Braun's lipoprotein

Last updated
Lipoprotein leucine-zipper
Identifiers
SymbolLPP
Pfam PF04728
InterPro IPR006817
CATH 1jccA00
SCOP2 d1jcca_ / SCOPe / SUPFAM
Use IPR016367 for full protein. E. coli protein is P69776 .

Braun's lipoprotein (BLP, Lpp, murein lipoprotein, or major outer membrane lipoprotein), 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 [1] ) 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.

Contents

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. [2] The mature protein is 6 kDa in size. [3] Three monomers of Lpp assemble into a leucine zipper coiled-coil trimer. [4]

Large amounts of Braun's lipoprotein is present, more than any other protein in E. coli. [5] Unlike other lipoproteins, it is linked covalently to the peptidoglycan. [4] Lpp connects the outer membrane to the peptidoglycan. Lpp is anchored to the outer membrane by its amino-terminal lipid group. In E. coli, one third of Lpp proteins form a peptide bond via the side chain of its carboxy-terminal lysine with diaminopimelic acid in the peptidoglycan layer. [5] [6] 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. [3]

Functions

Lpp, along with another OmpA-like lipoprotein called Pal/OprL ( P0A912 ), maintains the stability of the cell envelope by attaching the outer membrane to the cell wall. [3]

Lpp has been proposed as a virulence factor of Yersinia pestis , the cause of plague. [7] Y. pestis needs lpp for maximum survival in macrophages and to efficiently kill mouse models of bubonic and pneumonic plague. [8]

Immunology

Braun's lipoprotein binds to the pattern recognition receptor TLR2. Lpp induces adhesion of neutrophils to human endothelial cells by activating the latter. [9]

Related Research Articles

Cell wall Outermost layer of some cells

A cell wall is a structural layer surrounding some types of cells, just outside the cell membrane. It can be tough, flexible, and sometimes rigid. It provides the cell with both structural support and protection, and also acts as a filtering mechanism. Cell walls are present in most prokaryotes, in algae, fungi and eukaryotes including plants but are absent in animals. A major function is to act as pressure vessels, preventing over-expansion of the cell when water enters.

Gram-negative bacteria Group of bacteria that do not retain the crystal violet stain used in the Gram-staining method of bacterial differentiation

Gram-negative bacteria are bacteria that do not retain the crystal violet stain used in the gram-staining method of bacterial differentiation. They are characterized by their cell envelopes, which are composed of a thin peptidoglycan cell wall sandwiched between an inner cytoplasmic cell membrane and a bacterial outer membrane.

Peptidoglycan or murein is a polymer consisting of sugars and amino acids that forms a mesh-like layer outside the plasma membrane of most bacteria, forming the cell wall. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is a peptide chain of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. Peptidoglycan is also involved in binary fission during bacterial cell reproduction.

The cell envelope comprises the inner cell membrane and the cell wall of a bacterium. In gram-negative bacteria an outer membrane is also included. This envelope is not present in the Mollicutes where the cell wall is absent.

Biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined together to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.

These molecules can be referred to as small molecular motifs conserved within a class of microbes. They are recognized by toll-like receptors (TLRs) and other pattern recognition receptors (PRRs) in both plants and animals. A vast array of different types of molecules can serve as PAMPs, including glycans and glycoconjugates.

Bacterial outer membrane

The bacterial outer membrane is found in gram-negative bacteria. Its composition 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.

Penicillin-binding proteins

Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases.

The bacterium, despite its simplicity, contains a well-developed cell structure which is responsible for some of its unique biological structures and pathogenicity. Many structural features are unique to bacteria and are not found among archaea or eukaryotes. Because of the simplicity of bacteria relative to larger organisms and the ease with which they can be manipulated experimentally, the cell structure of bacteria has been well studied, revealing many biochemical principles that have been subsequently applied to other organisms.

Lysin

Lysins, also known as endolysins or murein hydrolases, are hydrolytic enzymes produced by bacteriophages in order to cleave the host's cell wall during the final stage of the lytic cycle. Lysins are highly evolved enzymes that are able to target one of the five bonds in peptidoglycan (murein), the main component of bacterial cell walls, which allows the release of progeny virions from the lysed cell. Cell-wall-containing Archaea are also lysed by specialized pseudomurein-cleaving lysins, while most archaeal viruses employ alternative mechanisms. Similarly, not all bacteriophages synthesize lysins: some small single-stranded DNA and RNA phages produce membrane proteins that activate the host's autolytic mechanisms such as autolysins.

In enzymology, a diaminopimelate epimerase is an enzyme that catalyzes the chemical reaction

Diaminopimelate decarboxylase

In enzymology, diaminopimelate decarboxylase, also known as diaminopimelic acid decarboxylase, DAPDC, meso-diaminopimelate decarboxylase, DAP-decarboxylase, and meso-2,6-diaminoheptanedioate carboxy-lyase, is an enzyme that catalyzes the cleavage of carbon-carbon bonds in meso 2,6 diaminoheptanedioate to produce CO2 and L-lysine, the essential amino acid. It employs the cofactor pyridoxal phosphate, also known as PLP, which participates in numerous enzymatic transamination, decarboxylation and deamination reactions.

