Emergence of coagulase-negative staphylococci

Becker, Karsten; Both, Anna; Weißelberg, Samira; Heilmann, Christine; Rohde, Holger

doi:10.1080/14787210.2020.1730813

Cited by 87 publications

(118 citation statements)

References 205 publications

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“…late, MR-CNSs are commonly prevalent in indoor/outdoor environments of hospitals and communities [13,39,40]. Apart from frequently associated with nosocomial infections, these infectious agents are also of great concern in a variety of indoor environments such as libraries, offices and other residential indoors [10,34].…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, Staphylococci species are the rapidly emerging threat to human health, particularly CNSs are largely implicated in skin and soft tissue infections (SSTIs) such as in patients with burns and have undergone surgeries [12,20]. CNS species frequently found responsible for infecting wounds and medical implants inside a hospital include: Staphylococcus capiti, Staphylococcus haemolyticus, Staphylococcus epidermidis, Staphylococcus lugdunensis, Staphylococcus hominis, Staphylococcus saprophyticus, Staphylococcus simulans and Staphylococcus auricularis [39,56].…”

Section: Discussionmentioning

confidence: 99%

“…CNSs are the common microflora of human skin, however, they can be pathogenic and virulent if they colonizes the open wounds. Of late, MR-CNSs are commonly prevalent in indoor/outdoor environments of hospitals and communities [ 13 , 39 , 40 ].…”

Section: Discussionmentioning

confidence: 99%

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Prevalence and antibiogram of coagulase negative Staphylococci in bioaerosols from different indoors of a university in India

et al. 2020

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Prevalence and antibiogram of coagulase negative Staphylococci in bioaerosols from different indoors of a university in India

et al. 2020

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“…This also makes them an interesting object of research into the possibilities for inducing food poisoning due to their ability to produce enterotoxins. Studies conducted on clinical strains have provided evidence suggesting that certain CoNS strains may be major hospital pathogens [ 3 , 4 ]. These include strains capable of producing superantigenic toxins such as staphylococcal enterotoxins (SE), toxic shock syndrome toxin-1 (TSST-1) and other toxins, including hemolysins, coagulase and exfoliative toxins [ 5 ].…”

Section: Introductionmentioning

confidence: 99%

Enterotoxigenic Potential of Coagulase-Negative Staphylococci from Ready-to-Eat Food

Chajęcka‐Wierzchowska

Gajewska

Wiśniewski

et al. 2020

Pathogens

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Although coagulase-positive staphylococci are considered to be the main factor responsible for food poisoning, an increasing role for the coagulase-negative staphylococci in the production of enterotoxins has been observed in recent years. This study was conducted to assess the occurrence of genes responsible for the production of staphylococcal enterotoxins (SE), enterotoxin-like toxins (SEI) and toxic shock syndrome toxin-1 (TSST-1) in coagulase-negative staphylococci (CoNS) isolated from ready-to-eat food from bars and restaurants. One hundred and eighteen CoNS strains were tested using polymerase chain reaction (PCR) to five superantigenic toxin genes, including five different types of classical enterotoxins (sea, seb, sec, sed and see) and the toxic shock syndrome toxin-1 (tsst-1) as well as to supertoxin-like genes. PCR-positive isolates were then tested using immunoenzymatic methods (SET-RPLA, Vidas SET 2) for toxin expression. Out of 118 CoNS strains, the presence of staphylococcal enterotoxins was confirmed in 72% of them. The most frequently found enterotoxin-like genotype was ser, selu. Two of the tested strains had up to ten different enterotoxin genes in the genome at the same time. Although no production of enterotoxins was detected in the CoNS, which means that their possible role in the epidemiology of food-borne diseases is minimal, the data demonstrated that the toxigenic capacity of the CoNS should not be ignored, and that this group of microorganisms should be continuously monitored in food.

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“…Infections typically occur after implantation of medical devices, e.g., central venous catheters, prosthetic heart valves, or prosthetic joints. Being usually considered a harmless skin commensal, the selective pathogenic potential of S. epidermidis in foreign-material associated infections is related to the pronounced biofilm forming ability of this species ( 3 ). Biofilm formation protects S. epidermidis from effectors of the host immune system and induces phenotypic resistance even against antimicrobial agents that have been tested susceptible under standard laboratory conditions ( 4 – 6 ).…”

Section: Introductionmentioning

confidence: 99%

A Giant Extracellular Matrix Binding Protein of Staphylococcus epidermidis Binds Surface-Immobilized Fibronectin via a Novel Mechanism

Büttner

Perbandt

Kohler³

et al. 2020

mBio

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Although it is normally an innocuous part of the human skin microbiota, Staphylococcus epidermidis has emerged as a major nosocomial pathogen, and implanted foreign materials are an essential risk factor for the development of an infection. The extraordinary efficiency of S. epidermidis to colonize artificial surfaces is particularly related to the ability to form biofilms. Biofilm formation itself critically depends on stable pathogen binding to extracellular host matrix components, e.g. fibronectin (Fn), covering inserted devices in vast amounts. Extracellular matrix binding protein (Embp) and its subdomains referred to as the F-repeat and the FG-repeat are critical for adherence of S. epidermidis to surface-immobilized Fn. Embp-Fn interactions preferentially occur with surface-bound, but not folded, globular Fn via binding to the F3 domain. High-resolution structure analysis of F- and FG-repeats revealed that both repeats are composed of two tightly connected triple α-helix bundles, exhibiting an elongated but rather rigid structural organization in solution. Both F- and FG-repeat possess Fn-binding capacity via interactions with type III subdomain FN12, involving residues within the C and F β-sheet. FN12 essentially supports stability of the globular Fn state, and thus these findings reasonably explain why Embp-mediated interaction of S. epidermidis necessitates Fn surface immobilization. Thus, Embp employs an uncharacterized bacterial Fn-binding mechanism to promote staphylococcal adherence. IMPORTANCE Staphylococcus epidermidis is a leading pathogen in implant-associated hospital infections. The pathogenesis critically depends on bacterial binding to ECM components, specifically fibronectin (Fn). The cell surface-localized, 1-MDa extracellular matrix binding protein (Embp) is essentially characterized by 10 F- and 40 FG-repeats. These repetitive units, each characterized by two α-helical bundles, organize themselves in a rigid, elongated form. Embp binds preferentially to surface-localized but not soluble Fn, with both F- and FG-repeats being sufficient for Fn binding and resulting bacterial adherence. Binding preferentially involves Fn type III domain, specifically residues of FN12 β-sheets C and F. Both play key role in stabilizing the globular Fn conformation, explaining the necessity of Fn surface immobilization for a subsequent interaction with Embp. In comparison to many other bacterial Fn-binding proteins using the Fn N terminus, Embp employs a previously undescribed mechanism supporting the adhesion of S. epidermidis to surface-immobilized Fn.

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Emergence of coagulase-negative staphylococci

Cited by 87 publications

References 205 publications

Prevalence and antibiogram of coagulase negative Staphylococci in bioaerosols from different indoors of a university in India

Prevalence and antibiogram of coagulase negative Staphylococci in bioaerosols from different indoors of a university in India

Enterotoxigenic Potential of Coagulase-Negative Staphylococci from Ready-to-Eat Food

A Giant Extracellular Matrix Binding Protein of Staphylococcus epidermidis Binds Surface-Immobilized Fibronectin via a Novel Mechanism

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