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rdf:type
lifeskim:mentions
pubmed:dateCreated
2008-3-11
pubmed:abstractText
The endoglycosidase EndoS and the cysteine proteinase SpeB from the human pathogen Streptococcus pyogenes are functionally related in that they both hydrolyze IgG leading to impairment of opsonizing antibodies and thus enhance bacterial survival in human blood. In this study, we further investigated the relationship between EndoS and SpeB by examining their in vitro temporal production and stability and activity of EndoS. Furthermore, theoretical structure modeling of EndoS combined with site-directed mutagenesis and chemical blocking of amino acids was used to identify amino acids required for the IgG glycan-hydrolyzing activity of EndoS.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-10456870, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-10635330, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-10891067, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-10922035, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-10931281, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-10964570, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-11069651, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-11169110, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-11598100, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-11679669, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-11927545, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12366839, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12438337, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12552129, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12574517, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12761074, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12824332, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-12949112, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-13931033, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-14638794, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-14651616, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-14658761, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-14976595, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-15028731, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-16516924, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-16598448, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-16980693, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-17899548, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-5040648, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-6059350, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-7044372, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-7516997, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-7689226, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-7730368, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-7790099, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-8335368, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-8535779, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-8601315, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-8890235, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-9042366, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-9345621, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-9529068, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-9673282, http://linkedlifedata.com/resource/pubmed/commentcorrection/18182097-9874803
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1471-2180
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:18182097-Amino Acid Sequence, pubmed-meshheading:18182097-Bacterial Proteins, pubmed-meshheading:18182097-Blotting, Western, pubmed-meshheading:18182097-Cysteine Endopeptidases, pubmed-meshheading:18182097-Glutamic Acid, pubmed-meshheading:18182097-Glycoside Hydrolases, pubmed-meshheading:18182097-Hydrolysis, pubmed-meshheading:18182097-Immunoglobulin G, pubmed-meshheading:18182097-Models, Molecular, pubmed-meshheading:18182097-Molecular Sequence Data, pubmed-meshheading:18182097-Mutagenesis, Site-Directed, pubmed-meshheading:18182097-Polysaccharides, pubmed-meshheading:18182097-Protein Structure, Secondary, pubmed-meshheading:18182097-Sequence Homology, Amino Acid, pubmed-meshheading:18182097-Streptococcus pyogenes, pubmed-meshheading:18182097-Structural Homology, Protein, pubmed-meshheading:18182097-Structure-Activity Relationship, pubmed-meshheading:18182097-Tryptophan
pubmed:year
2008
pubmed:articleTitle
EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity.
pubmed:affiliation
Department of Clinical Sciences, Division of Infection Medicine, Lund University, Biomedical Center B14, SE-221 84 Lund, Sweden. maria.allhorn@med.lu.se
pubmed:publicationType
Journal Article
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