Virulence-related outer membrane protein family

Virulence-related outer membrane proteins are expressed in the outer membrane of gram-negative bacteria and are essential to bacterial survival within macrophages and for eukaryotic cell invasion.

Diaminopimelic acid

Diaminopimelic acid (DAP) is an amino acid, representing an epsilon-carboxy derivative of lysine.

OmpA domain

In molecular biology, the OmpA domain is a conserved protein domain with a beta/alpha/beta/alpha-beta(2) structure found in the C-terminal region of many Gram-negative bacterial outer membrane proteins, such as porin-like integral membrane proteins, small lipid-anchored proteins, and MotB proton channels. The N-terminal half of these proteins is variable although some of the proteins in this group have the OmpA-like transmembrane domain at the N terminus. OmpA from Escherichia coli is required for pathogenesis, and can interact with host receptor molecules. MotB serve two functions in E. coli, the MotA(4)-MotB(2) complex attaches to the cell wall via MotB to form the stator of the flagellar motor, and the MotA-MotB complex couples the flow of ions across the cell membrane to movement of the rotor.

YadA bacterial adhesin protein domain

In molecular biology, YadA is a protein domain which is short for Yersinia adhesin A. These proteins have strong sequence and structural homology, particularly at their C-terminal end. The function is to promote their pathogenicity and virulence in host cells, though cell adhesion. YadA is found in three pathogenic species of Yersinia, Y. pestis,Y. pseudotuberculosis, and Y. enterocolitica. The YadA domain is encoded for by a virulence plasmid in Yersinia, which encodes a type-III secretion (T3S) system consisting of the Ysc injectisome and the Yop effectors.

Non-proteinogenic amino acids

In biochemistry, non-coded or non-proteinogenic amino acids are those not naturally encoded or found in the genetic code of any organism. Despite the use of only 22 amino acids by the translational machinery to assemble proteins, over 140 amino acids are known to occur naturally in proteins and thousands more may occur in nature or be synthesized in the laboratory. Many non-proteinogenic amino acids are noteworthy because they are;

The bacterial murein precursor exporter (MPE) family is a member of the cation diffusion facilitator (CDF) superfamily of membrane transporters. Members of the MPE family are found in a large variety of Gram-negative and Gram-positive bacteria and facilitate the translocation of lipid-linked murein precursors. A representative list of proteins belonging to the MPE family can be found in the Transporter Classification Database.

BamA is a β-barrel, outer membrane protein found in Gram-negative bacteria and it is the main and vital component of the β-barrel assembly machinery (BAM) complex in those bacteria. BAM Complex consists of five components; BamB, BamC, BamD, BamE and BamA. This complex is responsible in catalyzing folding and insertion of β-barrel proteins into the outer membrane of Gram-negative bacteria.

A proteolipid is a protein covalently linked to lipid molecules, which can be fatty acids or sterols. The process of such a linkage is known as protein lipidation, and falls into the wider category of acylation and post-translational modification. Proteolipids are abundant in brain tissue, and are also present in many other animal and plant tissues. They are proteins covalenently bound to fatty acid chains, often granting them an interface for interacting with biological membranes. They are not to be confused with lipoproteins, a kind of spherical assembly made up of many molecules of lipids and some apolipoproteins.

References

  1. Seltmann, Guntram; Holst, Otto (2002). The Bacterial Cell Wall. Berlin: Springer. pp. 81–82. ISBN   3-540-42608-6.
  2. Dramsi S, Magnet S, Davison S, Arthur M (2008). "Covalent attachment of proteins to peptidoglycan". FEMS Microbiology Reviews. 32 (2): 307–20. doi: 10.1111/j.1574-6976.2008.00102.x . PMID   18266854.
  3. 1 2 3 Konovalova A, Silhavy TJ (2015). "Outer membrane lipoprotein biogenesis: Lol is not the end". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 370 (1679). doi:10.1098/rstb.2015.0030. PMC   4632606 . PMID   26370942.
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  5. 1 2 Silhavy TJ, Kahne D, Walker S (2010). "The bacterial cell envelope". Cold Spring Harbor Perspectives in Biology. 2 (5): a000414. doi:10.1101/cshperspect.a000414. PMC   2857177 . PMID   20452953.
  6. Vollmer, Waldemar (2007). "Structure and biosynthesis of the murein (peptidoglycan) sacculus". In Ehrmann, Michael (ed.). The Periplasm ([Online-Ausg.]. ed.). Washington, DC: ASM Press. pp. 198–213. ISBN   9781555813987.
  7. Butler T (2009). "Plague into the 21st century". Clinical Infectious Diseases. 49 (5): 736–42. doi: 10.1086/604718 . PMID   19606935.
  8. Smiley ST (2008). "Immune defense against pneumonic plague". Immunological Reviews. 225: 256–71. doi:10.1111/j.1600-065X.2008.00674.x. PMC   2804960 . PMID   18837787.
  9. McIntyre TM, Prescott SM, Weyrich AS, Zimmerman GA (2003). "Cell-cell interactions: leukocyte-endothelial interactions". Current Opinion in Hematology. 10 (2): 150–8. doi:10.1097/00062752-200303000-00009. PMID   12579042.