Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2002-9-17
pubmed:abstractText
A mecA-containing Staphylococcus aureus strain was grown in the presence of high concentrations of D-serine, D-threonine, and D-phenylalanine. These growth conditions resulted in the replacement of the carboxyl-terminal (fifth) D-alanine residue of peptidoglycan stem peptides with the D-amino acid present in the growth medium and a reduced ability to grow in the presence of methicillin. The most dramatic effect was seen with D-serine. With 32 mM D-serine, strains that had been able to grow in the presence of 800 micro g of methicillin per ml were only able to grow in the presence of less than 50 micro g/ml. The results also suggest that in S. aureus vancomycin resistance mediated through the incorporation of precursors not terminating in D-alanyl-D-alanine would be mutually exclusive with expression of mecA-mediated methicillin resistance.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-10430946, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-11418146, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1317861, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1510429, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1512190, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1597460, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-1993184, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-2045371, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-2345297, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-2806258, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-3638304, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-7034001, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-775943, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-7872753, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-7961632, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8157576, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8215264, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-825075, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8253748, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8452368, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-8478340, http://linkedlifedata.com/resource/pubmed/commentcorrection/12234837-9177719
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/Methicillin, http://linkedlifedata.com/resource/pubmed/chemical/Muramoylpentapeptide..., http://linkedlifedata.com/resource/pubmed/chemical/Penicillin-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Peptidoglycan, http://linkedlifedata.com/resource/pubmed/chemical/Peptidyl Transferases, http://linkedlifedata.com/resource/pubmed/chemical/Serine, http://linkedlifedata.com/resource/pubmed/chemical/Threonine
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0066-4804
pubmed:author
pubmed:issnType
Print
pubmed:volume
46
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3151-5
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:12234837-Amino Acids, pubmed-meshheading:12234837-Bacterial Proteins, pubmed-meshheading:12234837-Carrier Proteins, pubmed-meshheading:12234837-Chromatography, High Pressure Liquid, pubmed-meshheading:12234837-Culture Media, pubmed-meshheading:12234837-Hexosyltransferases, pubmed-meshheading:12234837-Mass Spectrometry, pubmed-meshheading:12234837-Methicillin, pubmed-meshheading:12234837-Methicillin Resistance, pubmed-meshheading:12234837-Muramoylpentapeptide Carboxypeptidase, pubmed-meshheading:12234837-Penicillin-Binding Proteins, pubmed-meshheading:12234837-Peptides, pubmed-meshheading:12234837-Peptidoglycan, pubmed-meshheading:12234837-Peptidyl Transferases, pubmed-meshheading:12234837-Serine, pubmed-meshheading:12234837-Staphylococcus aureus, pubmed-meshheading:12234837-Threonine
pubmed:year
2002
pubmed:articleTitle
The carboxyl terminus of peptidoglycan stem peptides is a determinant for methicillin resistance in Staphylococcus aureus.
pubmed:affiliation
Laboratory of Microbiology, The Rockefeller University, New York, New York 10021, USA. boudewijn.dejonge@astrazeneca.com
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.