Abstract
The cuticle of Caenorhabditis elegans, a complex, multi-layered extracellular matrix, is a major interface between the animal and its environment. Biofilms produced by the bacterial genus Yersinia attach to the cuticle of the worm, providing an assay for surface characteristics. A C. elegans gene required for biofilm attachment, bah-1, encodes a protein containing the domain of unknown function DUF23. The DUF23 domain is found in 61 predicted proteins in C. elegans, which can be divided into three distinct phylogenetic clades. bah-1 is expressed in seam cells, which are among the hypodermal cells that synthesize the cuticle, and is regulated by a TGF-β signaling pathway.
Highlights
The cuticle of the nematode Caenorhabditis elegans is vital for proper morphology, locomotion, and protection from pathogens and environmental stresses [1]
No biofilm attaches to bah-1 animals in adult (Figure 1) or larval stages, and their development is identical whether fed E. coli or Yersinia
yeast artificial chromosome (YAC) spanning this interval were injected into bah-1 animals and transgenic lines established for each clone
Summary
The cuticle of the nematode Caenorhabditis elegans is vital for proper morphology, locomotion, and protection from pathogens and environmental stresses [1]. The cuticle basal layer is attached to the hypodermal cells [1], and distal to it are the medial and cortical layers. The most distal layer, the surface coat, is poorly characterized. It can be visualized in transmission electron microscopy with cationized ferritin particles, suggesting that it is anionic [2], and indirect evidence suggests that the surface coat contains O-linked glycoproteins [6]. In the parasitic nematode Toxocara canis the surface coat is labile, requiring only ethanol for extraction [7], but this has not been examined for C. elegans
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