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Related Experiment Videos

Domain structure, functional activity, and polymerization of trout complement protein C9

S Tomlinson1, K K Stanley, A F Esser

  • 1Department of Comparative and Experimental Pathology, University of Florida, Gainesville 32610.

Developmental and Comparative Immunology
|January 1, 1993
PubMed
Summary

Trout complement C9 has a unique thrombospondin domain that enables polymerization and forms smaller membrane attack complexes. Trout C9 and C8 do not interact with human complement components.

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Area of Science:

  • Immunology
  • Complement System
  • Comparative Genomics

Background:

  • The terminal complement pathway, crucial for immune defense, involves complement C9 polymerization to form membrane attack complexes.
  • Previous studies suggested that a thrombospondin domain in C9 might hinder polymerization, a hypothesis needing further investigation.
  • Understanding variations in complement components across species, like trout C9, offers insights into immune system evolution and function.

Purpose of the Study:

  • To resequence and characterize the trout C9 molecule, focusing on its 3' region and the presence of a thrombospondin domain.
  • To investigate the functional role of the trout C9 thrombospondin domain in complement polymerization and membrane attack complex formation.
  • To compare the structure and function of trout C9 and its interaction with other complement components to human counterparts.

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Main Methods:

  • Resequencing of the 3' region of trout C9.
  • Alternative pathway activation of trout complement using rabbit erythrocytes.
  • Analysis of membrane attack complex formation and lesion morphology on erythrocyte membranes.
  • Cross-species complement component interaction assays using human and trout serum components.

Main Results:

  • The resequenced trout C9 contains an additional carboxy-terminal thrombospondin domain, differing from previously published sequences.
  • This thrombospondin domain does not inhibit polymerization, as evidenced by the formation of circular membrane attack complexes on erythrocytes.
  • Trout membrane attack complexes are smaller than human counterparts, and trout C8/C9 do not interact with human C7/C8.
  • Trout and human sera exhibit similar efficacy against Salmonella minnesota Re595.

Conclusions:

  • Trout C9 possesses a functional thrombospondin domain that facilitates polymerization, contrary to previous hypotheses.
  • Structural differences exist between trout and human C9, resulting in smaller membrane attack complexes in trout.
  • Trout complement components C8 and C9 exhibit species-specific binding, unable to interact with human complement intermediates.
  • Despite structural variations, trout complement demonstrates effective antimicrobial activity against certain bacterial strains.