scholarly journals Essential Functional Role of the Polysaccharide Intercellular Adhesin of Staphylococcus epidermidis in Hemagglutination

1999 ◽  
Vol 67 (2) ◽  
pp. 1004-1008 ◽  
Author(s):  
Dietrich Mack ◽  
Joachim Riedewald ◽  
Holger Rohde ◽  
Tim Magnus ◽  
Hubert H. Feucht ◽  
...  

ABSTRACT Hemagglutination of erythrocytes is a common property ofStaphylococcus epidermidis strains, which is related to adherence and biofilm formation and may be essential for the pathogenesis of biomaterial-associated infections caused byS. epidermidis. In three independent biofilm-producing, hemagglutination-positive S. epidermidis isolates, interruption of the icaADBC operon essential for polysaccharide intercellular adhesin (PIA) synthesis by Tn917 insertions led to a hemagglutination-negative phenotype. An immunoglobulin G fraction of antiserum to PIA greatly reduced hemagglutination. Purified PIA led to a 64-fold decrease of hemagglutination titers of these strains; however, it did not mediate hemagglutination by itself. These observations define PIA as the hemagglutinin of S. epidermidis or at least as its major functional component.

Biofilms ◽  
2004 ◽  
Vol 1 (2) ◽  
pp. 101-106 ◽  
Author(s):  
S. Dobinsky ◽  
H. Rohde ◽  
J. K.-M. Knobloch ◽  
M. A. Horstkotte ◽  
D. Mack

Biofilm-formation in Staphylococcus epidermidis depends on the expression of the icaADBC operon encoding the enzymes required for the synthesis of polysaccharide intercellular adhesin (PIA). Different S. epidermidis strains vary widely in the degree of PIA and biofilm that they produce. In 11 clinical S. epidermidis strains we analyzed the biofilm-forming capacity in relation to the amount of ica expressed in static biofilm cultures. In mid-exponential growth phase no correlation could be detected between the level of ica transcription and the biofilm-forming phenotype. When the different strains were grown under conditions leading to a biofilm-negative phenotype, ica-expression was highly upregulated. Sequence analysis demonstrated that the observed differences were not due to major mutations in the ica promoter region but apparently to other strain-specific regulators.


2004 ◽  
Vol 186 (8) ◽  
pp. 2449-2456 ◽  
Author(s):  
Kimberly K. Jefferson ◽  
Danielle B. Pier ◽  
Donald A. Goldmann ◽  
Gerald B. Pier

ABSTRACT Infections involving Staphylococcus aureus are often more severe and difficult to treat when the organism assumes a biofilm mode of growth. The polysaccharide poly-N-acetylglucosamine (PNAG), also known as polysaccharide intercellular adhesin, is synthesized by the products of the intercellular adhesin (ica) locus and plays a key role in biofilm formation. Numerous conditions and exogenous factors influence ica transcription and PNAG synthesis, but the regulatory factors and pathways through which these environmental stimuli act have been only partially characterized. We developed a DNA affinity chromatography system to purify potential regulatory proteins that bind to the ica promoter region. Using this technique, we isolated four proteins, including the staphylococcal gene regulator SarA, a MarR family transcriptional regulator of the teicoplanin-associated locus TcaR, DNA-binding protein II, and topoisomerase IV, that bound to the ica promoter. Site-directed deletion mutagenesis of tcaR indicated that TcaR was a negative regulator of ica transcription, but deletion of tcaR alone did not induce any changes in PNAG production or in adherence to polystyrene. We also investigated the role of IcaR, encoded within the ica locus but divergently transcribed from the biosynthetic genes. As has been shown previously in Staphylococcus epidermidis, we found that IcaR was also a negative regulator of ica transcription in S. aureus. We also demonstrate that mutation of icaR augmented PNAG production and adherence to polystyrene. Transcription of the ica locus, PNAG production, and adherence to polystyrene were further increased in a tcaR icaR double mutant. In summary, TcaR appeared to be a weak negative regulator of transcription of the ica locus, whereas IcaR was a strong negative regulator, and in their absence PNAG production and biofilm formation were enhanced.


2001 ◽  
Vol 183 (8) ◽  
pp. 2624-2633 ◽  
Author(s):  
Johannes K.-M. Knobloch ◽  
Katrin Bartscht ◽  
Axel Sabottke ◽  
Holger Rohde ◽  
Heinz-Hubert Feucht ◽  
...  

ABSTRACT Staphylococcus epidermidis is a common pathogen in medical device-associated infections. Its major pathogenetic factor is the ability to form adherent biofilms. The polysaccharide intercellular adhesin (PIA), which is synthesized by the products of theicaADBC gene cluster, is essential for biofilm accumulation. In the present study, we characterized the gene locus inactivated by Tn917 insertions of two isogenic,icaADBC-independent, biofilm-negative mutants, M15 and M19, of the biofilm-producing bacterium S. epidermidis 1457. The insertion site was the same in both of the mutants and was located in the first gene, rsbU, of an operon highly homologous to thesigB operons of Staphylococcus aureus andBacillus subtilis. Supplementation of Trypticase soy broth with NaCl (TSBNaCl) or ethanol (TSBEtOH), both of which are known activators of sigB, led to increased biofilm formation and PIA synthesis by S. epidermidis 1457. Insertion of Tn917 into rsbU, a positive regulator of alternative sigma factor ςB, led to a biofilm-negative phenotype and almost undetectable PIA production. Interestingly, in TSBEtOH, the mutants were enabled to form a biofilm again with phenotypes similar to those of the wild type. In TSBNaCl, the mutants still displayed a biofilm-negative phenotype. No difference in primary attachment between the mutants and the wild type was observed. Similar phenotypic changes were observed after transfer of the Tn917 insertion of mutant M15 to the independent and biofilm-producing strain S. epidermidis8400. In 11 clinical S. epidermidis strains, a restriction fragment length polymorphism of the sigB operon was detected which was independent of the presence of theicaADBC locus and a biofilm-positive phenotype. Obviously, different mechanisms are operative in the regulation of PIA expression in stationary phase and under stress induced by salt or ethanol.


