Article Abstract:
The interaction of human immunodeficiency virus type I envelope glycoproteins with cells and molecules of the immune system produce pleiotropic biological effects on immune functions. These include changes in CD34+ lymphoid progenitor cells and thymocytes differentiation, abnormal activation and cytokine secretion by mature T cells, B-cell hyperactivity, and suppression of T-cell-dependent B-cell differentiation. The similarity in the amino acid sequence of the glycoproteins and cellular proteins suggests that disease pathogenesis involves molecular mimicry.
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Article Abstract:
The glycoprotein-glycuprotein interactions in the agglutination of budding yeasts were explained using biochemical and molecular genetic methods Alpha-agglutinins enhance mating between yeast cells of opposite types. The glycoproteins also act as a medium to communicate response to pheromones by providing contact sites between cells for pheromone secretions and cell fusion. The proposed binding region for alpha-agglutinins was the carbon-terminal region which is composed of 80%-95% oxygen-linked oligosaccharide units.
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Article Abstract:
The structure and binding properties of cell wall-bound adhesions of ascomycetous yeasts and relation of them to their effects on cellular interactions with emphasis on the agglutinins and flocculins of Saccharomycees and the Als proteins of Candida is discussed.
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