دورية أكاديمية

An extracellular Staphylococcus epidermidis polysaccharide: relation to Polysaccharide Intercellular Adhesin and its implication in phagocytosis

التفاصيل البيبلوغرافية
العنوان: An extracellular Staphylococcus epidermidis polysaccharide: relation to Polysaccharide Intercellular Adhesin and its implication in phagocytosis
المؤلفون: Spiliopoulou Anastasia I, Krevvata Maria I, Kolonitsiou Fevronia, Harris Llinos G, Wilkinson Thomas S, Davies Angharad P, Dimitracopoulos Georgios O, Karamanos Nikos K, Mack Dietrich, Anastassiou Evangelos D
المصدر: BMC Microbiology, Vol 12, Iss 1, p 76 (2012)
بيانات النشر: BMC
سنة النشر: 2012
المجموعة: Directory of Open Access Journals: DOAJ Articles
مصطلحات موضوعية: Microbiology, QR1-502
الوصف: Background The skin commensal and opportunistic pathogen Staphylococcus epidermidis is a leading cause of hospital-acquired and biomaterial-associated infections. The polysaccharide intercellular adhesin (PIA), a homoglycan composed of β-1,6-linked N-acetylglucosamine residues, synthesized by enzymes encoded in icaADBC is a major functional factor in biofilm accumulation, promoting virulence in experimental biomaterial-associated S. epidermidis infection. Extracellular mucous layer extracts of S. epidermidis contain another major polysaccharide, referred to as 20-kDa polysaccharide (20-kDaPS), composed mainly out of glucose, N-acetylglucosamine, and being partially sulfated. 20-kDaPS antiserum prevents adhesion of S . epidermidis on endothelial cells and development of experimental keratitis in rabbits. Here we provide experimental evidence that 20-kDaPS and PIA represent distinct molecules and that 20-kDaPS is implicated in endocytosis of S . epidermidis bacterial cells by human monocyte-derived macrophages. Results Analysis of 75 clinical coagulase-negative staphylococci from blood-cultures and central venous catheter tips indicated that 20-kDaPS is expressed exclusively in S. epidermidis but not in other coagulase-negative staphylococcal species. Tn 917 -insertion in various locations in icaADBC in mutants M10, M22, M23, and M24 of S. epidermidis 1457 are abolished for PIA synthesis, while 20-kDaPS expression appears unaltered as compared to wild-type strains using specific anti-PIA and anti-20-kDaPS antisera. While periodate oxidation and dispersin B treatments abolish immuno-reactivity and intercellular adhesive properties of PIA, no abrogative activity is exerted towards 20-kDaPS immunochemical reactivity following these treatments. PIA polysaccharide I-containing fractions eluting from Q-Sepharose were devoid of detectable 20-kDaPS using specific ELISA. Preincubation of non-20-kDaPS-producing clinical strain with increasing amounts of 20-kDaPS inhibits endocytosis by human macrophages, whereas, ...
نوع الوثيقة: article in journal/newspaper
اللغة: English
تدمد: 1471-2180
العلاقة: http://www.biomedcentral.com/1471-2180/12/76Test; https://doaj.org/toc/1471-2180Test; https://doaj.org/article/b134a7c1f2874d04bd6effcc7ab723e3Test
DOI: 10.1186/1471-2180-12-76
الإتاحة: https://doi.org/10.1186/1471-2180-12-76Test
https://doaj.org/article/b134a7c1f2874d04bd6effcc7ab723e3Test
رقم الانضمام: edsbas.DECA00D9
قاعدة البيانات: BASE
الوصف
تدمد:14712180
DOI:10.1186/1471-2180-12-76