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Gene Review

lpp  -  major outer membrane lipoprotein

Escherichia coli CFT073

 
 
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Disease relevance of lpp

 

High impact information on lpp

 

Chemical compound and disease context of lpp

  • 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 [8].
 

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 [9].
  • 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 [10].
  • 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 [11].
 

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 [12].
 

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 [13].

References

  1. 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. Tokunaga, H., Wu, H.C. J. Biol. Chem. (1984) [Pubmed]
  2. Evolution of the lipoprotein gene in the enterobacteriaceae. Cloning and DNA sequence of the lpp gene from Proteus mirabilis. Ching, G., Inouye, M. J. Mol. Biol. (1985) [Pubmed]
  3. Prolipoprotein modification and processing in Escherichia coli. A unique secondary structure in prolipoprotein signal sequence for the recognition by glyceryl transferase. Giam, C.Z., Chai, T., Hayashi, S., Wu, H.C. Eur. J. Biochem. (1984) [Pubmed]
  4. Characterization of a novel lipoprotein mutant in Escherichia coli. Giam, C.Z., Hayashi, S., Wu, H.C. J. Biol. Chem. (1984) [Pubmed]
  5. Effects of replacing serine and threonine residues within the signal peptide on the secretion of the major outer membrane lipoprotein of Escherichia coli. Vlasuk, G.P., Inouye, S., Inouye, M. J. Biol. Chem. (1984) [Pubmed]
  6. Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coli. Vlasuk, G.P., Inouye, S., Ito, H., Itakura, K., Inouye, M. J. Biol. Chem. (1983) [Pubmed]
  7. Distribution of newly synthesized lipoprotein over the outer membrane and the peptidoglycan sacculus of an Escherichia coli lac-lpp strain. Hiemstra, H., Nanninga, N., Woldringh, C.L., Inouye, M., Witholt, B. J. Bacteriol. (1987) [Pubmed]
  8. OspA, a lipoprotein antigen of the obligate intracellular bacterial pathogen Piscirickettsia salmonis. Kuzyk, M.A., Burian, J., Thornton, J.C., Kay, W.W. J. Mol. Microbiol. Biotechnol. (2001) [Pubmed]
  9. Induction kinetics and cell surface distribution of Escherichia coli lipoprotein under lac promoter control. Hiemstra, H., de Hoop, M.J., Inouye, M., Witholt, B. J. Bacteriol. (1986) [Pubmed]
  10. Effects of inserting eight amino acid residues into the major lipoprotein on its assembly in the outer membrane of Escherichia coli. Inukai, M., Masui, Y., Vlasuk, G.P., Inouye, M. J. Bacteriol. (1983) [Pubmed]
  11. Half-life of Escherichia coli polyadenylated lipoprotein mRNA. Taljanidisz, J., Shen, P., Sarkar, N. Biochem. Mol. Biol. Int. (1997) [Pubmed]
  12. Activities of a mechanosensitive ion channel in an E. coli mutant lacking the major lipoprotein. Kubalski, A., Martinac, B., Ling, K.Y., Adler, J., Kung, C. J. Membr. Biol. (1993) [Pubmed]
  13. In vivo and in vitro lipidation of recombinant immunogens for direct iscom incorporation. Andersson, C., Wikman, M., Lövgren-Bengtsson, K., Lundén, A., Ståhl, S. J. Immunol. Methods (2001) [Pubmed]
 
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