Maggots and wound healing: an investigation of the effects of secretions from Lucilia sericata larvae upon the migration of human dermal fibroblasts over a fibronectin-coated surface

Wound Repair Regen. 2005 Jul-Aug;13(4):422-33. doi: 10.1111/j.1067-1927.2005.130410.x.


Lucilia sericata larvae, or greenbottle fly maggots, placed within chronic wounds have been observed to remove necrotic tissue and infection. They are also believed to actively promote granulation tissue formation. Interactions between fibroblasts and the surrounding extracellular matrix play a crucial role in tissue formation, influencing fibroblast proliferation, migration, and tissue remodeling. For example, the strength of cell adhesion to surfaces coated with extracellular matrix influences cell motility. L. sericata larval excretory/secretory products having previously been shown to modify fibroblast adhesion to collagen and particularly fibronectin, it was hypothesized that these products would alter fibroblast migration. This was investigated using a two-dimensional in vitro wound assay, time-lapse digital photography, enzyme class-specific substrates and inhibitors, and gel electrophoresis. Results showed that L. sericata excretory/secretory products promoted fibroblast migration upon a fibronectin-coated surface. This was related to the degradation of fibronectin by serine proteinases within maggot excretion/secretions. The presence of a metalloproteinase activity may also have played a role. Thus, a possible mechanism by which maggots enhance tissue formation within wounds may be via the promotion of fibroblast motility, providing for a wider distribution of viable fibroblasts.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Movement / drug effects*
  • Cells, Cultured
  • Dermis
  • Fibroblasts / drug effects*
  • Fibronectins
  • Humans
  • In Vitro Techniques
  • Infant, Newborn
  • Larva / physiology*
  • Peptide Hydrolases / physiology
  • Wound Healing*


  • Fibronectins
  • Peptide Hydrolases