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PubMed1998

Use of 16S rRNA gene sequencing to identify Lactobacillus casei in septicaemia secondary to a paraprosthetic enteric fistula.

Human infections caused by Lactobacillus spp. are rarely reported in the literature. Underlying conditions are frequently reported, and identification of lactobacilli to the species level remains rare. A case of Lactobacillus casei septicaemia secondary to a vascular graft infection is reported. The 16S rRNA sequencing technique was used to definitively identify Lactobacillus casei.

Aged↗
PubMed1988

Molecular cloning and nucleotide sequence of the factor IIIlac gene of Lactobacillus casei.

The lactose-specific factor III (FIIIlac of the phosphoenolpyruvate-dependent phosphotransferase system (PTS) was isolated from Lactobacillus casei and purified to homogeneity by conventional protein purification methods. Its apparent native Mr, estimated from steric exclusion chromatography (approx. 39 kDa), and subunit Mr, estimated from sodium dodecyl sulfate-polyacrylamide gels, indicated that it exists as a trimer of identical subunits of 13 kDa. The gene for FIII L. casei lac was cloned into Escherichia coli using the vector pUC18. The coding sequences were contained on an 860-bp BglII-HindIII DNA fragment of the L. casei lactose plasmid, pLZ64. A protein identical in properties to FIII L. casei lac was isolated from clones of E. coli carrying this DNA insert. The nucleotide sequence of the FIII L. casei lac gene was determined by the dideoxy chain-termination technique. The 336-bp open reading frame for FIII L. casei lac was followed by a stem-loop structure, analogous to a Rho-independent terminator. We concluded that the FIII L. casei lac was the terminal gene in what appears to be an operon comprised of the lactose-PTS-P-beta Gal-coding genes. Comparison of the deduced amino acid sequence of FIII L. caseilac with the amino acid sequence of FIII S. aureus lac (derived from peptide sequencing) demonstrated a high degree of homology (49 identical residues and 21 conservative exchanges out of 103 total aa residues). The FIII L. casei lac lacked his82, previously identified as the phosphorylation site of FIII S. aureus. lac His80 was proposed to be the site of histidyl phosphorylation of FIII L. casei lac.

Amino Acid Sequence↗
PubMed1999

Validation of a new restraint docking method for solution structure determinations of protein-ligand complexes.

A new method is proposed for docking ligands into proteins in cases where an NMR-determined solution structure of a related complex is available. The method uses a set of experimentally determined values for protein-ligand, ligand-ligand, and protein-protein restraints for residues in or near to the binding site, combined with a set of protein-protein restraints involving all the other residues which is taken from the list of restraints previously used to generate the reference structure of a related complex. This approach differs from ordinary docking methods where the calculation uses fixed atomic coordinates from the reference structure rather than the restraints used to determine the reference structure. The binding site residues influenced by replacing the reference ligand by the new ligand were determined by monitoring differences in 1H chemical shifts. The method has been validated by showing the excellent agreement between structures of L. casei dihydrofolate reductase trimetrexate calculated by conventional methods using a full experimentally determined set of restraints and those using this new restraint docking method based on an L. casei dihydrofolate reductase methotrexate reference structure.

Binding Sites↗
PubMed1976

The effect of medium redox potential on the folate-limited growth of Lactobacillus casei var. rhamnosus.

The medium redox potential (Eh) influenced the folate-limited growth of Lactobacillus casei; the growth response was maximal at an Eh of +120 mV (pH 6-35). At raised Eh serum folate would support less growth than pteroylglutamic acid, and the response to N5-methyl tetrahydrofolic acid was intermediate between them. Pteroylglutamic acid was not destroyed during 24 h incubation at 37 degrees C in medium with Eh values between +40 and +440 mV. Destruction of N5-methyl tetrahydrofolic acid occurred within 24 h when the medium Eh was greater than +125 mV. Folate was taken up rapidly by L. casei with an Eh optimum at +270 mV.

Ascorbic Acid↗
PubMed1977

Phage receptor material in Lactobacillus casei.

In Lactobacillus casei S-I, D-galactosamine and L-rhamnose comprised a phage receptor for phage J-I. A mixture of D-galactosamine and L-rhamnose effectively inactivated phage J-I, and a J-I-resistant mutant strain, L. casei S-I/J-I, lacked D-galactosamine in its surface component. The phage-inactivating effects of D-galactosamine and L-rhamnose were strongly dependent on the concentration of each substance and on temperature. It is suggested that the receptor for phage J-I involves both D-galactosamine in the cytoplasmic membrane and L-rhamnose in the wall of the host bacterium L. casei S-I, which lacts teichoic acid in its wall.

Bacteriophages↗