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- W2167573728 endingPage "4802" @default.
- W2167573728 startingPage "4793" @default.
- W2167573728 abstract "ABSTRACT Staphylococci can cause a wide spectrum of infections, including endocarditis, osteomyelitis, and sepsis, which is reflected by the numerous virulence factors they produce, among them a recently identified new class of adhesins, namely, the multifunctional autolysins/adhesins. Here we report the identification and molecular characterization of Aaa, a novel autolysin/adhesin from Staphylococcus aureus . The gene encoding Aaa was cloned from the clinical isolate Staphylococcus aureus 4074. DNA sequence analysis revealed that aaa encodes a deduced protein of 334 amino acids with a predicted molecular mass of 35.8 kDa. Aaa contains three N-terminal repetitive sequences that comprise features of a peptidoglycan-binding domain, the LysM domain. The expression of aaa by Escherichia coli and its subsequent characterization revealed that Aaa possesses bacteriolytic activity as well as adhesive properties, such as binding to extracellular matrix proteins. Real-time biomolecular interaction analysis demonstrated that the interaction of Aaa with fibrinogen, fibronectin, and vitronectin is dose dependent and saturable and occurs with a high affinity. Furthermore, we demonstrate that Aaa binds to the Aα and Bβ chains of fragment D of fibrinogen. Immunofluorescence microscopy revealed that Aaa is located at the cell surface. Finally, an aaa knockout mutant showed reduced adherence to surface-adsorbed fibrinogen and fibronectin, strongly suggesting a role for Aaa in the colonization of host factor-coated polymer surfaces and/or host tissue." @default.
- W2167573728 created "2016-06-24" @default.
- W2167573728 creator A5024373557 @default.
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- W2167573728 creator A5055008734 @default.
- W2167573728 creator A5068975361 @default.
- W2167573728 date "2005-08-01" @default.
- W2167573728 modified "2023-10-16" @default.
- W2167573728 title "The Multifunctional <i>Staphylococcus aureus</i> Autolysin Aaa Mediates Adherence to Immobilized Fibrinogen and Fibronectin" @default.
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- W2167573728 doi "https://doi.org/10.1128/iai.73.8.4793-4802.2005" @default.
- W2167573728 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1201280" @default.
- W2167573728 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16040992" @default.
- W2167573728 hasPublicationYear "2005" @default.
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