Fattore anti-lps da Parietaria Judaica

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[automatically translated] Endotoxin is a microbial toxin, an integral part of the wall of the outer membrane of Gram-negative bacteria that is completely released with the lysis of the bacterium. It consists of sub-units' molecular which have dimensions of between 10,000 and 20,000 Daltons, while the aggregations have dimensions of about 100,000 Daltons. A typical example is represented by the endotoxin lipopolysaccharide (LPS) that is present in the outer membrane of Gram-negative bacteria. Endotoxins are the main responsible for the clinical consequences of infection by gram-negative bacteria. In fact, the endotoxin is considered responsible for the pathogenesis of sepsis, septic shock and the resulting multi-organ disease (MOF) (1). Because of its particularly aggressive nature and multifactorial, sepsis leads quickly to death and is the leading cause of death in non-coronary intensive care units worldwide. Hence the need, for the treatment of sepsis, removing and / or deactivate the endotoxin from the patient's body before the degenerate disease. In fact, in relation to the presence of endotoxin in the blood it triggers a complex immunological activation involving various biological systems (immune and reticuloendothelial) and a number of mediators, primarily released by the activation of macrophages, monocytes and other cells. In addition, endotoxins are frequent contaminants of plasmid DNA extracted from the bacteria and of all those products that are extracted and / or have come in contact with them. Endotoxins must be removed from these products to avoid inflammatory reactions in the course of in vivo applications, such as gene therapy. From the therapeutic point of view, in recent years they have assumed an important role in a class of proteins and / or peptides (and their derivatives) that, as innate immunity products, are able to bind and neutralize cell wall components including the 'LPS. The peptides that are able to neutralize this type of process are now defined with a broad term such as that of Host Defense Peptide (HDP). This latter class of proteins are of particular interest in that in addition a direct antimicrobial activity, are able to strengthen the body's immune response, promoting in vitro various defense responses (eg. Migration of leukocytes, maturation of dendritic cells) and thus contributing to the enhancement of adaptive immune response. These proteins are generally characterized by having a molecular weight of between 2 and 80 kDa and preferentially, containing amino-acids positively charged (hence the term of cationic proteins) (2). The proteins called non-specific Lipid Transfer proteins (ns-LTPs) are small particularly stable protein molecules of approximately 10 kDa usually present in all plant organisms studied until today (3). These proteins are linked by the ability to promote, in vitro, the transfer of lipid molecules across membranes although recent studies, They have shown that they seem to play a protective function in that they can act as peptides with antimicrobial activity. In some plant species it was demonstrated their allergenic capacity as in the case of the Rosaceae Prunoideae (peach, apricot, plum), Pomoideae (apple) and Urticaceae Parietaria such as (4). The recombinant DNA technology has allowed the isolation of several allergens of the ns-LTPs family of proteins, including those of Parietaria denominated Parj1 and Parj2. In particular, it has been isolated to date two Parj1 denominated allergen isoforms (according to the international nomenclature) Parj1.01 and Par1.02 (5, 6). Th
Original languageItalian
Number of pages4
Publication statusPublished - 2009

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