Disease relevance of nlpD

• Outer surface lipoprotein (Osp) C is a virulence factor required for transmission of the Lyme disease agent, Borrelia burgdorferi [1].
• We show that rpoS transcription in E. carotovora subsp. carotovora is driven from a major promoter which resides within the nlpD gene located upstream of rpoS as in E. coli [2].
• Like in other gram-negative bacteria, a homolog of the nlpD gene was found upstream to the rpoS gene [3].
• The virion consists of a lipoprotein envelope surrounding an icosahedral capsid composed of dimers of a 183-residue protein, 'core antigen' (HBcAg) [4].
• Lipoprotein e(P4) is essential for hemin uptake by Haemophilus influenzae [5].

High impact information on nlpD

• This recognition mechanism provides the basis for regulation of protein transport from the TGN to endosomes/lysosomes, which is shared by sortilin and low-density lipoprotein receptor-related protein [6].
• Human serum albumin, high density and low density lipoprotein, and IgG together protect erythrocytes and platelets against attack by even high doses (5-25 micrograms/ml) of ECH [7].
• Spleen cells from these mice were unresponsive to a series of B-cell mitogens including LPS prepared from Escherichia coli K235 and from E. coli 0111:B4, lipoprotein mitogen from E. coli, and Nocardia water-soluble mitogen (NWSM) [8].
• A complex of structures including the Ig-receptor molecules, the LPS receptor, and the lipoprotein receptor appear involved in the regulation of mitogenic stimulation of B cells to proliferation and differentiation to IgM-secreting cells [9].
• Removal of ester-linked fatty acids from the amino-terminal end of the lipoprotein by alkaline hydrolysis abolishes the mitogenicity of the lipoprotein [9].

Chemical compound and disease context of nlpD

• A signal peptidase specifically required for the secretion of the lipoprotein of the Escherichia coli outer membrane cleaves off the signal peptide at the bond between a glycine and a cysteine residue [10].
• The same tetrapeptide occurs in the signal sequence of the prolipoprotein of Escherichia coli, and the cysteine residue in the tetrapeptide of prolipoprotein is modified to form glyceride-cysteine which becomes the NH2 terminus of Braun's lipoprotein [11].
• Plasmids were constructed that contain a thermoinducible runaway replicon and either the E. coli tryptophan or lipoprotein promoter and ribosome binding sites, which served as transcriptional and translational initiation sites for the expression of the bGH gene [12].
• Under the same conditions, globomycin does not prevent the attachment of palmitate or glycerol to the E. coli prolipoprotein but inhibits processing of the modified precursor to the mature lipoprotein [13].
• A characteristic signal peptide is present at the amino terminus whose removal is inhibited by the antibiotic, globomycin, suggesting that mature chitobiase is a lipoprotein with a maturation pathway similar to that of the Escherichia coli major outer membrane lipoprotein [14].

Biological context of nlpD

• The nlpD gene is located in an operon with rpoS on the Escherichia coli chromosome and encodes a novel lipoprotein with a potential function in cell wall formation [15].
• Disruption of the chromosomal E. coli nlpD gene by insertional mutagenesis results in decreased stationary-phase survival after 7 days [16].
• An outer membrane protein playing a critical role in Lpp incorporation was identified, and partial amino acid sequences of the protein, named LolB, were identical to those of HemM, which has been suggested to play a role in 5-aminolevulinic acid synthesis in the cytosol [17].
• This cysteine residue was altered to a glycine residue by guided site-specific mutagenesis using a synthetic oligonucleotide and a plasmid carrying an inducible lipoprotein gene [10].
• (d) The nucleotide sequence from position 46 to 168 of the lpp gene was deleted [18].

Anatomical context of nlpD

• Anti-immunoglobulin antibodies inhibit the mitogenic stimulation of B cells by lipoprotein [9].
• The Escherichia coli major outer membrane lipoprotein (Lpp) is released from the inner membrane into the periplasm as a complex with a carrier protein, LolA (p20), and is then specifically incorporated into the outer membrane [17].
• The recent model of Treponema pallidum molecular architecture proposes that the vast majority of the bacterium's integral membrane proteins are lipoprotein immunogens anchored in the cytoplasmic membrane while the outer membrane contains only a limited number of surface-exposed transmembrane proteins [19].
• Whereas lipoprotein in the wild-type strain is exclusively located in the outer membrane of the cell envelope, the membrane-bound lipoprotein in this mutant is recovered in both the inner and outer membranes of the cell envelope [20].
• Both the bacterially produced and authentic plasma apoE bound similarly to apolipoprotein B,E(low density lipoprotein) receptors of human fibroblasts and to hepatic apoE receptors [21].

Associations of nlpD with chemical compounds

• Cholesteryl ester transfer protein (CETP) facilitates exchange of HDL cholesterol for very low density lipoprotein (VLDL) triglyceride, leading to catabolism of HDL [22].
• It was found that all lipoprotein classes bound LPS in direct proportion to their plasma cholesterol concentration [23].
• Amino acid analysis of the purified mutant lipoprotein indicates that the mutant lipoprotein corresponds to the uncleaved prolipoprotein with a single amino acid replacement of glycine with aspartic acid [20].
• Likewise, when [3H]-palmitate-labeled JE5505 cell envelope was incubated with the MM18 cell envelope containing unmodified prolipoprotein in the presence of detergent, [3H]palmitate radioactivity was incorporated into prolipoprotein by ester linkage and into mature lipoprotein by both ester and amide linkages [24].
• We previously reported that, on treatment of cells with globomycin, a precursor of Braun's lipoprotein accumulated in the cell envelope (Hussain, M., Ichihara, S., and Mizushima, S. (1980) J. Biol. Chem. 255, 3707-3712) [25].

Analytical, diagnostic and therapeutic context of nlpD

• Eighteen hours after an intraperitoneal injection of endotoxin, the hepatic LDL-receptor expression and the plasma lipoprotein pattern were analyzed [26].
• We believe that the molecular cloning and characterization of N-SMase cDNA will accelerate the process to define its role as a key regulator in apoptosis, lipid and lipoprotein metabolism, and other cell regulatory pathways [27].
• Immunoblotting analysis using the antibody against the 45-kDa protein revealed a 48-kDa precursor of the protein, which accumulated in the cyanobacterial cells treated with globomycin, an antibiotic that specifically inhibits cleavage of the signal peptide of lipoprotein precursors [28].
• Compared to native apoE3 (299 residues), all had reduced affinity for lipoproteins, as assessed by incubation of 125I-labeled proteins with plasma followed by fractionation of lipoprotein classes by gel filtration [29].
• The mRNA that codes for a structural lipoprotein in the outer membrane was purified from the total RNA by three successive electrophoreses on polyacrylamide slab gels, twice at pH 8.3 and once at pH 3.5 in 7 M urea [30].

References