In 1988, we found a large (250–400 × 80–150 μm in protargol preparations) Uroleptus-like hypotrich in a freshwater pond in Harbin, China. We studied the morphology of non-dividers and the cell division using protargol impregnation. Since we disregarded live observations and due to the lack of a modern revision of the uroleptids, a final identification was not possible. A detailed comparison with the most similar limnetic Uroleptus-like hypotrichs and with Rigidothrix goiseri revealed that the Chinese population is very likely identical with Uroleptus magnificus [basionym Holosticha (Paruroleptus) magnificus Kahl, 1932], a very rare species possibly confined to limnetic, stagnant water bodies of the holarctic region. Besides the large size, main features of U. cf. magnificus are: (i) about 80 adoral membranelles; (ii) three or four inconspicuous transverse cirri; (iii) 5–8 dorsomarginal kineties; (iv) the oral primordium originates de novo left of the postoral midventral cirri; (v) the frontal-ventral-transverse cirri anlagen of the proter and the opisthe originate via primary primordia; (vi) the left frontal cirrus of the proter originates from the middle portion of the disorganizing parental paroral; (vii) the parental endoral becomes the undulating membrane anlage for the proter; and (viii) the frontoterminal cirri originate in the plesiomorphic manner, that is, from the rearmost anlage. A compilation reveals that 59 species, subspecies, etc. have been described in or assigned to Uroleptus and Paruroleptus, but only about 50% of them seem to be true uroleptids. Many species of this predominantly limnetic group are little known.
In order to investigate the anti-tumor activity of a soluble B7-1/immunoglobulin G fusion protein and explore an effective method to eliminate immune escape of tumor cells, a recombinant vector encoding this fusion protein was constructed and constitutively expressed in Chinese hamster ovary cells. After purification with protein G affinity chromatography, the soluble fusion protein was tested for bioactivity. Results showed that the fusion protein could significantly increase the density of B7-1 molecules on WEHI-3 cells, a mouse leukemia cell line. Through allogeneic mixed lymphocyte tumor cultures, it was demonstrated that, with the presence of the first signal, it could also significantly enhance T cell activation and killing activity against WEHI-3 cells and interleukin-2 secretion by activated mouse T lymphocytes. The conclusion can be drawn that the soluble B7-IgG fusion protein has a potent capacity to generate or enhance anti-tumor immune response in vitro, and its clinical value deserves further investigation.
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