Disease relevance of lpp

• The gene for the outer membrane lipoprotein (lpp), the most abundant protein of Escherichia coli, was used to construct multi-purpose expression cloning vehicles [1].
• Evolution of the lipoprotein gene in the enterobacteriaceae. Cloning and DNA sequence of the lpp gene from Proteus mirabilis [2].
• Comparison with the lpp genes from Escherichia coli, Serratia marcescens, Erwinia amylovora and Morganella morganii revealed several unique features of the evolution of the lpp gene in the Enterobacteriaceae and enabled us to establish phylogenetic relationships between these bacteria [2].
• Next, the coding sequence for Met-UG was inserted in a runaway-replication plasmid and expressed under the control of the lpp promoter and the RBS derived from bacteriophage Mu cII gene [3].
• A fragment of human DNA encoding the mature form of interferon alpha 2 (hIFN-alpha 2), and carrying both an in-phase ATG initiation codon and the ribosome binding site (RBS) of the Escherichia coli membrane lipoprotein gene (lpp), was fused to the aminoglycoside phosphotransferase gene (aph) promoter (aphP) from Streptomyces fradiae [4].

High impact information on lpp

• (d) The nucleotide sequence from position 46 to 168 of the lpp gene was deleted [1].
• However, the 3' end position of the lpp gene of 154 bp was retained, which contains not only translation termination codons in three different reading frames but also the transcription termination signal of the lpp gene [1].
• The in vitro decay of two different mRNAs (trxA and lpp) is triggered by the addition of ATP only when polysomes are prepared from s strain carrying the wild-type gene for PAP I (pcnB+) [5].
• These data provide the first direct evidence that the TNF inducing lipid modification of native Borrelia lipoproteins is a structural homologue of the murein lipoprotein of Escherichia coli [6].
• The DNA sequence analysis of the F0F1-ATPase operon of the bacterium Mycoplasma pneumoniae predicted that the subunit b, encoded by the gene atpF, is a lipoprotein of the murein lipoprotein type of Escherichia coli [7].

Chemical compound and disease context of lpp

• In addition to the prolipoprotein, two ery-lpp hybrid proteins containing a 45- and a 22-amino acid extension preceding the NH2 terminus of prolipoprotein, respectively, are also synthesized in E. coli [8].
• Eighty globomycin-resistant mutants were independently isolated from Escherichia coli K-12 which had a deletion mutation in chromosomal lipoprotein gene (lpp), but contained a plasmid carrying the wild-type lpp gene [9].
• Lipoprotein was briefly induced with isopropyl-beta-D-thiogalactopyranoside in cells carrying lac-lpp on a low-copy-number plasmid in an E. coli lpp host [10].
• Palmitate incorporation demonstrated that OspA is posttranslationally lipidated in E. coli, albeit poorly expressed as a lipoprotein even after replacement of the signal sequence with the signal sequence from lpp (Braun lipoprotein) or the rickettsial 17 kDa homologue [11].
• The effects of 3,4-dihydroxybutyl-1-phosphonate, a four-carbon analog of sn-glycerol 3-phosphate, on the biosynthesis of the glyceryl moiety in murein lipoprotein of Escherichia coli were studied [12].

Biological context of lpp

• Using in vitro gene fusion techniques, the lpp gene was placed under the control of the promoter for the erythromycin-resistance (ery) gene [8].
• DNA sequence analysis of the mutant lpp allele and determination of the amino acid composition of the mutant lipoprotein revealed a single amino acid substitution of cysteine for arginine at the 68th amino acid residue of prolipoprotein [13].
• We have cloned the Escherichia coli lipoprotein structural gene (lpp) into a shuttle vector and studied its expression in both E. coli and in Bacillus subtilis [8].
• The induction kinetics and surface accessibility of the outer membrane lipoprotein were studied in an Escherichia coli strain with the lpp gene under control of the lac promoter [14].
• A 192-bp DNA fragment containing the coding sequence for methionyl UG (Met-UG) and the ribosome-binding site (RBS) was chemically synthesized and placed downstream from the promotor for the Escherichia coli outer-membrane lipoprotein gene (lpp) on a plasmid [3].

Anatomical context of lpp

• Whereas small amphipaths (chlorpromazine, trinitrophenol) or a larger amphipath (lysolecithin) all activated the MS channel in the wild-type membrane under minimal suction, only the larger lysolecithin could activate the MS channel in the lpp membranes [15].
• Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins synthesized in spheroplasts revealed the preferential synthesis of five polypeptides, one of which has been identified as the free form of murein lipoprotein [16].
• Murein lipoprotein from the outer membrane of Escherichia coli could be fixed to erythrocytes without pretreatment of the erythrocytes [17].

Associations of lpp with chemical compounds

• These pseudorevertants in the lpp gene which could be recognized by the anomalous prolipoprotein mobility in sodium dodecyl sulfate gels, exhibited altered globomycin sensitivity in vivo [18].
• Radioactive labeling experiments in the presence or absence of globomycin showed that the hybrid protein is modified with a diglyceride and fatty acids and is processed by signal peptidase II, as is the murein lipoprotein [19].
• Mutants with alterations in the structure, biosynthesis, or assembly of murein lipoprotein were selected by a procedure based on radiation suicide of wild-type organisms by [3H]arginine under conditions where the radioactive arginine was preferentially incorporated into lipoprotein [20].
• Antibody titres against OM proteins I and II, lipopolysaccharide and murein-lipoprotein were determined by the enzyme-linked immunosorbent assay (ELISA) in these sera, and in antisera elicited against whole formaldehyde-fixed bacteria or isolated OM [21].

Other interactions of lpp

• The biosynthesis of the acyl moieties in murein lipoprotein was studied by fusion of [3H]palmitate-labeled phospholipid vesicles with intact cells of an fadD mutant of Escherichia coli [22].

Analytical, diagnostic and therapeutic context of lpp

• For the in vivo lipidation strategy, a general expression vector was constructed encoding a composite tag consisting of a sequence (lpp) of the major lipoprotein of E. coli, fused to a dual affinity fusion tag to allow efficient recovery by affinity chromatography [23].
• Our goal in the current work was to determine if passive immunization directed to MLP and PAL protects mice from Gram-negative sepsis [24].
• Neither monoclonal nor polyclonal IgG directed to MLP or PAL conferred survival protection in 3 different models of sepsis: cecal ligation and puncture, an infected burn model, and an infected fibrin clot model mimicking peritonitis [24].

References