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Complement System01:27

Complement System

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 membrane...
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Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
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Selectins

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, which...
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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
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Immunoglobulin-like Cell Adhesion Molecules

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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Carbohydrate recognition and complement activation by rat ficolin-B.

Umakhanth Venkatraman Girija1, Daniel A Mitchell, Silke Roscher

  • 1Department of Infection, Immunity and Inflammation, University of Leicester, Leicester, UK.

European Journal of Immunology
|December 25, 2010
PubMed
Summary
This summary is machine-generated.

Rat ficolin-B, unlike its mouse counterpart, binds to MASP-2 and activates complement. This study reveals key structural differences in ficolin-B that impact innate immune responses.

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Area of Science:

  • Innate immunity
  • Complement system
  • Structural biology

Background:

  • Ficolins are crucial innate immune proteins recognizing pathogen-associated molecular patterns (PAMPs) and apoptotic cells.
  • Mammalian ficolins exhibit species-specific variations in structure and function, particularly ficolin-B orthologues.
  • Mouse ficolin-B lacks the ability to bind mannan-binding lectin-associated serine proteases (MASPs) and activate complement.

Purpose of the Study:

  • To characterize rat ficolin-B and compare its properties to rat ficolin-A.
  • To investigate the functional differences between rodent ficolin-B orthologues and their human counterparts.
  • To elucidate the molecular basis for the lack of complement activation by mouse ficolin-B.

Main Methods:

  • Biochemical characterization of rat ficolin-A and ficolin-B.
  • Ligand-binding assays to determine carbohydrate specificity.
  • Complement activation assays using MASP-2.
  • Site-directed mutagenesis to identify critical amino acid residues.

Main Results:

  • Both rat ficolins possess archetypal oligomeric structures.
  • Rat ficolin-B exhibits broad specificity for sialylated sugars, while rat ficolin-A shows narrow specificity for an N-acetylated trisaccharide.
  • Rat ficolin-B effectively activates MASP-2, comparable to ficolin-A.
  • A single amino acid change in the MASP-binding site of mouse ficolin-B likely prevents MASP interaction and complement activation.

Conclusions:

  • Rat ficolin-B is functionally active in complement activation, contrasting with mouse ficolin-B.
  • Species-specific amino acid substitutions significantly influence ficolin-MASP interactions and complement pathway function.
  • Understanding these variations is critical for deciphering innate immune mechanisms across species.