1996
DOI: 10.1128/iai.64.9.3893-3896.1996
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The hemagglutinin of Staphylococcus saprophyticus is a major adhesin for uroepithelial cells

Abstract: The 160-kDa hemagglutinin of Staphylococcus saprophyticus also serves as a fibronectin-binding protein, and the two activities may be present on different parts of the molecule. Bacteria expressing the 160-kDa hemagglutinin bound in large numbers to histological sections of human ureters, whereas nonhemagglutinating bacteria did not bind. Binding was decreased by an antiserum to the 160-kDa protein and by a preparation of sheep erythrocyte membranes. Fibronectin had no effect. We therefore conclude that bindin… Show more

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Cited by 31 publications
(7 citation statements)
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“…The homologous autolysin/adhesins from other coagulase‐negative staphylococcal species, such as Aas from S. saprophyticus and AtlC from Staphylococcus caprae have been shown to bind to Fn (Hell et al ., 1998; Allignet et al ., 2001). Aas also binds to human uroepithelia and agglutinates sheep erythrocytes (Meyer et al ., 1996). Recently, the Atl homologues of further coagulase‐negative staphylococci have been characterized for their bacteriolytic activities, such as the AtlL of Staphylococcus lugdunensis (Bourgeois et al ., 2009) and Atl WM of Staphylococcus warneri M (Yokoi et al ., 2008).…”
Section: Introductionmentioning
confidence: 99%
“…The homologous autolysin/adhesins from other coagulase‐negative staphylococcal species, such as Aas from S. saprophyticus and AtlC from Staphylococcus caprae have been shown to bind to Fn (Hell et al ., 1998; Allignet et al ., 2001). Aas also binds to human uroepithelia and agglutinates sheep erythrocytes (Meyer et al ., 1996). Recently, the Atl homologues of further coagulase‐negative staphylococci have been characterized for their bacteriolytic activities, such as the AtlL of Staphylococcus lugdunensis (Bourgeois et al ., 2009) and Atl WM of Staphylococcus warneri M (Yokoi et al ., 2008).…”
Section: Introductionmentioning
confidence: 99%
“…There are 8 additional nonsynonymous polymorphisms in the fibronectin binding domain; however, none are as highly associated with human-pathogenic isolates. Adhesins such as Aas are important in the pathogenesis of S. saprophyticus urinary tract infections, and the gene encoding Aas has been previously implicated as a virulence factor ( 9 , 31 , 32 ).…”
Section: Resultsmentioning
confidence: 99%
“…UafA and Aas are found in all isolates, suggesting that they play important roles in the diverse niches occupied by S. saprophyticus . Aas has autolytic, fibronectin binding, and hemagluttinating functions ( 9 , 31 , 32 , 59 ). We identified a single, nonsynonymous polymorphism as a target of selection in the fibronectin binding repeats of Aas .…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…S. saprophyticus is primarily a pathogen of the urinary tract, and the factors involved in the mediation of UTI caused by S. saprophyticus are relatively well studied. S. saprophyticus possesses various types of adhesins such as hemagglutinins, autolysin Ass, and surface-associated lipases such as Ssp, which facilitate effective bacterial adherence to fibronectin and fibrinogen and, hence, colonization of the uroepithelium [12][13][14]. It can also form a bacterial biofilm, which confers an anti-phagocytic and antimicrobial-resistance phenotype and increases the virulence of the bacteria [15].…”
Section: Discussionmentioning
confidence: 99%