6533b7defe1ef96bd1275e7c
RESEARCH PRODUCT
Cloning of aas, a gene encoding a Staphylococcus saprophyticus surface protein with adhesive and autolytic properties.
Wolfgang HellSören GatermannHeinz-georg W. Meyersubject
DNA BacterialStaphylococcusMolecular Sequence DataBiologyMicrobiologyHomology (biology)BacteriolysisAmino Acid SequenceCloning MolecularAdhesins BacterialMolecular BiologyGenePeptide sequenceAllelesStaphylococcus saprophyticusBinding SitesBase SequenceAutolysinSequence Analysis DNAbiology.organism_classificationMolecular biologyFibronectinsBacterial adhesinOpen reading frameSubcloningHemagglutininsBiochemistryGenes Bacterialdescription
A gene encoding a novel cell wall-associated protein of Staphylococcus saprophyticus that binds fibronectin and to sheep erythrocytes has been cloned and sequenced. The 4392 bp open reading frame codes for an amino acid sequence that is quite similar to the Atl, an autolysin, of Staphylococcus aureus and to the AtlE of S. epidermidis. The two regions of most pronounced homology code for an N-acetyl-muramyl-L-alanine amidase and for an endo-beta-N-acetyl-D-glucosaminidase. The cloned protein lysed cells of S. saprophyticus and Micrococcus luteus exogenously. Subcloning localized the enzymatic activities to the regions of high homology and demonstrated that the interposed sequence is responsible for the adhesive activities. Two allelic replacement mutants were constructed that lacked autolytic activity and adhesive properties. The N-terminal portion of the protein contains seven highly conserved, contiguous repeats with no similarity to published sequences. It lacks the motifs typical of Gram-positive surface proteins and shows a different overall organization. This autolysin/adhesin of S. saprophyticus (Aas) appears to represent a new class of staphylococcal adhesins.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1998-08-01 | Molecular microbiology |