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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Medical microbiology and immunology 178 (1989), S. 105-112 
    ISSN: 1432-1831
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Antigen A60 has been purified from the cytoplasm of Mycobacterium bovis BCG, and its composition has been determined: it has proved to be able to elicit immune reactions of both humoral and cellular type. Inoculation of A60 into the footpad of mice previously sensitized with the same antigen, or with whole mycobacterial cells produced a footpad swelling showing a peak at 24 h. Similar delayed hypersensitivity reactions were induced in sensitized guinea-pigs by subcutaneous injection of an A60 dose of 0.01 μg (minimal revealing dose). A quantity thousandfold higher (15 μg A60) was unable to induce in unsensitized guinea pigs the mounting of a cellular immunisation against A60, as shown by negative cutaneous testings 1 month later. Our results show that A60 preparations satisfied the requirements of the European Pharmacopoeia Commission and met the WHO recommandations for new tuberculins. Handicaps of old tuberculin and PPD (heterogeneous mixtures titrated biologically and unstable in solution) can be overcome by A60 preparations (a single antigen spectrophoretically measurable and stable).
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Coelomic cytolytic factor (CCF) is a 42 kDa invertebrate pattern recognition molecule isolated from the coelomic fluid of the earthworm Eisenia foetida (Oligochaeta, Annelida). CCF displays a number of similarities with the mammalian cytokine tumour necrosis factor-α (TNF-α) as a result of a shared N,N′-diacetylchitobiose lectin-like domain. However, these similarities are solely functional and are not based on any (DNA or amino acid) sequence homology, thus suggesting a form of convergent evolution. In particular, the lectin-like domain of TNF-α has been shown to induce membrane depolarization in various mammalian cell types, through interactions with endogenous amiloride-sensitive ion channels. This nonreceptor-mediated activity of TNF-α has been reported to be involved in the resorption of oedema. Likewise, the lectin-like domain of CCF also induces membrane depolarization in mammalian cells. Here, we show that CCF appears to be able to induce oedema resorption in an alveolar epithelial cell line through its lectin-like domain. This lectin-like domain of CCF interacts (directly or indirectly) with endogenous sodium and/or chloride channels, and not potassium channels, on mammalian cells. Additionally, we suggest that the JNK/SAPK and Erk1/2 pathways are involved in CCF-induced macrophage activation. These results further establish the functional analogy between an invertebrate pattern recognition molecule and a mammalian cytokine and, from a more applied point of view, suggest the possibility of utilizing CCF in the treatment of oedema.
    Type of Medium: Electronic Resource
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