Disease relevance of lpp

• Studies on the modification and processing of prolipoprotein in Escherichia coli. Effects of structural alterations in prolipoprotein on its maturation in wild type and lpp mutants [1].
• 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].
• Evolution of the lipoprotein gene in the enterobacteriaceae. Cloning and DNA sequence of the lpp gene from Proteus mirabilis [2].
• Both the wild-type and the lpp-14-1 alleles of the lpp gene have been cloned onto a phage lambda vector [3].
• Passive immunization to outer membrane proteins MLP and PAL does not protect mice from sepsis [4].

High impact information on lpp

• 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 [5].
• 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 [6].
• 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 [7].
• 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 [1].
• Mutants altered in the structural gene for murein lipoprotein in Escherichia coli can be isolated by globomycin selection [7].

Chemical compound and disease context of lpp

• 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 [8].
• 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 [9].
• 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 [10].

Biological context of lpp

• 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 [11].
• A DNA sequence consisting of 24 base pairs was inserted into the structural gene (lpp) coding for the major lipoprotein of the Escherichia coli outer membrane which was carried on a high-copy-number plasmid in which expression was regulated through a lac promoter-operator region [12].
• In the light of recent evidence that the half-life of bacterial mRNA may be modulated by polyadenylation at the 3' end, we determined the half-life of polyadenylated lpp mRNA, which is an abundant and comparatively stable message encoding a major lipoprotein of the outer membrane [13].
• A fusion gene (lpp'cma) was constructed which determined two proteins: Lpp'-Cma composed of the signal sequence of the murein lipoprotein (Lpp) and colicin M (Cma), and unaltered colicin M [14].

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

• 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 [18].
• 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 [19].
• 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 [20].

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 [21].

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 [22].
• Our goal in the current work was to determine if passive immunization directed to MLP and PAL protects mice from Gram-negative sepsis [4].
• 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 [4].

References