Linked Life Data

10878118

Source:http://linkedlifedata.com/resource/pubmed/id/10878118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-8-30
pubmed:databankReference
pubmed:abstractText
Staphylococcus epidermidis can express three different cell-surface-associated proteins, designated SdrF, SdrG and SdrH, that contain serine-aspartate dipeptide repeats. Proteins SdrF and SdrG are similar in sequence and structural organization to the Sdr proteins of Staphylococcus aureus and comprise unique 625- and 548-residue A regions at their N termini, respectively, followed by 110-119-residue B-repeat regions and SD-repeat regions. The C termini contain LPXTG motifs and hydrophobic amino acid segments characteristic of surface proteins covalently anchored to peptidoglycan. In contrast, SdrH has a short 60-residue A region at its N terminus followed by a SD-repeat region, a unique 277-residue C region and a C-terminal hydrophobic segment. SdrH lacks a LPXTG motif. Recombinant proteins representing the A regions of SdrF, SdrG and SdrH were expressed and purified from Escherichia coli. Antisera specific to these proteins were raised in rabbits and used to identify Sdr proteins expressed by S. epidermidis. Only SdrF was released from lysostaphin-generated protoplasts of cells grown to late-exponential phase. SdrG and SdrH remained associated with the protoplast fraction and thus appear to be ineffectively sorted along the conventional pathway used for cell-wall-anchored proteins. In Southern hybridization analyses, the sdrG and sdrH genes were present in all 16 strains tested, whilst sdrF was present in 12 strains. Antisera from 16 patients who had recovered from S. epidermidis infections contained antibodies that reacted with recombinant A regions of SdrG and SdrH, suggesting that these proteins can be expressed during infection.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
146 ( Pt 7)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1535-46
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10878118-Anti-Bacterial Agents, pubmed-meshheading:10878118-Bacterial Adhesion, pubmed-meshheading:10878118-Bacterial Proteins, pubmed-meshheading:10878118-Blotting, Southern, pubmed-meshheading:10878118-Blotting, Western, pubmed-meshheading:10878118-Cloning, Molecular, pubmed-meshheading:10878118-DNA Primers, pubmed-meshheading:10878118-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10878118-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:10878118-Escherichia coli, pubmed-meshheading:10878118-Gene Expression Regulation, Bacterial, pubmed-meshheading:10878118-Genes, Bacterial, pubmed-meshheading:10878118-Humans, pubmed-meshheading:10878118-Immune Sera, pubmed-meshheading:10878118-Lysostaphin, pubmed-meshheading:10878118-Membrane Proteins, pubmed-meshheading:10878118-Molecular Sequence Data, pubmed-meshheading:10878118-Peptides, pubmed-meshheading:10878118-Recombinant Proteins, pubmed-meshheading:10878118-Staphylococcus aureus, pubmed-meshheading:10878118-Staphylococcus epidermidis
pubmed:year
2000
pubmed:articleTitle
The serine-aspartate repeat (Sdr) protein family in Staphylococcus epidermidis.
pubmed:affiliation
Institute of Biosciences and Technology, Texas Medical Center, 2121 West Holcombe Boulevard, Houston, TX 77030-3303, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't