Three-dimensional fine structural reconstruction of the nose sensory structures of Acrobeles complexus compared to Caenorhabditis elegans (Nematoda: Rhabditida)

J Morphol. 2007 Aug;268(8):649-63. doi: 10.1002/jmor.10535.

Abstract

Nematode sensory structures can be divided into two classes; cuticular sensillae, with dendrites ending outside the epidermis, and internal receptors, that typically are single dendrites terminating within the body cavity. Fine structure of the former has been described completely in more than a dozen nematode taxa, while the latter were previously only well understood in the microbial feeder Caenorhabditis elegans. The distantly related nematode Acrobeles complexus has a similar ecology and together the two span a clade representing a large proportion of nematode biodiversity. The cuticular sensillae and internal receptors of A. complexus are here shown to be remarkably similar in number, arrangement, and morphology to those of C. elegans. Several key differences are reported that likely relate to function, and suggest that this nematode has a cuticular sensillum morphology that is closer to that of the common ancestor of the two taxa. Internal sensory receptors have more elaborate termini than those of C. elegans. The existence of a novel form of mechanoreceptor in A. complexus and spatial relationships between sensillum dendrites suggest differences between two classes of sensillae in how a touch-response behavior may be mediated.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Animals
  • Caenorhabditis elegans / anatomy & histology
  • Caenorhabditis elegans / cytology
  • Caenorhabditis elegans / ultrastructure*
  • Microscopy, Electron, Transmission
  • Models, Anatomic
  • Nose / anatomy & histology*
  • Nose / innervation*
  • Nose / ultrastructure
  • Phylogeny
  • Rhabditida / anatomy & histology
  • Rhabditida / cytology
  • Rhabditida / ultrastructure*
  • Sensory Receptor Cells / ultrastructure*