Outer membrane in Gram-negative

When deficient in iron, bacteria and fungi produce and excrete to the extracellular medium low molecular weight, specific iron-carrier molecules, called siderophores. These siderophores bind ferric ions, to form soluble complexes. The complexed ferric ions are transported into the cell through high-affinity and energy-dependent receptor proteins located on the outer membrane. In Gram-negative bacteria, such as E. coli, the most studied system, siderophore-iron complexes are transported initially to the periplasm. 

On the principle that blocking the incorporation of 3-deoxy- B-D-manno-octulopyranosonic acid (110) in the biosynthesis of the outer membrane in Gram-negative bacteria might lead to new types of antibacterial agents, the 1,2-oxaphosphorinane analogue... 

Periplasmic space The space between the cell membrane and the outer membrane in Gram-negative bacteria that is filled with periplasm. 

As shown in Figure 9.24, the outer membrane of Gram-negative bacteria is coated with a highly complex lipopolysaccharide, which consists of a lipid group (anchored in the outer membrane) joined to a polysaccharide made up of long chains with many different and characteristic repeating structures... 

Endotoxins are the lipopolysaccharides (LPS) of the outer membrane of Gram-negative bacteria. They trigger inflammatory reactions in the infected organism, activate complement and cause fever or even a septic shock. They act on toll-like receptors. 

Figure 7.7 Structure of a generalized LPS molecule. LPS constitutes the major structural component of the outer membrane of Gram-negative bacteria. Although LPSs of different Gram-negative organisms differ in their chemical structure, each consists of a complex polysaccharide component, linked to a lipid component. Refer to text for specific details...

LPS, the immunoactive component of endotoxin, is a constituent of the outer membrane of Gram-negative bacterial cell walls. LPS is found in the environment and has been extensively studied, both as a mediator of inflammation and as a major contributing factor to bacterial pathogenesis.60 LPS exerts many of its effects through induction of pro-inflammatory cytokines, including IL-ip, TNF-a and IL-6.61 An important feature... 

Carbohydrates related to membranes can be found as lipopolysaccharides or as parts of glycoproteins. Sugars are often characteristic determinants of cell surfaces (see below). The great majority of carbohydrates are found in the outer leaflet of a membrane, resulting in an asymmetrical structure. This is especially true for many plasma membranes and the outer membrane of Gram-negative bacterial cells (see below). 

The insertion of (i-barrel precursors is one of the two translocation processes, besides the sorting of inner membrane and IMS proteins, that are clearly derived from a eubacterial translocation system. (1-Barrel proteins are exclusively found in the outer membranes of Gram-negative bacteria and of endosymbiotic organelles such as mitochondria and plastids (Wim-... 

Lipopolysaccharides are the dominant surface feature of the outer membrane of gram-negative bacteria such as Escherichia coli and Salmonella ty-phimurium. These molecules are prime targets of the antibodies produced by the vertebrate immune system in response to bacterial infection and are therefore important determinants of the serotype of bacterial strains (serotypes are strains that are distinguished on the basis of antigenic properties). The lipopolysaccharides of S. typhimurium contain six fatty acids bound to two... 

Transport and Cell Penetration. One of the causes of bacterial resistance to the cephalosporins is poor transport of the antibiotic through tlie outer membrane of gram-negative bacteria. This lipid-bilayer membrane carries receptor proteins for the recognition and transport of essential nutrients, but provides an effective barrier to large molecules. In the case of the cephalosporins there can be a considerable difference between the concentration required to inhibit intact cells and the concentrations required to saturate the target enzymes in broken cell piepaiations. 

While gramicidin and other channel formers can show high transport rates, they do not show the high selectivity that characterizes natural channels. There is much interest at present in a class of proteins called porins, which form natural pores in the outer membranes of Gram-negative bacteria. Several different porin proteins have been isolated from Escherichia coli. These form water-filled channels of various sizes in membranes. Thus the proteins OmpC and OmpF seem to be cation-specific channels while other proteins give larger diameter channels that seem to be specific for anions.34,35... 

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