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Lipopolysaccharide is a significant factor that makes bacteria harmful, and it helps categorize them into different groups based on their structure and function. This makes LPS a useful marker for telling apart various Gram-negative bacteria.
Chemical structure of lipid A as found in E. coli [1]. Lipid A is a lipid component of an endotoxin held responsible for the toxicity of gram-negative bacteria.It is the innermost of the three regions of the lipopolysaccharide (LPS), also called endotoxin molecule, and its hydrophobic nature allows it to anchor the LPS to the outer membrane. [2]
Bacterial lipopolysaccharides (LPSs), also known as endotoxins, are found on the cell membranes of gram-negative bacteria, [10] are considered to be the prototypical class of PAMPs. The lipid portion of LPS, lipid A, contains a diglycolamine backbone with multiple acyl chains.
Lipopolysaccharide binding protein (LBP) is a protein that in humans is encoded by the LBP gene. [ 5 ] [ 6 ] LBP is a soluble acute-phase protein that binds to bacterial lipopolysaccharide (or LPS) to elicit immune responses by presenting the LPS to important cell surface pattern recognition receptors called CD14 and TLR4 .
Galactogen is a polysaccharide of galactose that functions as energy storage in pulmonate snails and some Caenogastropoda. [23] This polysaccharide is exclusive of the reproduction and is only found in the albumen gland from the female snail reproductive system and in the perivitelline fluid of eggs. [ 24 ]
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 ...
CD14 (cluster of differentiation 14) is a human protein made mostly by macrophages as part of the innate immune system. [5] [6] It helps to detect bacteria in the body by binding lipopolysaccharide (LPS), a pathogen-associated molecular pattern (PAMP).
The MD-2 protein appears to associate with toll-like receptor 4 on the cell surface and confers responsiveness to lipopolysaccharide (LPS), thus providing a link between the receptor and LPS signaling. [7] That is, the primary interface between TLR4 and MD-2 is formed before binding LPS and the dimerization interface is induced by binding LPS. [8]