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Related Experiment Videos

Distinct carbohydrate recognition domains of an invertebrate defense molecule recognize Gram-negative and

M Bilej1, P De Baetselier, E Van Dijck

  • 1Department of Immunology, Institute of Microbiology, Academy of Sciences of the Czech Republic, Prague 4, Czech Republic.

The Journal of Biological Chemistry
|October 5, 2001
PubMed
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Earthworm coelomic fluid contains a defense molecule, coelomic cytolytic factor (CCF), that recognizes diverse microbial patterns. CCF utilizes two distinct domains to bind pathogen-associated molecular patterns, initiating immune responses.

Area of Science:

  • Invertebrate immunology
  • Molecular recognition
  • Biochemistry

Background:

  • The coelomic fluid of Eisenia foetida earthworms contains a 42-kDa defense molecule, coelomic cytolytic factor (CCF).
  • CCF plays a role in the innate immune response by binding microbial antigens and activating the prophenoloxidase cascade.
  • Known binding targets for CCF include lipopolysaccharide (LPS), beta-1,3-glucans, and N,N'-diacetylchitobiose.

Purpose of the Study:

  • To identify the specific pattern recognition domains within the CCF molecule.
  • To elucidate how CCF recognizes a broad range of pathogen-associated molecular patterns (PAMPs).
  • To understand the structural basis for CCF's interaction with different microbial components.

Main Methods:

  • Deletion mutants of CCF were analyzed for their ability to reconstitute the prophenoloxidase cascade.

Related Experiment Videos

  • Experiments were conducted using coelomic fluid depleted of endogenous CCF and supplemented with various PAMPs (LPS, beta-1,3-glucans, N,N'-diacetylchitobiose, muramic acid).
  • Affinity chromatography of CCF peptides on immobilized beta-1,3-glucans and N,N'-diacetylchitobiose was performed.

    • Main Results:

    • CCF possesses two distinct pattern recognition domains responsible for its broad specificity.
    • A central domain, homologous to glucanase motifs, interacts with LPS and beta-1,3-glucans.
    • A C-terminal tryptophan-rich domain mediates interactions with N,N'-diacetylchitobiose and muramic acid.

    Conclusions:

    • The broad PAMP recognition of CCF is attributed to two spatially distinct carbohydrate recognition domains.
    • These findings reveal a sophisticated molecular mechanism for innate immunity in invertebrates.
    • The study highlights the presence of specialized domains for carbohydrate recognition within an invertebrate defense molecule.