Growth phase-dependent production of a cell wall-associated elastinolytic cysteine proteinase by Staphylococcus epidermidis.

Staphylococcus epidermidis, a Gram-positive, coagulase-negative bacterium is a predominant inhabitant of human skin and mucous membranes. Recently, however, it has become one of the most important agents of hospital-acquired bacteriemia, as it has been found to be responsible for surgical wound infections developed in individuals with indwelling catheters or prosthetic devices, as well as in immunosupressed or neutropenic patients. Despite their medical significance, little is known about proteolytic enzymes of S.

The Staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease.

Staphostatins are the endogenous inhibitors of the major secreted cysteine proteases of Staphylococcus aureus, the staphopains. Our recent crystal structure of staphostatin B has shown that this inhibitor forms a mixed, eight-stranded beta-barrel with statistically significant similarity to lipocalins, but not to cystatins. We now present the 1.

Proteolysis of interleukin-6 receptor (IL-6R) by Porphyromonas gingivalis cysteine proteinases (gingipains) inhibits interleukin-6-mediated cell activation.

Current consensus is that periodontitis is an infectious disease in which a deregulated chronic inflammatory reaction not only may lead to periodontal tissue damage but also eventually may cause tooth loss. In controlling the inflammatory state the interplay between a network of cytokines and their receptors plays an important role. Here we show that the interleukin-6 receptor (IL-6R) is rapidly and efficiently inactivated by gingipains, the arginine- (HRgpA and RgpB) and lysine- (Kgp) specific cysteine proteinases from Porphyromonas gingivalis.