Исследование методов декомпозиции моделей системы функционирования книжно-журнальных изданий с измененяемым информационным наполнением

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The carbohydrate recognition domain of collectins

Collectins are effector molecules of the innate immune system that play an important role in the first line of defence against bacteria, viruses and fungi. Most of their interactions with microorganisms are mediated through their carbohydrate recognition domain (CRD), which binds in a Ca2+-dependent manner to glycoconjugates. This domain is a well-known structure that is present in a larger group of proteins comprising the C-type lectin domain family. Collectins form a subgroup within this family based on the presence of a collagen domain and the trimerization of CRDs, which are essential for the ligand-binding properties of these proteins. The ligand specificity among the nine collectin members is significantly different as a result of both the structural organization of the trimers and specific sequence changes in the binding pocket of the CRD. In addition, some collectin members have additional features, such as N-linked glycosylation of CRD residues and additional loop structures within the CRD that have a large impact on their interaction with the glycoconjugates present on microorganisms or host cells. The availability of crystal structures of three members of the collectin family (surfactant proteins A and D and mannanbinding protein) provides an important tool for addressing the impact of these CRD differences on ligand binding. In this review, the structural differences and similarities between the CRDs of collectins are summarized and their relationship with their ligand-binding characteristics is discussed

Avian defensins

Modulation of defensin expression may be one way to improve animal health and to reduce zoonotic diseases. Defensins are small, cationic, and amphipathic cysteine-rich antibiotic peptides found in plants, insects, mammals and birds. Whereas a- and udefensins appear to be absent in birds, several b-defensins have been isolated from avian heterophils. In addition, b-defensins were found to be constitutively or inducibly expressed at mucosal surfaces of the respiratory, intestinal and urogenital tracts. In this review the current knowledge of the defensin repertoire of birds, their tissue-specific expression, regulation and corresponding biological functions are described

Phosphate analysis of natural sausage casings preserved in brines with phosphate additives as inactivating agent – Method validation

Certain phosphates have been identified as suitable additives for the improvement of the microbial and mechanical properties of processed natural sausage casings. When mixed with NaCl (sodium chloride) and used under specific treatment and storage conditions, these phosphates are found to prevent the spread of foot-and-mouth disease and classical swine fever via treated casings. The commercially available QuantichromTM phosphate assay kit has been evaluated as to whether it can serve as a reliable and low-tech method for routine analysis of casings treated with phosphate. The outcome of this study indicates that this particular assay kit has sufficient sensitivity to qualitatively determine the presence of phosphate in treated casings without interference of naturally occurring phosphate in salt used for brines in which casings are preserved

Low temperature and binding to food components inhibit the antibacterial activity of carvacrol against Listeria monocytogenes in steak tartare.

Carvacrol is a major component of thyme and oregano essential oils and has potential uses as a food preservative. The effect of carvacrol on the growth of Listeria monocytogenes was investigated in vitro and in steak tartare. Carvacrol had strong antilisterial activity in growth medium (MIC = 1.6 mM), but no effect was observed when carvacrol was tested in steak tartare. There were two reasons for this reduced activity: the antilisterial activity of carvacrol was strongly reduced at lower temperatures (10 versus 30°C), and the presence of food components interfered with the activity of carvacrol. Both bovine serum albumin and egg yolk inhibited carvacrol activity at >0.2% (wt/vol) in growth medium. For the first time, carvacrol was found to bind to albumin, suggesting that the reduced antilisterial activity of carvacrol in foods such as dairy products and uncooked meats is the result of fewer free unbound carvacrol molecules available to interact with bacteria