Expression of type 1 fimbriae and mannose-sensitive hemagglutinin by recombinant plasmids.

Deletions within the cloned genes (fimA) encoding the type 1 major fimbrial subunits of two isolates of Klebsiella pneumoniae resulted in a nonfimbriate but hemagglutinating phenotype after transformation of Escherichia coli HB101 or ORN103. Phenotypic expression of type 1 fimbriae could be restored by transformation with plasmids containing the fimA genes of the fimbrial gene clusters from different strains. The surface fimbriae expressed were serologically identical to those of the polymerized product of the introduced fimA gene.

Type 3 fimbriae among enterobacteria and the ability of spermidine to inhibit MR/K hemagglutination.

The distribution of the gene cluster encoding type 3 fimbriae among various isolates of the family Enterobacteriaceae was investigated by using 112 clinical and nonclinical isolates. Closely related DNA sequences were detected in all Klebsiella strains, in most Enterobacter isolates, in a smaller number of Escherichia coli and Salmonella spp., and in a single isolate each of Yersinia enterocolitica and Serratia liquefaciens but not in isolates of Morganella or Providencia species or Serratia marcescens.

Molecular characterization of the type 3 (MR/K) fimbriae of Klebsiella pneumoniae.

The expression of type 3 (MR/K) fimbriae by Klebsiella pneumoniae requires the production of at least four polypeptides with molecular masses of 20.5, 25, 34, and 78 kilodaltons. The genes encoding these polypeptides are located on a gene cluster 5,500 base pairs in length.

Characterization of two genes encoding antigenically distinct type-1 fimbriae of Klebsiella pneumoniae.

A uropathogenic isolate of Klebsiella pneumoniae was shown to exhibit a mannose-sensitive hemagglutinating phenotype and to produce type-1 fimbriae consisting of subunits with a different electrophoretic mobility than those previously investigated. The gene cluster encoding expression of fimbriae was cloned and the genetic organization of the encoded polypeptides was determined. The gene encoding the major fimbrial subunit was localized and further examined by nucleotide sequence analysis.

Efficacy of an immunomodulating drug in immunodeficient and immunocompetent mice.

Bacillus subtilis culture filtrate (BSKR) was examined for its immunomodulating ability in the immunodeficient beige mouse and the immunocompetent Han:NMRI mouse strain. Following various application schemes the mice were challenged either subcutaneously with Escherichia coli or intranasally with Streptococcus pneumoniae. The mortality rates and the median of survival time were determined.

Interaction of immobilized phosphofructokinase with soluble muscle proteins.

Selected glycolytic enzymes (including phosphoglucose isomerase, aldolase, glyceraldehyde phosphate dehydrogenase, enolase, pyruvate kinase and lactate dehydrogenase), as well as glycogen phosphorylase, creatine kinase, and adenylate kinase, bound to phosphofructokinase immobilized on an agarose gel. The affinity of phosphofructokinase to these various proteins differed, with phosphorylase exhibiting the strongest binding. Binding was reversed either by: (1) elution with high-ionic-strength buffer (0.

The role of detergent in labeling of Erysipelothrix rhusiopathiae bacteria.

The chelating agents oxine, acetylacetone, tropolone, and 2-mercaptopyridine 1-oxide were analysed for their suitability in labeling the bacterium Erysipelothrix rhusiopathiae (E.r.), strain B10, with 111In and 67Ga.