Range of the antigenic specificity of peptidoglycan in Staphylococcus aureus compared to other representatives of the Staphylococcus genus

In investigations based on the use of a highly sensitive test system permitting the detection of normal human antibodies to S. aureus peptidoglycan, the antigenic relationships between the peptidoglycans of S. aureus and other representatives of the genus Staphylococcus have been studied. Among other staphylococcal species, S. simulans, S. xylosus, S. hyicus, S. cohnii, S. hyicus s. s. chromogenes have been found to possess peptidoglycans most closely related to S. aureus peptidoglycans, while S. warneri and S. epidermidis peptidoglycans have proved to be least closely related to it.     

Prooxidant and cytotoxic action of N-acetylcysteine and glutathione combined with vitamin Bl2b

We studied the prooxidant and cytotoxic action of thiols N-acetylcystein (NAC) and glutathione (GSH) combined with vitamin Bl2b. The synergism of action of the thiols and Bl2b resulted in human carcinoma cell damage was found. It was shown that GSH and NAC in physiological doses combined with Bl2b caused the initiation of apoptosis. It was established that prooxidant action of the thiols combined with vitamin Bl2b, i. e. generation and accumulation of hydrogen peroxide in culture medium, led to intracellular oxidative stress and injury of cell redox system. These effects were completely abolished by nonthiol antioxidants catalase and pyruvate. The chelators of iron phenanthroline and deferoxamine did not suppress the H2O2 accumulation in culture medium but significantly inhibited the cell death induced by the thiols combined with Bl2b. Therefore, the thiols GSH and NAC widely used as antioxidants, in combination with vitamin Bl2b show prooxidant characteristics and induce, with the participation of intracellular iron, apoptotic HEp-2 cell death.     

Passive Aseptic Calcification of Fixed Pericardial Biomaterials Is Mediated by Damage to the Structure and Microarchitectonics of Their Extracellular Matrix

Biophysics - Abstract—The mechanism of passive (independent of recipient cells) aseptic calcification of pericardial materials fixed with gluteraldehyde, which are used for the manufacture of...     

Both PA63 and PA83 are endocytosed within an anthrax protective antigen mixed heptamer: a putative mechanism to overcome a furin deficiency

Anthrax toxin consists of protective antigen (PA), and lethal (LF) and edema (EF) factors. A 83 kDa PA monomer (PA83) precursor binds to the cell receptor. Furin-like proprotein convertases (PCs) cleave PA83 to generate cell-bound 63 kDa protein (PA63). PA63 oligomerizes to form a ring-shaped heptamer that binds LF-EF and facilitates their entry into the cells. Several additional PCs, as opposed to furin alone, are capable of processing PA83. Following the incomplete processing of the available pool of PA83, the functional heptamer includes both PA83 and PA63. The available structures of the receptor-PA complex imply that the presence of either one or two molecules of PA83 will not impose structural limitations on the formation of the heptamer and the association of either the (PA83)(1)(PA63)(6) or (PA83)(2)(PA63)(5) heteroheptamer with LF-EF. Our data point to the intriguing mechanism of anthrax that appears to facilitate entry of the toxin into the cells which express limiting amounts of PCs and an incompletely processed PA83 pool.     

Staphylococcal toxic shock exotoxin (its isolation and characteristics)

The method for obtaining the preparation of toxic shock exotoxin (TSE) has been developed. This method comprises the following operations: the sorption of the toxin from the culture fluid on Amberlite CG-50, elution, dialysis, gel chromatography in a column with biogel P-2, isoelectric focusing, and gel chromatography in a column with Sephadex G-75. TSE is a relatively thermostable protein with a molecular weight of 24,000. Its isoelectric point is 7.2. Monospecific antiserum to TSE with precipitating antibody titer equal to 1:16, identical to the reference serum (M. S. Bergdoll), has been prepared. This antiserum has shown no cross reactions with the homogeneous preparations of staphylococcal enterotoxins.     

Study of the chemical and immunogenic properties of the capsular Staphylococcus aureus antigen. 2. Evaluation of the immunogenic properties of the capsular antigen in experiments in vitro

Albino mice were immunized with a purified capsular antigen isolated from the S. aureus strain 1193/74. The presence of specific anticapsular antibodies in the sera of animals were determined by two methods: 1) by conversion of diffuse growth of a homologous strain into compact one, and 2) by determination of opsonic index in phagocytosis of homologous staphylococci by human neutrophils. It was revealed that antibodies converting the microbical growth were absent in the sera of normal mice and reached the highest level after the second antigen injection; opsonins were present in the sera of normal mice in widely varying quantities; their maximal level was noted after the 3rd immunization.     

Serologic and immunogenic properties of staphylococcal protein A]

Protein antigen A was isolated from the microbial cells of Cowan I strain of Staphylococcus aureus by hot extraction method. Ion exchange chromatography on DEAE-cellulose-32 and gel-filtration on sephadex F-100 were used for purification of protein A. Microprecipitation in agar test against homologous immune rabbit serum and normal human serum showed purified protein A to be identical by serological specificity to the standard preparation obtained from Prof. Oeding's laboratory. In order to assess the immunogenic properties of protein A by various doses of the preparation (from 2 to 1000 microgram) mixed with A1 (OH)3 albino mice were immunized and then infected with the microbial culture of the homologous strain. As revealed, protein A not only failed to protect the animals from death, but even aggravated the course of infection.     

Quantitative indices of lysozyme activity in staphylococci]

The lysozyme activity of 354 lysozyme-positive and 100 lysozyme-negative (by the results of qualitative test) staphylococcus strains were studied quantitatively. The method was based on titration of the lysozyme in the culture fluid of 48-hour broth cultures of the strains under study. The quantitative method proved to be more sensitive than the qualitative one, and permitted to reveal the lysozyme production in 71% of the strains which were formerly considered to be lysozyme-negative. There were distinct species differences between the lysozyme-positive staphylococci: the mean lysozyme level in the S. aureus was significantly greater then in the S. epidermis. There was no regular association between the lysozyme activity, staphylococcus origin, bacteriophage reference and the antibiotic resistance.