Biosynthesis of Cryptic Lipopolysaccharide Glycoforms in Haemophilus influenzae Involves a Mechanism Similar to That Required for O-Antigen Synthesis
Identifieur interne : 000078 ( Pmc/Corpus ); précédent : 000077; suivant : 000079Biosynthesis of Cryptic Lipopolysaccharide Glycoforms in Haemophilus influenzae Involves a Mechanism Similar to That Required for O-Antigen Synthesis
Auteurs : Derek W. Hood ; Gaynor Randle ; Andrew D. Cox ; Katherine Makepeace ; Jianjun Li ; Elke K. H. Schweda ; James C. Richards ; E. Richard MoxonSource :
- Journal of Bacteriology [ 0021-9193 ] ; 2004.
Abstract
It is generally thought that mucosal bacterial pathogens of the genera
Url:
DOI: 10.1128/JB.186.21.7429-7439.2004
PubMed: 15489455
PubMed Central: 523191
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PMC:523191Le document en format XML
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Involves a Mechanism Similar to That Required for O-Antigen Synthesis</title>
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<author><name sortKey="Li, Jianjun" sort="Li, Jianjun" uniqKey="Li J" first="Jianjun" last="Li">Jianjun Li</name>
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<author><name sortKey="Richards, James C" sort="Richards, James C" uniqKey="Richards J" first="James C." last="Richards">James C. Richards</name>
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<author><name sortKey="Moxon, E Richard" sort="Moxon, E Richard" uniqKey="Moxon E" first="E. Richard" last="Moxon">E. Richard Moxon</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Biosynthesis of Cryptic Lipopolysaccharide Glycoforms in <italic>Haemophilus influenzae</italic>
Involves a Mechanism Similar to That Required for O-Antigen Synthesis</title>
<author><name sortKey="Hood, Derek W" sort="Hood, Derek W" uniqKey="Hood D" first="Derek W." last="Hood">Derek W. Hood</name>
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<author><name sortKey="Makepeace, Katherine" sort="Makepeace, Katherine" uniqKey="Makepeace K" first="Katherine" last="Makepeace">Katherine Makepeace</name>
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<author><name sortKey="Li, Jianjun" sort="Li, Jianjun" uniqKey="Li J" first="Jianjun" last="Li">Jianjun Li</name>
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<author><name sortKey="Schweda, Elke K H" sort="Schweda, Elke K H" uniqKey="Schweda E" first="Elke K. H." last="Schweda">Elke K. H. Schweda</name>
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<author><name sortKey="Richards, James C" sort="Richards, James C" uniqKey="Richards J" first="James C." last="Richards">James C. Richards</name>
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<author><name sortKey="Moxon, E Richard" sort="Moxon, E Richard" uniqKey="Moxon E" first="E. Richard" last="Moxon">E. Richard Moxon</name>
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<series><title level="j">Journal of Bacteriology</title>
<idno type="ISSN">0021-9193</idno>
<idno type="eISSN">1098-5530</idno>
<imprint><date when="2004">2004</date>
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<front><div type="abstract" xml:lang="en"><p>It is generally thought that mucosal bacterial pathogens of the genera <italic>Haemophilus</italic>
, <italic>Neisseria</italic>
, and <italic>Moraxella</italic>
elaborate lipopolysaccharide (LPS) that is fundamentally different from that of enteric organisms that express O-specific polysaccharide side chains. <italic>Haemophilus influenzae</italic>
elaborates short-chain LPS that has a role in the pathogenesis of <italic>H. influenzae</italic>
infections. We show that the synthesis of LPS in this organism can no longer be as clearly distinguished from that in other gram-negative bacteria that express an O antigen. We provide evidence that a region of the <italic>H. influenzae</italic>
genome, the <italic>hmg</italic>
locus, is involved in the synthesis of glycoforms in which tetrasaccharide units are added en bloc, not stepwise, to the normal core glycoforms, similar to the biosynthesis of an O-antigen.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Bacteriol</journal-id>
<journal-id journal-id-type="publisher-id">jb</journal-id>
<journal-title>Journal of Bacteriology</journal-title>
<issn pub-type="ppub">0021-9193</issn>
<issn pub-type="epub">1098-5530</issn>
<publisher><publisher-name>American Society for Microbiology</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">15489455</article-id>
<article-id pub-id-type="pmc">523191</article-id>
<article-id pub-id-type="publisher-id">0548-04</article-id>
<article-id pub-id-type="doi">10.1128/JB.186.21.7429-7439.2004</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Molecular Biology of Pathogens</subject>
</subj-group>
</article-categories>
<title-group><article-title>Biosynthesis of Cryptic Lipopolysaccharide Glycoforms in <italic>Haemophilus influenzae</italic>
Involves a Mechanism Similar to That Required for O-Antigen Synthesis</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Hood</surname>
<given-names>Derek W.</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
<xref ref-type="corresp" rid="cor1">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Randle</surname>
<given-names>Gaynor</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cox</surname>
<given-names>Andrew D.</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Makepeace</surname>
<given-names>Katherine</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Li</surname>
<given-names>Jianjun</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Schweda</surname>
<given-names>Elke K. H.</given-names>
</name>
<xref ref-type="aff" rid="aff1">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Richards</surname>
<given-names>James C.</given-names>
</name>
<xref ref-type="aff" rid="aff1">2</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Moxon</surname>
<given-names>E. Richard</given-names>
</name>
<xref ref-type="aff" rid="aff1">1</xref>
</contrib>
</contrib-group>
<aff id="aff1">Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, United Kingdom,<label>1</label>
Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada,<label>2</label>
Clinical Research Centre, Karolinska Institutet and University College of South Stockholm, NOVUM, Huddinge, Sweden<label>3</label>
</aff>
<author-notes><fn id="cor1"><label>*</label>
<p>Corresponding author. Mailing address: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom. Phone: (44) 1865 222347. Fax: (44) 1865 222626. E-mail: <email>derek.hood@paediatrics.oxford.ac.uk</email>
.</p>
</fn>
</author-notes>
<pub-date pub-type="ppub"><month>11</month>
<year>2004</year>
</pub-date>
<volume>186</volume>
<issue>21</issue>
<fpage>7429</fpage>
<lpage>7439</lpage>
<history><date date-type="received"><day>15</day>
<month>4</month>
<year>2004</year>
</date>
<date date-type="accepted"><day>10</day>
<month>8</month>
<year>2004</year>
</date>
</history>
<copyright-statement>Copyright © 2004, American Society for Microbiology</copyright-statement>
<copyright-year>2004</copyright-year>
<abstract><p>It is generally thought that mucosal bacterial pathogens of the genera <italic>Haemophilus</italic>
, <italic>Neisseria</italic>
, and <italic>Moraxella</italic>
elaborate lipopolysaccharide (LPS) that is fundamentally different from that of enteric organisms that express O-specific polysaccharide side chains. <italic>Haemophilus influenzae</italic>
elaborates short-chain LPS that has a role in the pathogenesis of <italic>H. influenzae</italic>
infections. We show that the synthesis of LPS in this organism can no longer be as clearly distinguished from that in other gram-negative bacteria that express an O antigen. We provide evidence that a region of the <italic>H. influenzae</italic>
genome, the <italic>hmg</italic>
locus, is involved in the synthesis of glycoforms in which tetrasaccharide units are added en bloc, not stepwise, to the normal core glycoforms, similar to the biosynthesis of an O-antigen.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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