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Related Experiment Videos

The C-type lectin fold as an evolutionary solution for massive sequence variation.

Stephen A McMahon1, Jason L Miller, Jeffrey A Lawton

  • 1Department of Chemistry & Biochemistry, University of California at San Diego, La Jolla, California 92093, USA.

Nature Structural & Molecular Biology
|September 20, 2005
PubMed
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The C-type lectin (CLec) fold, found in Bordetella phage Mtd proteins, allows for extensive sequence variation, enabling phage adaptation. This protein fold provides a stable scaffold for diverse receptor binding.

Area of Science:

  • Structural biology
  • Protein engineering
  • Microbial genetics

Background:

  • Protein folds that allow extensive sequence variation for binding diversity are rare.
  • The immunoglobulin fold is the most studied example of such a protein fold.
  • Bacteriophage Mtd proteins utilize a C-type lectin (CLec) fold for receptor binding and adaptation.

Purpose of the Study:

  • To identify and characterize novel protein folds that tolerate significant sequence variation.
  • To investigate the structural basis of receptor binding diversity in Bordetella bacteriophage Mtd.
  • To explore the evolutionary implications of the CLec fold in balancing protein stability and sequence diversity.

Main Methods:

  • Bioinformatic analysis of Bordetella bacteriophage genomes.

Related Experiment Videos

  • Structural analysis of the Mtd protein and its C-type lectin fold.
  • Sequence variation analysis of Mtd to assess binding diversity potential.

    • Main Results:

    • The C-type lectin (CLec) fold is identified as a protein fold that tolerates massive sequence variation.
    • The Mtd protein, encoded by Bordetella bacteriophage, exemplifies this CLec fold, enabling approximately 10^13 possible sequences.
    • The CLec fold acts as a static scaffold for displaying variable residues at discrete receptor-binding sites, facilitating phage adaptation to Bordetella species.
    • Mtd variants show a bias towards the pertactin receptor, suggesting a specific evolutionary trajectory.

    Conclusions:

    • The C-type lectin (CLec) fold represents a newly recognized structural solution for achieving extensive binding diversity while maintaining protein stability.
    • The Mtd protein's CLec fold provides a versatile platform for phage adaptation and evolution within Bordetella populations.
    • Evidence suggests the broad utilization of the CLec fold for sequence variation among related retroelements.