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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 membrane...
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Engineering novel complement activity into a pulmonary surfactant protein.

Umakhanth Venkatraman Girija1, Christopher Furze, Julia Toth

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The Journal of Biological Chemistry
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Area of Science:

  • Immunology
  • Biochemistry

Background:

  • The complement system is crucial for innate and adaptive immunity, neutralizing pathogens and clearing cellular debris.
  • Activation pathways, including the lectin pathway, rely on recognition complexes binding to pathogen surfaces.
  • Mannose-binding lectins (MBLs) and ficolins share structural similarities with C1q, all associating with serine proteases for complement activation.

Purpose of the Study:

  • To investigate the structural requirements for complement activation by modifying MBLs and engineering MASP binding into SP-A.
  • To understand the role of MASP binding sites and collagenous stalks in MBL-mediated complement initiation.

Main Methods:

  • Creation of novel recombinant rat MBLs with altered MASP-binding site positions and orientations.
  • Engineering MASP binding into pulmonary surfactant protein-A (SP-A) to assess its complement activity.
  • Analysis of complement activation in response to structural modifications and the presence/absence of carbohydrate targets.

Main Results:

  • Complement activity demonstrates high tolerance to alterations in MBL collagenous stalk size and orientation, indicating flexibility.
  • Engineered SP-A gained novel complement activity upon MASP binding, even without a carbohydrate target.
  • The default state of lectin-MASP complexes is active, requiring inhibitory regions in MBLs for regulation until pathogen recognition.

Conclusions:

  • The structural flexibility of MBLs allows for significant modifications without compromising complement activity.
  • MASP binding alone can confer uncontrolled complement activity, highlighting the importance of regulatory mechanisms.
  • Circulating MBLs must maintain an inhibited state to prevent spontaneous complement activation, relying on pathogen recognition for triggering.