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Related Experiment Videos

Conservation in decay accelerating factor (DAF) structure among primates.

L Kuttner-Kondo1, V B Subramanian, J P Atkinson

  • 1Department of Pathology, Case Western Reserve University, School of Medicine, Cleveland, Ohio 44106, USA.

Developmental and Comparative Immunology
|July 25, 2000
PubMed
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The decay accelerating factor (DAF, CD55) is highly conserved across primates, with key functional sites remaining unchanged. Studies revealed variations in DAF protein isoforms and a Rhesus macaque model for a human blood group deficiency.

Area of Science:

  • Immunology
  • Molecular Biology
  • Genetics

Background:

  • The decay accelerating factor (DAF, CD55) is crucial for preventing self-cell complement activation by inhibiting C3 convertases.
  • DAF's functional sites are located within its four complement control protein (CCP) repeats, supported by a serine/threonine-rich region.
  • Previous research proposed specific amino acid residues in DAF's CCPs as critical for C3 convertase interaction.

Purpose of the Study:

  • To characterize the amino acid sequence and functional conservation of DAF in five non-human primate species.
  • To investigate potential variations in DAF protein isoforms due to alternative splicing in the S/T-rich region.
  • To identify primate models for human complement-related blood group phenotypes.

Main Methods:

Related Experiment Videos

  • Amino acid sequence analysis of DAF in gorillas, chimpanzees, hamadryas baboons, Rhesus macaques, and patas monkeys.
  • Comparative analysis of DAF homology with human sequences, focusing on putative ligand-interactive residues.
  • Investigation of alternative splicing in the S/T-rich region and its impact on DAF protein expression.

    • Main Results:

    • High amino acid homology to human DAF was observed (approx. 98% in great apes, 83% in Old World monkeys).
    • Putative ligand-interactive residues within DAF's CCPs were fully conserved across all studied primates.
    • Alternative splicing of the S/T region led to multiple DAF isoforms in chimpanzees but a single band in patas monkeys.
    • A Rhesus macaque exhibited a 44-base pair deletion in CCP3, mimicking the human Cromer Dr(a-) blood group phenotype.

    Conclusions:

    • DAF's critical functional regions are evolutionarily conserved across diverse primate species.
    • Variations in DAF alternative splicing contribute to protein isoform diversity.
    • Non-human primates, particularly Rhesus macaques, offer valuable models for studying human complement disorders and blood group variations.