys</em>U) protein is responsible for L-PG production. The <em>Mtb lysX</em> mutant is sensitive to cationic antibiotics and peptides, shows increased association with lysosome-associated membrane protein–positive vesicles, and it exhibits altered membrane potential compared to wild type. A <em>lysX</em> complementing strain expressing the intact <em>lysX</em> gene, but not one expressing <em>mprF</em> alone, restored the production of L-PG and rescued the <em>lysX</em> mutant phenotypes, indicating that the expression of both proteins is required for LysX function. The <em>lysX</em> mutant also showed defective growth in mouse and guinea pig lungs and showed reduced pathology relative to wild type, indicating that LysX activity is required for full virulence. Together, our results suggest that LysX-mediated production of L-PG is necessary for the maintenance of optimal membrane integrity and for survival of the pathogen upon infection.</p></div>", "links"=>[], "tags"=>["two-domain", "lysx", "lysinylated", "phosphatidylglycerol", "cationic", "antimicrobial", "peptides"], "article_id"=>146890, "categories"=>["Cancer", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1000534.s001", "https://dx.doi.org/10.1371/journal.ppat.1000534.s002", "https://dx.doi.org/10.1371/journal.ppat.1000534.s003", "https://dx.doi.org/10.1371/journal.ppat.1000534.s004", "https://dx.doi.org/10.1371/journal.ppat.1000534.s005"], "stats"=>{"downloads"=>1, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/The_Two_Domain_LysX_Protein_of_Mycobacterium_tuberculosis_Is_Required_for_Production_of_Lysinylated_Phosphatidylglycerol_and_Resistance_to_Cationic_Antimicrobial_Peptides/146890", "title"=>"The Two-Domain LysX Protein of <em>Mycobacterium tuberculosis</em> Is Required for Production of Lysinylated Phosphatidylglycerol and Resistance to Cationic Antimicrobial Peptides", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2009-07-31 01:54:50"}
  • {"files"=>["https://ndownloader.figshare.com/files/889303"], "description"=>"<p>A: MALDI mass spectrometry analysis of L-PG in negative-ion mode. The <i>m/z</i> 681 [M-H]<sup>−</sup> represented the molecular ion peak. B: Structural analysis of L-PG. <sup>1</sup>H-NMR spectrum of L-PG. The acetyl group can be found at δ<sub>C<u>H</u>3</sub> 2.1 ppm, and δ<sub>C<u>H</u>2</sub> from the primary amine in lysine was detectable at 2.4 ppm. The inset shows the <sup>31</sup>P-NMR spectrum, in which the phosphorus resonance shifted at −14.96 ppm. C: The amino acid profile of L-PG. Pure lipid was hydrolyzed with 6 N HCl for 24 h, and the soluble hydrolytic product was analyzed in an amino acid analyzer. Note that the elution of lysine at 54.33 min coincides with the standard (not shown). The small peak at position 41 min corresponds to a buffer change during the run, and the ammonia peak at 56.11 min is from the buffer used to run the analyzer. D: The proposed L-PG structure. The proposed structure of L-PG with a C<sub>18</sub> fatty acid identified from fatty acid analysis (data not shown).</p>", "links"=>[], "tags"=>["infectious diseases/bacterial infections", "microbiology", "microbiology/innate immunity", "microbiology/microbial physiology and metabolism", "molecular biology"], "article_id"=>559749, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g002", "stats"=>{"downloads"=>1, "page_views"=>3, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Structural_analysis_of_L_PoL_/559749", "title"=>"Structural analysis of L-PoL.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 02:42:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/889197"], "description"=>"<p>A: <i>Mtb</i> strains were grown in the presence and absence of <sup>14</sup>C-lysine. Total lipids were extracted in chloroform∶methanol (2∶1 v/v) and resolved by TLC on Silcia Gel 60 (EMD Chemicals, New Jersey) in a solvent system of chloroform∶methanol∶water (65∶25∶4 v/v/v). TLC plates were either visualized by autoradiography (lanes i, iv, vii and x), exposed to iodine vapors (lanes ii, v, viii and xi), or stained with ninhydrin (lanes iii, vi, ix and xii). B: Southern blot analysis of <i>Mtb lysX</i> mutant strains. B-i: The <i>Cla</i>I fragment bearing the wild type <i>lysX</i> gene (3.5 kb) with the locations of the <i>mprF</i> and <i>lysU</i> regions