Surf Wiki
Save to docs
general/lipoproteins

From Surf Wiki (app.surf) — the open knowledge base

Braun's lipoprotein

FieldValue
NameLipoprotein leucine-zipper
PfamPF04728
SymbolLPP
InterProIPR006817
belowUse for full protein. E. coli protein is .
CATH1jccA00
SCOPd1jcca_

Braun's lipoprotein (BLP, Lpp, murein lipoprotein, or major outer membrane lipoprotein) was first identified by V. Braun and K. Rehn in 1969, it was the first Lipoprotein identified prompting much further study in this area. It is found in some gram-negative cell walls, is one of the most abundant membrane proteins; its molecular weight is about 7.2 kDa. It is bound at its C-terminal end (a lysine) by a covalent bond to the peptidoglycan layer (specifically to diaminopimelic acid molecules) and is embedded in the outer membrane by its hydrophobic head (a cysteine with lipids attached). BLP tightly links the two layers and provides structural integrity to the outer membrane.

Characteristics

The gene encoding Braun's lipoprotein initially produces a protein composed of 78 amino acids, which includes a 20 amino acid signal peptide at the amino terminus. The mature protein is 6 kDa in size. Three monomers of Lpp assemble into a leucine zipper coiled-coil trimer.

Large amounts of Braun's lipoprotein is present, more than any other protein in E. coli. Unlike other lipoproteins, it is linked covalently to the peptidoglycan. The rest of the Lpp molecules are present in a "free" form unlinked to peptidoglycan. The free form is exposed on the surface of E. coli.

Functions

Lpp, along with another OmpA-like lipoprotein called Pal/OprL (), maintains the stability of the cell envelope by attaching the outer membrane to the cell wall.

Lpp has been proposed as a virulence factor of Yersinia pestis, the cause of plague. Y. pestis needs lpp for maximum survival in macrophages and to efficiently kill mouse models of bubonic and pneumonic plague.

Immunology

Braun's lipoprotein binds to the pattern recognition receptor TLR2. Lpp induces adhesion of neutrophils to human endothelial cells by activating the latter.

References

References

  1. (October 10, 1969). "Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure". European Journal of Biochemistry.
  2. (2002). "The Bacterial Cell Wall". Springer.
  3. (2008). "Covalent attachment of proteins to peptidoglycan". FEMS Microbiology Reviews.
  4. (2015). "Outer membrane lipoprotein biogenesis: Lol is not the end". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences.
  5. (2011). "Lipoproteins of bacterial pathogens". Infection and Immunity.
  6. (2010). "The bacterial cell envelope". Cold Spring Harbor Perspectives in Biology.
  7. (2007). "The Periplasm". ASM Press.
  8. (2009). "Plague into the 21st century". Clinical Infectious Diseases.
  9. (2008). "Immune defense against pneumonic plague". Immunological Reviews.
  10. (2003). "Cell-cell interactions: leukocyte-endothelial interactions". Current Opinion in Hematology.
Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

lipoproteins peripheral-membrane-proteins
Want to explore this topic further?

Ask Mako anything about Braun's lipoprotein — get instant answers, deeper analysis, and related topics.

Research with Mako

Free with your Surf account

Content sourced from Wikipedia, available under CC BY-SA 4.0.

This content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.

Report