Disease relevance of Lactococcus

• Here, we developed a highly efficient Escherichia coli genetic assay to determine detailed target site recognition rules for the Lactococcus lactis group II intron Ll.LtrB and to select introns that insert into desired target sites [1].
• Treatment of murine colitis by Lactococcus lactis secreting interleukin-10 [2].
• Comparative molecular modeling was performed with repressor protein Rro of the temperate Lactococcus lactis bacteriophage r1t using the known 3D-structures of related repressors in order to obtain thermolabile derivatives of Rro [3].
• Genetically modified Lactococcus lactis secreting interleukin 10 provides a therapeutic approach for inflammatory bowel disease [4].
• The discovery and characterization of insertion sequences in Lactobacillus and Lactococcus and the exploitation of heterologous conjugation and transposition systems in the lactic acid bacteria are described [5].

High impact information on Lactococcus

• To address the mechanism by which group II introns are disseminated, we have studied the bacterial L1.LtrB intron from Lactococcus lactis [6].
• The Lactococcus lactis group II intron Ll.ltrB is similar to mobile yeast mtDNA group II introns, which encode reverse transcriptase, RNA maturase, and DNA endonuclease activities for site-specific DNA insertion [7].
• Here, we show that the primary binding site for the maturase (LtrA) encoded by the Lactococcus lactis Ll.LtrB intron is within a region of intron domain IV that includes the start codon of the LtrA ORF [8].
• We report the engineering of Lactococcus lactis to produce the amino acid L-alanine [9].
• Here, we identify the major exonuclease in Lactococcus lactis, a Gram-positive organism evolutionarily distant from E. coli, and provide evidence for exonuclease-Chi interactions [10].

Chemical compound and disease context of Lactococcus

• Intragastric administration of IL-10-secreting Lactococcus lactis caused a 50% reduction in colitis in mice treated with dextran sulfate sodium and prevented the onset of colitis in IL-10(-/-) mice [2].
• The lactose genes show characteristic configurations and very high sequence identity in some phylogenetically distant lactic acid bacteria such as Leuconostoc and Lactobacillus or Lactococcus and Lactobacillus [11].
• Structural and kinetic studies of sugar binding to galactose mutarotase from Lactococcus lactis [12].
• CitS belongs to the family of the 2-hydroxycarboxylate transporters in which also the citrate carriers, CitPs, of lactic acid bacteria and the malate transporter, MleP, of Lactococcus lactis are found [13].
• Membrane potential generation via malate/lactate exchange catalyzed by the malate carrier (MleP) of Lactococcus lactis, together with the generation of a pH gradient via decarboxylation of malate to lactate in the cytoplasm, is a typical example of a secondary proton motive force-generating system [14].

Biological context of Lactococcus

• Molecular cloning, transcriptional analysis, and nucleotide sequence of lacR, a gene encoding the repressor of the lactose phosphotransferase system of Lactococcus lactis [15].
• The tagatose 6-phosphate pathway gene cluster (lacABCD) encoding galactose-6-phosphate isomerase, tagatose-6-phosphate kinase, and tagatose-1,6-diphosphate aldolase of Lactococcus lactis subsp. lactis MG1820 has been characterized by cloning, nucleotide sequence analysis, and enzyme assays [16].
• Upon fusion of these proteoliposomes with membrane vesicles of Lactococcus lactis, the delta p generated by cytochrome c-oxidase activity was capable to drive uphill transport of leucine [17].
• Molecular rearrangement of lactose plasmid DNA associated with high-frequency transfer and cell aggregation in Lactococcus lactis 712 [18].
• tRNATrp as a key element of antitermination in the Lactococcus lactis trp operon [19].

Anatomical context of Lactococcus

• The proton motive force-driven efflux pump LmrP confers multidrug resistance on Lactococcus lactis cells by extruding a wide variety of lipophilic cationic compounds from the inner leaflet of the cytoplasmic membrane to the exterior of the cell [20].
• In vitro, the purified cell wall proteinase of Lactococcus lactis was shown to liberate oligopeptides from beta- and alpha-caseins which contain amino acid sequences present in casomorphins, casokinines, and immunopeptides [21].
• These compounds also stimulated the vanadate-inhibitable ATPase activity in membranes prepared from bacteria (Lactococcus lactis) expressing BCRP [22].
• The induction of interferon (IFN) and interleukin-1 (IL-1) production in murine macrophages by a phosphopolysaccharide, produced by a dairy lactic acid bacteria, Lactococcus lactis ssp. cremoris, was investigated [23].
• Nine strains of the genus Lactococcus were examined for their probiotic properties, such as adherence to human enterocyte-like Caco-2 cells and tolerance to acid and bile [24].

Gene context of Lactococcus

• Sterol transport by the human breast cancer resistance protein (ABCG2) expressed in Lactococcus lactis [25].
• Cloning and verification of the Lactococcus lactis pyrG gene and characterization of the gene product, CTP synthase [26].
• Thus, as hsdS determinants are widespread in the genus Lactococcus, new restriction specificities may evolve rapidly after homologous recombination between these genes [27].
• Only one of the two annotated Lactococcus lactis fabG genes encodes a functional beta-ketoacyl-acyl carrier protein reductase [28].
• Mucosal delivery of murine interleukin-2 (IL-2) and IL-6 by recombinant strains of Lactococcus lactis coexpressing antigen and cytokine [29].

Analytical, diagnostic and therapeutic context of Lactococcus

• Biological containment of genetically modified Lactococcus lactis for intestinal delivery of human interleukin 10 [4].
• Here, we analyzed the interaction of the Lactococcus lactis Ll.LtrB group II intron endonuclease with its DNA target site by DNA footprinting and modification-interference approaches [30].
• The presence of lactose-utilizing Lactococcus species in nondairy environments was studied by using identification methods based on PCR amplification and (sub)species-specific probes derived from 16S rRNA sequences [31].
• Cloning and sequence analysis of putative histidine protein kinases isolated from Lactococcus lactis MG1363 [32].
• Purification and characterization of dihydroorotate dehydrogenase A from Lactococcus lactis, crystallization and preliminary X-ray diffraction studies of the enzyme [33].

References