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Related Concept Videos

Complement System01:27

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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An antigen is any substance the immune system identifies as foreign and potentially harmful to the body, prompting an immune response. Antigens have two functional properties: immunogenicity and reactivity. Immunogenicity is the ability of an antigen to stimulate a specific immune response. At the same time, reactivity describes the antigen's ability to react with the cells and antibodies produced in response to it.
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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
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Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain,...
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Glycocalyx and its Functions01:14

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Author Spotlight: Dendritic Cells Maturation Using Sialidases-Based Enzymatic Treatment of the Cell Surface
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Structural basis for sialic acid-mediated self-recognition by complement factor H.

Bärbel S Blaum1, Jonathan P Hannan2, Andrew P Herbert3

  • 1Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.

Nature Chemical Biology
|November 18, 2014
PubMed
Summary
This summary is machine-generated.

Complement factor H binds sialylated glycans to regulate innate immunity. This study reveals its binding site structure, crucial for human kidney health and bacterial evasion.

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • Complement factor H (FH) regulates the complement alternative pathway, a key part of innate immunity.
  • FH interacts with host cell surface glycans to prevent complement-mediated damage.

Purpose of the Study:

  • To investigate the binding interaction between FH and sialylated glycans.
  • To determine the structural basis of FH-glycan recognition and its implications for complement homeostasis.

Main Methods:

  • Ligand-based Nuclear Magnetic Resonance (NMR) screening of sialylated glycans.
  • X-ray crystallography to solve the structure of a ternary complex involving FH domains, a sialylated trisaccharide, and C3b.

Main Results:

  • Identified specific sialylated glycans that bind to FH.
  • Determined the crystal structure of a ternary complex, revealing the FH sialic acid binding site.
  • Found conservation of key binding residues across species and identified a link between atypical hemolytic uremic syndrome and this binding site.

Conclusions:

  • Sialic acid recognition by FH is critical for human renal complement homeostasis.
  • The FH binding site's structural homology to other proteins offers new insights.
  • Understanding this interaction is vital for deciphering bacterial immune evasion strategies.