marked. The dark box designated as “probe 1” is an approximately 750 bp fragment that hybridizes with the 5′-end of <i>lysX</i> and 160 bp of the <i>lysX</i> coding region. The <i>Cla</i>I fragment bearing the mutant <i>lysX</i> gene disrupted with the gentamycin cassette (0.9 kb) is also shown. The dark band designated as “probe 2” is the 900 bp gentamycin gene that hybridizes with the mutant <i>lysX</i> gene. B-ii: Southern blot analysis of <i>Cla</i>I-digested <i>Mtb</i> genomic DNA hybridized with probe 1. The 7 kb and 4 kb band positions represent Rv-03 and Rv-80lys, respectively. Note that the complemented copy contains a band corresponding to the integrated copy of <i>lysX</i> gene plus the flanking plasmid sequence. B-iii: Southern blot analysis of <i>Cla</i>I-digested <i>Mtb</i> genomic DNA (see <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1000534#ppat-1000534-g001\" target=\"_blank\">Fig. 1B-iii</a>) hybridized with probe 2. pMMR85 is a positive control plasmid containing the mutant <i>lysX</i> gene plus flanking regions.</p>", "links"=>[], "tags"=>["lipid", "blot", "mutant"], "article_id"=>559640, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g001", "stats"=>{"downloads"=>1, "page_views"=>9, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Polar_lipid_and_Southern_blot_analysis_of_the_lysX_mutant_strain_/559640", "title"=>"Polar lipid and Southern blot analysis of the <i>lysX</i> mutant strain.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 02:40:40"}
  • {"files"=>["https://ndownloader.figshare.com/files/889781"], "description"=>"<p>Panel A: MDMO were infected with <i>Mtb</i> strains, and TNF-α release was measured by ELISA. PMA was used as a positive control. TNF-α levels in panel A were measured after 24 h. * Represents <i>P</i><0.05 compared to Rv-03, Rv-81ami, control (untreated cells) and PMA. Panel B: Secretion of IL-6 by MDMO after 48 h of infection. * <i>P</i><0.05 compared to Rv-03, Rv-81ami and control. The experiments were done in duplicate, and representative results are shown. Data are mean±standard error. Student-Newman-Keuls Method was used.</p>", "links"=>[], "tags"=>["cytokine", "responses"], "article_id"=>560229, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g007", "stats"=>{"downloads"=>4, "page_views"=>4, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Select_cytokine_responses_of_macrophages_/560229", "title"=>"Select cytokine responses of macrophages.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 00:03:49"}
  • {"files"=>["https://ndownloader.figshare.com/files/889682"], "description"=>"<p>Panel A: THP-1-derived macrophages were infected with GFP-expressing <i>Mtb</i> strains (Rv-03, Rv-80lys, Rv-81ami and Rv-82med). Bacteria (green spots) inside LAMP-1-positive phagosomes (red) produce a yellow signal indicating co-localization (merged). Panel B: The percent co-localization was determined by visual scoring of yellow spots after 72 h of infection. We analyzed 126 macrophages for Rv-80lys, 164 for wild type, 168 for complemented, and 127 for Rv-82med and scored 534 bacterial cells for Rv-80lys, 1,307 for wild type, 848 for Rv-81ami, and 402 for Rv-82med. <i>Mtb</i> Rv-03 (black bar; 21.2±1.6%), Rv-80lys (white bar; 52.0±3.0%), Rv-81ami (grey bar; 26.4±2.2%) and Rv-82med (dashed bar; 52.6±2.8%). * <i>P</i><0.001 versus Rv-03 and Rv-81ami using the Student-Newman-Keuls Method; bars represent mean±standard error.</p>", "links"=>[], "tags"=>["lamp-1-expressing"], "article_id"=>560129, "categories"=>["Infectious Diseases", "Molecular Biology", "Microbiology"], "users"=>["Erin Maloney", "Dorota Stankowska", "Jian Zhang", "Marek Fol", "Qi-Jian Cheng", "Shichun Lun", "William R. Bishai", "Malini Rajagopalan", "Delphi Chatterjee", "Murty V. Madiraju"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1000534.g006", "stats"=>{"downloads"=>1, "page_views"=>6, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Co_localization_of_Mtb_with_LAMP_1_expressing_phagosomes_/560129", "title"=>"Co-localization of <i>Mtb</i> with LAMP-1-expressing phagosomes.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2009-07-31 00:02:09"}

PMC Usage Stats | Further Information

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Relative Metric

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