Lipopolysaccharide binding protein

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Lipopolysaccharide binding protein (LBP) is a type of protein that plays a crucial role in the immune system's response to bacterial infection. It is primarily produced in the liver and is found in the blood plasma.

Function[edit | edit source]

LBP is responsible for binding to lipopolysaccharides (LPS), which are components of the outer membrane of Gram-negative bacteria. This binding process is a key step in the body's immune response to bacterial infections. Once LBP has bound to LPS, it transfers the LPS to CD14, a protein found on the surface of certain immune cells. This triggers a cascade of immune responses, including the release of cytokines and the activation of white blood cells, which help to fight off the infection.

Structure[edit | edit source]

The structure of LBP is complex, consisting of several different domains. The N-terminal domain is responsible for binding to LPS, while the C-terminal domain is involved in the transfer of LPS to CD14. The structure of LBP is similar to that of other lipid-binding proteins, such as bile acid-binding protein and fatty acid-binding protein.

Clinical significance[edit | edit source]

Abnormal levels of LBP in the blood can be indicative of a number of medical conditions. High levels of LBP are often seen in patients with sepsis, a severe and potentially life-threatening response to infection. LBP levels can also be elevated in patients with liver disease, kidney disease, and certain types of cancer. As such, LBP is often used as a biomarker in the diagnosis and monitoring of these conditions.

File:Lipopolysaccharide binding protein.jpg
Structure of Lipopolysaccharide binding protein

See also[edit | edit source]

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Contributors: Prab R. Tumpati, MD