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Horse complement protein C9: primary structure and cytotoxic activity

A F Esser1, R W Tarnuzzer, S Tomlinson

  • 1Department of Comparative and Experimental Pathology, University of Florida Health Science Center, Gainesville, USA.

Molecular Immunology
|May 1, 1996
PubMed
Summary
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Horse C9 protein lacks hemolytic activity, but efficiently kills bacteria. Structural analysis reveals no obvious differences from hemolytic bovine C9, suggesting other factors influence red blood cell lysis.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Horse serum C9 (Complement 9) protein is known for its lack of hemolytic activity.
  • Understanding the molecular basis for this deficiency is crucial for comprehending complement system function.

Purpose of the Study:

  • To elucidate the molecular reasons behind the deficiency in hemolytic activity of horse C9.
  • To compare the structure and function of horse C9 with other species, particularly human and bovine C9.

Main Methods:

  • Cloning and sequencing of horse C9 cDNA from a horse liver cDNA library.
  • Purification of C9 protein from horse plasma and subsequent microsequencing.
  • Amino acid sequence analysis and comparison with human and bovine C9.

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Main Results:

  • Horse C9 cDNA encodes a mature protein of 526 amino acids, 77% identical to human C9.
  • Identical domain structure and conserved regions, including the membrane interaction domain, were observed.
  • Horse C9 exhibits efficient cytotoxic activity against Gram-negative bacteria, despite lacking hemolytic activity.

Conclusions:

  • Horse C9 is a structurally sound molecule with potent antibacterial cytotoxic activity.
  • The inability of horse C9 to lyse erythrocytes may be due to interactions with regulatory proteins or target cell membranes, rather than intrinsic structural defects.