2020 ◽  
Vol 9 (2) ◽  
pp. 78-88
Author(s):  
Mulugeta Mulat ◽  
Raksha Anand ◽  
Fazlurrahman Khan

The diversity of indole concerning its production and functional role has increased in both prokaryotic and eukaryotic systems. The bacterial species produce indole and use it as a signaling molecule at interspecies, intraspecies, and even at an interkingdom level for controlling the capability of drug resistance, level of virulence, and biofilm formation. Numerous indole derivatives have been found to play an important role in the different systems and are reported to occur in various bacteria, plants, human, and plant pathogens. Indole and its derivatives have been recognized for a defensive role against pests and insects in the plant kingdom. These indole derivatives are produced as a result of the breakdown of glucosinolate products at the time of insect attack or physical damages. Apart from the defensive role of these products, in plants, they also exhibit several other secondary responses that may contribute directly or indirectly to the growth and development. The present review summarized recent signs of progress on the functional properties of indole and its derivatives in different plant systems. The molecular mechanism involved in the defensive role played by indole as well as its’ derivative in the plants has also been explained. Furthermore, the perspectives of indole and its derivatives (natural or synthetic) in understanding the involvement of these compounds in diverse plants have also been discussed.


2016 ◽  
Vol 81 (8) ◽  
pp. 835-857 ◽  
Author(s):  
Y. L. Dorokhov ◽  
E. V. Sheshukova ◽  
E. N. Kosobokova ◽  
A. V. Shindyapina ◽  
V. S. Kosorukov ◽  
...  

2005 ◽  
Vol 73 (5) ◽  
pp. 3188-3191 ◽  
Author(s):  
Hualin Li ◽  
Lin Xu ◽  
Jianping Wang ◽  
Yumei Wen ◽  
Cuong Vuong ◽  
...  

ABSTRACT To test if biofilm formation in Staphylococcus epidermidis is dependent on the polysaccharide intercellular adhesin, whose biosynthesis is driven by the ica locus, a plasmid containing the ica locus was transferred to three ica-negative strains. Using in vitro biofilm assays and a rat central venous catheter infection model, we confirmed the importance of the ica locus for biofilm production and pathogenesis of S. epidermidis.


PLoS ONE ◽  
2013 ◽  
Vol 8 (6) ◽  
pp. e67240 ◽  
Author(s):  
Florent Valour ◽  
Sophie Trouillet-Assant ◽  
Jean-Philippe Rasigade ◽  
Sébastien Lustig ◽  
Emmanuel Chanard ◽  
...  

Microbiology ◽  
2016 ◽  
Vol 85 (4) ◽  
pp. 506-508
Author(s):  
D. V. Eroshenko ◽  
T. V. Polyudova ◽  
V. P. Korobov

2009 ◽  
Vol 191 (22) ◽  
pp. 7007-7016 ◽  
Author(s):  
Robin L. Macintosh ◽  
Jane L. Brittan ◽  
Ritwika Bhattacharya ◽  
Howard F. Jenkinson ◽  
Jeremy Derrick ◽  
...  

ABSTRACT The opportunistic pathogen Staphylococcus epidermidis colonizes indwelling medical devices by biofilm formation but is primarily a skin resident. In many S. epidermidis strains biofilm formation is mediated by a cell wall-anchored protein, the accumulation-associated protein (Aap). Here, we investigate the role of Aap in skin adhesion. Aap is an LPXTG protein with a domain architecture including a terminal A domain and a B-repeat region. S. epidermidis NCTC 11047 expresses Aap as localized, lateral tufts of fibrils on one subpopulation of cells (Fib+), whereas a second subpopulation does not express these fibrils of Aap (Fib−). Flow cytometry showed that 72% of NCTC 11047 cells expressed Aap and that 28% of cells did not. Aap is involved in the adhesion of Fib+ cells to squamous epithelial cells from the hand (corneocytes), as the recombinant A-domain protein partially blocked binding to corneocytes. To confirm the role of the Aap A domain in corneocyte attachment, Aap was expressed on the surface of Lactococcus lactis MG1363 as sparsely distributed, peritrichous fibrils. The expression of Aap increased corneocyte adhesion 20-fold compared to L. lactis carrying Aap without an A domain. S. epidermidis isolates from catheters, artificial joints, skin, and the nose also used the A domain of Aap to adhere to corneocytes, emphasizing the role of Aap in skin adhesion. In addition, L. lactis expressing Aap with different numbers of B repeats revealed a positive correlation between the number of B repeats and adhesion to corneocytes, suggesting an additional function for the B region in enhancing A-domain-dependent attachment to skin. Therefore, in addition to its established role in biofilm formation, Aap can also promote adhesion to corneocytes and is likely to be an important adhesin in S. epidermidis skin colonization.


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