Objectives
CD55, a cell surface complement inhibitory protein serves as a cellular receptor for multiple viruses and bacteria that cause chronic/intracellular infection. Using uropathogenic E. coli, the first CD55-recognizing pathogen described, as a model and a series of CD55 mutants we investigated the mechanism of CD55-mediated invasion and persistence.
Methods
CD55 amino acids in the vicinity of the binding pocket-Ser155 for E. coli Dr adhesin were mutated to alanine and subjected to a modified temporal-gentamicin-invasion/survival assay in Chinese Hamster Ovary cells. CD55/Microtubule (MT) responses were studied using confocal-microscopy, histo-chemistry and 3-D-structure analysis. Mutation at Ser165 decreased Dr+ E. coli internalization by >70% (p<0.05), retained low rate persistence without multiplication and correlated with Ser165Ala disrupted negative-charge distribution.
Methods
CD55 amino acids in the vicinity of the binding pocket-Ser155 for E. coli Dr adhesin were mutated to alanine and subjected to a modified temporal-gentamicin-invasion/survival assay in Chinese Hamster Ovary cells. CD55/Microtubule (MT) responses were studied using confocal-microscopy, histo-chemistry and 3-D-structure analysis. Mutation at Ser165 decreased Dr+ E. coli internalization by >70% (p<0.05), retained low rate persistence without multiplication and correlated with Ser165Ala disrupted negative-charge distribution.
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