staphylococcal infections/protease

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Staphylococcus aureus infection triggers production of neutralizing, V8 protease-specific antibodies.

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Staphylococcus aureus infection triggers polyclonal B-cell activation. It was sought to further characterize the hypergammaglobulinemia seen in Staphylococcus aureus infection, focusing on the significance of protease-specific B-cell responses. Sera from mice infected with Staphylococcus aureus

[Protease inhibitors as immunomodulators in experimental acute pancreatitis and staphylococcal infection].

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The influence of protease-inhibiting preparations on the development of humoral immune response in diseases involving the development of secondary immunodeficiency (experimentally induced acute pancreatitis and staphylococcal infection) has been studied. Five injections of contrycal and

msaABCR operon positively regulates biofilm development by repressing proteases and autolysis in Staphylococcus aureus.

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Staphylococcus aureus is an important human pathogen that causes nosocomial and community-acquired infections. One of the most important aspects of staphylococcal infections is biofilm development within the host, which renders the bacterium resistant to the host's immune response and antimicrobial

Structure and protective efficacy of the Staphylococcus aureus autocleaving protease EpiP.

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Despite the global medical needs associated with Staphylococcus aureus infections, no licensed vaccines are currently available. We identified and characterized a protein annotated as an epidermin leader peptide processing serine protease (EpiP), as a novel S. aureus vaccine candidate. In addition,

Degradation of fibrinogen and collagen by staphopains, cysteine proteases released from Staphylococcus aureus.

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Staphylococcus aureus is the most frequently isolated pathogen in gram-positive sepsis often complicated by a blood clotting disorder, and is the leading cause of infective endocarditis induced by bacterial destruction of endocardial tissues. The bacterium secretes cysteine proteases referred to as

Roles of the Site 2 Protease Eep in Staphylococcus aureus

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In Enterococcus faecalis, the site 2 protease Eep generates sex pheromones, including cAM373. Intriguingly, in Staphylococcus aureus, a peptide similar to cAM373, named cAM373_SA, is produced from the camS gene. Here, we report that the staphylococcal Eep homolog is not only

Staphylococcus aureus protects its immune-evasion proteins against degradation by neutrophil serine proteases.

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Neutrophils store large quantities of neutrophil serine proteases (NSPs) that contribute, via multiple mechanisms, to antibacterial immune defences. Even though neutrophils are indispensable in fighting Staphylococcus aureus infections, the importance of NSPs in anti-staphylococcal defence is yet

A peptide immunization approach to counteract a Staphylococcus aureus protease defense against host immunity.

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Pathogens that induce acute and chronic infections, as well as certain cancers, employ numerous strategies to thwart host cellular and humoral immune defenses. One proposed evasion mechanism against humoral immunity is a localized expression of extracellular proteases that cleave the IgG hinge and

Staphylococcus aureus proteases degrade lung surfactant protein A potentially impairing innate immunity of the lung.

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The pulmonary surfactant is a complex mixture of lipids and proteins that is important for respiratory lung functions, which also provides the first line of innate immune defense. Pulmonary surfactant protein-A (SP-A) is a major surfactant component with immune functions with importance during

A secreted bacterial protease tailors the Staphylococcus aureus virulence repertoire to modulate bone remodeling during osteomyelitis.

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Osteomyelitis is a common manifestation of invasive Staphylococcus aureus infection. Pathogen-induced bone destruction limits antimicrobial penetration to the infectious focus and compromises treatment of osteomyelitis. To investigate mechanisms of S. aureus-induced bone destruction, we developed a

Clp chaperones and proteases are central in stress survival, virulence and antibiotic resistance of Staphylococcus aureus.

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Intracellular proteolysis carried out by energy-dependent proteases is one of the most conserved biological processes. In all cells proteolysis maintains and shapes the cellular proteome by ridding the cell of damaged proteins and by regulating abundance of functional proteins such as regulatory

Defense against own arms: staphylococcal cysteine proteases and their inhibitors.

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Staphylococcus aureus is a human pathogen causing a wide range of diseases. Most staphylococcal infections, unlike those caused by other bacteria are not toxigenic and very little is known about their pathogenesis. It has been proposed that a core of secreted proteins common to many infectious

Staphylococcus aureus secretes a unique class of neutrophil serine protease inhibitors.

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Neutrophils are indispensable for clearing infections with the prominent human pathogen Staphylococcus aureus. Here, we report that S. aureus secretes a family of proteins that potently inhibits the activity of neutrophil serine proteases (NSPs): neutrophil elastase (NE), proteinase 3, and cathepsin

Clumping factor A-mediated virulence during Staphylococcus aureus infection is retained despite fibrinogen depletion.

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Clumping factor A (ClfA), a fibrinogen-binding protein expressed on the Staphylococcus aureus cell surface, has previously been shown to act as a virulence factor in experimental septic arthritis. Although the interaction between ClfA and fibrinogen is assumed to be of importance for the virulence

[Immunostimulating and protective effects of terrilytin preparations in staphylococcal infection].

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In mice infected with staphylococci there was observed less pronounced development of the immune response to sheep red blood cells (SRBC) than in intact animals subjected only to immunization. Administration of free terrilytin to the infected mice increased the immune response development induced by

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