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Articles 1 - 3 of 3
Full-Text Articles in Veterinary Microbiology and Immunobiology
Further Characterization Of A Complement-Sensitive Mutant Of A Virulent Avian Escherichia Coli Isolate, Theodore J. Kottom, Lisa K. Nolan, Michael Robinson, John Brown, Tom Gustad, Shelley M. Horne, Catherine W. Giddings
Further Characterization Of A Complement-Sensitive Mutant Of A Virulent Avian Escherichia Coli Isolate, Theodore J. Kottom, Lisa K. Nolan, Michael Robinson, John Brown, Tom Gustad, Shelley M. Horne, Catherine W. Giddings
Lisa K. Nolan
An attempt was made to characterize the mechanism of complement resistance operating in a virulent avian Escherichia coli isolate. Using flow cytometry to detect antibody to C3, we found that there was significantly more antibody bound to a complement-sensitive mutant of this wild type than to the parent organism, suggesting that more C3 subunits were bound to the wild type. Neither the wild type nor the mutant degraded C3. Further, the mutant was phagocytosed to a significantly greater degree than the wild type by cultured phagocytes in the presence of C5-deficient serum. These data suggest that the wild type is …
Decreased Intracellular Survival Of An Fkpa Mutant Of Salmonella Typhimurium Copenhagen, Shelley M. Horne, Theodore J. Kottom, Lisa K. Nolan, Kevin D. Young
Decreased Intracellular Survival Of An Fkpa Mutant Of Salmonella Typhimurium Copenhagen, Shelley M. Horne, Theodore J. Kottom, Lisa K. Nolan, Kevin D. Young
Lisa K. Nolan
The fkpA gene of Salmonella typhimurium encodes a protein similar to the macrophage infectivity potentiator (Mip) proteins of Legionella pneumophila and Chlamydia trachomatis. Because Mip proteins enhance the ability of these intracellular pathogens to survive within macrophages and epithelial cells, we tested whether the product of the fkpA gene would have the same effect on the intracellular growth of a virulent strain of S. typhimurium. By a series of P22 transductions, the fkpA gene of S. typhimurium Copenhagen was replaced with the inactive fkpA1::omega-Cm gene from Escherichia coli, creating the mutant S. typhimurium KY32H1. The Copenhagen and KY32H1 strains were …
Phosphorylation Within The Amino-Terminal Acidic Domain I Of The Phosphoprotein Of Vesicular Stomatitis Virus Is Required For Transcription But Not For Replication, Asit K. Pattnaik, Leroy Hwang, Tong Le, Nathan Englund, Manjula Mathur, Tapas Das, Amiya Banerjee
Phosphorylation Within The Amino-Terminal Acidic Domain I Of The Phosphoprotein Of Vesicular Stomatitis Virus Is Required For Transcription But Not For Replication, Asit K. Pattnaik, Leroy Hwang, Tong Le, Nathan Englund, Manjula Mathur, Tapas Das, Amiya Banerjee
School of Veterinary and Biomedical Sciences: Faculty Publications
Phosphorylation by casein kinase II at three specific residues (S-60, T-62, and S-64) within the acidic domain I of the P protein of Indiana serotype vesicular stomatitis virus has been shown to be critical for in vitro transcription activity of the viral RNA polymerase (P-L) complex. To examine the role of phosphorylation of P protein in transcription as well as replication in vivo, we used a panel of mutant P proteins in which the phosphate acceptor sites in domain I were substituted with alanines or other amino acids. Analyses of the alanine-substituted mutant P proteins for the ability to support …