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            <name>Title</name>
            <description>A name given to the resource</description>
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                <text>Coronavirus</text>
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            <description>An account of the resource</description>
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                <text>Dominio científico: Coronavirus</text>
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    <description>A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.</description>
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          <name>Title</name>
          <description>A name given to the resource</description>
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              <text>Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci.</text>
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          <name>Creator</name>
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            <elementText elementTextId="4117">
              <text>Silvia Herbert, Agnieszka Bera, Christiane Nerz, Dirk Kraus, Andreas Peschel, Christiane Goerke, Michael Meehl, Ambrose Cheung, Friedrich Götz</text>
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          <name>Description</name>
          <description>An account of the resource</description>
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              <text>It has been shown recently that modification of peptidoglycan by O-acetylation renders pathogenic staphylococci resistant to the muramidase activity of lysozyme. Here, we show that a Staphylococcus aureus double mutant defective in O-acetyltransferase A (OatA), and the glycopeptide resistance-associated two-component system, GraRS, is much more sensitive to lysozyme than S. aureus with the oatA mutation alone. The graRS single mutant was resistant to the muramidase activity of lysozyme, but was sensitive to cationic antimicrobial peptides (CAMPs) such as the human lysozyme-derived peptide 107R-A-W-V-A-W-R-N-R115 (LP9), polymyxin B, or gallidermin. A comparative transcriptome analysis of wild type and the graRS mutant revealed that GraRS controls 248 genes. It up-regulates global regulators (rot, sarS, or mgrA), various colonization factors, and exotoxin-encoding genes, as well as the ica and dlt operons. A pronounced decrease in the expression of the latter two operons explains why the graRS mutant is also biofilm-negative. The decrease of the dlt transcript in the graRS mutant correlates with a 46.7% decrease in the content of esterified d-alanyl groups in teichoic acids. The oatA/dltA double mutant showed the highest sensitivity to lysozyme; this mutant completely lacks teichoic acid-bound d-alanine esters, which are responsible for the increased susceptibility to CAMPs and peptidoglycan O-acetylation. Our results demonstrate that resistance to lysozyme can be dissected into genes mediating resistance to its muramidase activity (oatA) and genes mediating resistance to CAMPs (graRS and dlt). The two lysozyme activities act synergistically, as the oatA/dltA or oatA/graRS double mutants are much more susceptible to lysozyme than each of the single mutants.</text>
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          <name>Date</name>
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              <text>2007</text>
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          <name>Identifier</name>
          <description>An unambiguous reference to the resource within a given context</description>
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              <text>DOI: 10.1371/journal.ppat.0030102</text>
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          <name>Source</name>
          <description>A related resource from which the described resource is derived</description>
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            <elementText elementTextId="4121">
              <text>PLoS Pathogens</text>
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        <element elementId="45">
          <name>Publisher</name>
          <description>An entity responsible for making the resource available</description>
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            <elementText elementTextId="4122">
              <text>Public Library of Science (PLoS)</text>
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          <name>Coverage</name>
          <description>The spatial or temporal topic of the resource, the spatial applicability of the resource, or the jurisdiction under which the resource is relevant</description>
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            <elementText elementTextId="4123">
              <text>Biology (General), Immunologic diseases. Allergy</text>
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          <name>Language</name>
          <description>A language of the resource</description>
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              <text>EN</text>
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