Biology:Bacterial outer membrane

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Short description: Plasma membrane found in gram-negative bacteria
Structure of gram-negative cell envelope
Lipopolysaccharide-assembly, LptC-related
Identifiers
SymbolLptC
PfamPF06835
Pfam clanCL0259
InterProIPR010664
Lipopolysaccharide-assembly
Identifiers
SymbolLptE
PfamPF04390
InterProIPR007485
TCDB1.B.42
OPM superfamily412
OPM protein4q35

The bacterial outer membrane is found in gram-negative bacteria. Gram-negative bacteria form two lipid bilayers in their cell envelopes - an inner membrane (IM) that encapsulates the cytoplasm, and an outer membrane (OM) that encapsulates the periplasm.[1]

The composition of the outer membrane is distinct from that of the inner cytoplasmic cell membrane - among other things, the outer leaflet of the outer membrane of many gram-negative bacteria includes a complex lipopolysaccharide whose lipid portion acts as an endotoxin - and in some bacteria such as E. coli it is linked to the cell's peptidoglycan by Braun's lipoprotein.

Porins can be found in this layer.[2]

Clinical significance

If lipid A, part of the lipopolysaccharide, enters the circulatory system it causes a toxic reaction by activating toll like receptor TLR 4. Lipid A is very pathogenic and not immunogenic. However, the polysaccharide component is very immunogenic, but not pathogenic, causing an aggressive response by the immune system. The sufferer will have a high temperature and respiration rate and a low blood pressure. This may lead to endotoxic shock, which may be fatal. The bacterial outer membrane is physiologically shed as the bounding membrane of outer membrane vesicles in cultures, as well as in animal tissues at the host–pathogen interface, implicated in translocation of gram-negative microbial biochemical signals to host or target cells.[citation needed]

Biogenesis

The biogenesis of the outer membrane requires that the individual components are transported from the site of synthesis to their final destination outside the inner membrane by crossing both hydrophilic and hydrophobic compartments. The machinery and the energy source that drive this process are not yet fully understood. The lipid A-core moiety and the O-antigen repeat units are synthesized at the cytoplasmic face of the inner membrane and are separately exported via two independent transport systems, namely, the O-antigen transporter Wzx (RfbX) and the ATP binding cassette (ABC) transporter MsbA that flips the lipid A-core moiety from the inner leaflet to the outer leaflet of the inner membrane.[3][4][5][6][7] O-antigen repeat units are then polymerised in the periplasm by the Wzy polymerase and ligated to the lipid A-core moiety by the WaaL ligase.[8][9]

The LPS transport machinery is composed of LptA, LptB, LptC, LptD, LptE. This supported by the fact that depletion of any one of these proteins blocks the LPS assembly pathway and results in very similar outer membrane biogenesis defects. Moreover, the location of at least one of these five proteins in every cellular compartment suggests a model for how the LPS assembly pathway is organised and ordered in space.[9]

LptC is required for the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.[9] LptE forms a complex with LptD, which is involved in the assembly of LPS in the outer leaflet of the outer membrane and is essential for envelope biogenesis.[9][10][11]

See also

References

  1. ↑ "Molecular mechanism of phospholipid transport at the bacterial outer membrane interface". Nat Commun 14 (1): 8285. December 2023. doi:10.1038/s41467-023-44144-8. PMID 38092770. 
  2. ↑ "Topology of outer membrane porins in pathogenic Neisseria spp". Infection and Immunity 59 (9): 2963–71. September 1991. doi:10.1128/IAI.59.9.2963-2971.1991. PMID 1652557. 
  3. ↑ "The activity of a putative polyisoprenol-linked sugar translocase (Wzx) involved in Escherichia coli O antigen assembly is independent of the chemical structure of the O repeat". J. Biol. Chem. 274 (49): 35129–38. December 1999. doi:10.1074/jbc.274.49.35129. PMID 10574995. 
  4. ↑ "An O-antigen processing function for Wzx (RfbX): a promising candidate for O-unit flippase". J. Bacteriol. 178 (7): 2102–7. April 1996. doi:10.1128/jb.178.7.2102-2107.1996. PMID 8606190. 
  5. ↑ "An Escherichia coli mutant defective in lipid export". J. Biol. Chem. 276 (15): 11461–4. April 2001. doi:10.1074/jbc.C100091200. PMID 11278265. 
  6. ↑ "Mutational analysis and properties of the msbA gene of Escherichia coli, coding for an essential ABC family transporter". Mol. Microbiol. 20 (6): 1221–33. June 1996. doi:10.1111/j.1365-2958.1996.tb02642.x. PMID 8809774. 
  7. ↑ "Function of Escherichia coli MsbA, an essential ABC family transporter, in lipid A and phospholipid biosynthesis". J. Biol. Chem. 273 (20): 12466–75. May 1998. doi:10.1074/jbc.273.20.12466. PMID 9575204. 
  8. ↑ "Lipopolysaccharide endotoxins". Annu. Rev. Biochem. 71: 635–700. 2002. doi:10.1146/annurev.biochem.71.110601.135414. PMID 12045108. 
  9. ↑ 9.0 9.1 9.2 9.3 "Functional analysis of the protein machinery required for transport of lipopolysaccharide to the outer membrane of Escherichia coli". J. Bacteriol. 190 (13): 4460–9. July 2008. doi:10.1128/JB.00270-08. PMID 18424520. 
  10. ↑ "Identification of a protein complex that assembles lipopolysaccharide in the outer membrane of Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 103 (31): 11754–9. August 2006. doi:10.1073/pnas.0604744103. PMID 16861298. Bibcode: 2006PNAS..10311754W. 
  11. ↑ "Identification of an outer membrane protein required for the transport of lipopolysaccharide to the bacterial cell surface". Proc. Natl. Acad. Sci. U.S.A. 101 (25): 9417–22. June 2004. doi:10.1073/pnas.0402340101. PMID 15192148. Bibcode: 2004PNAS..101.9417B. 
This article incorporates text from the public domain Pfam and InterPro: IPR007485
This article incorporates text from the public domain Pfam and InterPro: IPR010664



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