Identification of a DNA transformation gene required for com101A+ expression and supertransformer phenotype in Haemophilus influenzae.

DNA sequencing, RNA mapping, and protein expression experiments revealed the presence of a gene, tfoX+, encoding a 24.9-kDa polypeptide, that is transcribed divergently from a common promoter region with the Haemophilus influenzae rec-1+ gene. H.

Structural organization, nucleotide sequence, and regulation of the Haemophilus influenzae rec-1+ gene.

The Haemophilus influenzae rec-1+ protein plays a central role in DNA metabolism, participating in general homologous recombination, recombinational (postreplication) DNA repair, and prophage induction. Although many H. influenzae rec-1 mutants have been phenotypically characterized, little is known about the rec-1+ gene at the molecular level.

Urethral obstruction of 6 hours or less causes bacteriuria, bacteremia, and pyelonephritis in mice challenged with "nonuropathogenic" Escherichia coli.

Urethral obstruction may be caused by prostatic hypertrophy, urethral stricture, or encrustation of a urethral-catheter lumen. Bacteriuria often complicates these obstructions. The sequelae include fever, acute pyelonephritis, chronic renal inflammation, and death.

Early colonic damage and invasion of Campylobacter jejuni in experimentally challenged infant Macaca mulatta.

Experimental challenge studies with Campylobacter jejuni were conducted in 3.5-month-old infant Macaca mulatta. One infant monkey (92-1) was challenged with 2.

Contribution of Proteus mirabilis urease to persistence, urolithiasis, and acute pyelonephritis in a mouse model of ascending urinary tract infection.

Proteus mirabilis, a significant cause of bacteriuria and acute pyelonephritis in humans, produces urease. This high-molecular-weight, multimeric, cytoplasmic enzyme hydrolyzes urea to ammonia and carbon dioxide. To assess the role of urease in colonization, urolithiasis, and acute pyelonephritis in an animal model of ascending urinary tract infection, we compared a uropathogenic strain of P.

The effect of signal sequences on the efficiency of secretion of a heterologous phosphotriesterase by Streptomyces lividans.

A heterologous phosphotriesterase (parathion hydrolase) containing the native Flavobacterium species signal sequence was previously shown to be secreted by Streptomyces lividans. Western blot analysis of the recombinant phosphotriesterase produced by S. lividans demonstrated only the mature form extracellularly but both processed and unprocessed forms in cell-associated samples.

Investigation of an outbreak of bloody diarrhea: association with endoscopic cleaning solution and demonstration of lesions in an animal model.

Unlabelled: OUTBREAK INVESTIGATION: An outbreak of diarrhea, bloody diarrhea, and abdominal cramps occurred among persons undergoing flexible sigmoidoscopy at a branch clinic of a local health center. Illness was associated with use of sigmoidoscopes cleaned by one clinic assistant and appeared to be caused by 2% glutaraldehyde disinfectant solution left in the instruments after cleaning.

Animal Studies: In subsequent animal studies, colonic instillation of 2% glutaraldehyde solutions caused bloody diarrhea and a distinctive pattern of mucosal damage; similar changes were seen in a review of pathologic samples from other human cases of glutaraldehyde disinfectant-associated diarrhea.

Cold agglutinins in cats with haemobartonellosis.

Coombs-positive anemia developed in cats inoculated with Haemobartonella felis. Cold agglutinins were detected in serum during the acute stage of the disease when anemia was present. The cold agglutinating activity was associated with IgM, was demonstrated at 4 C, and was abolished by treatment of sera with 2-mercaptoethanol.

Purification and characterization of S-adenosylhomocysteine deaminase from streptonigrin-producing Streptomyces flocculus.

An S-adenosylhomocysteine deaminase has been isolated and purified from streptonigrin-producing Streptomyces flocculus ATCC 13257. Deamination represents the major metabolic route of S-adenosylhomocysteine in this organism. The protein was found to be monomeric with a molecular weight of 56,100 +/- 1,600.

S-adenosylhomocysteine metabolism in Streptomyces flocculus.

S-Adenosylhomocysteine metabolism was studied in cell extracts of streptonigrin-producing Streptomyces flocculus. The major route of metabolism was found to be deamination to form S-inosylhomocysteine. The metabolite was purified by high-performance liquid chromatography and identified by its UV and nuclear magnetic resonance spectra and by its chemical degradation to hypoxanthine.