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Published on: July 30, 2012
Zebrafish CD59 has both bacterial-binding and inhibiting activities
Chen Sun1, Jie Wu, Shousheng Liu
1Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity and Department of Marine Biology, Ocean University of China, Qingdao 266003, China.
Developmental and Comparative Immunology
|May 28, 2013
Summary
Zebrafish CD59 (protectin) binds bacteria and their components, exhibiting novel antimicrobial activity beyond its complement inhibition role. This study characterizes its unique functions in zebrafish development and immunity.
Area of Science:
- Immunology
- Developmental Biology
- Genomics
Background:
- CD59 (protectin) is a complement regulatory protein.
- CD59 possesses functions beyond complement inhibition.
- The role of CD59 in non-mammalian vertebrates is largely unexplored.
Purpose of the Study:
- To identify and characterize a zebrafish (Danio rerio) ortholog of mammalian CD59.
- To investigate the expression pattern of zebrafish CD59.
- To explore potential novel functions of zebrafish CD59, including antimicrobial activity.
Main Methods:
- Sequence and genomic structure analysis of zebrafish cd59.
- Maternal and embryonic expression analysis.
- Recombinant protein expression and binding assays with bacteria (Gram-negative and Gram-positive) and microbial molecules (LPS, LTA).
- Antimicrobial activity assays against E. coli and S. aureus.
Main Results:
- Zebrafish cd59 is conserved in amino acid sequence, genomic structure, and synteny.
- Zebrafish CD59 is maternally expressed and shows tissue-specific expression, abundant in the brain.
- Recombinant zebrafish CD59 binds to Gram-negative and Gram-positive bacteria, LPS, and LTA.
- Recombinant zebrafish CD59 exhibits antimicrobial activity against E. coli and S. aureus.
Conclusions:
- Zebrafish CD59 is a conserved ortholog of mammalian CD59.
- Zebrafish CD59 plays a role in early development and has tissue-specific expression.
- Zebrafish CD59 possesses a novel, non-complement-dependent antimicrobial function, binding bacteria and inhibiting their growth.
