Chemotaxis for enhanced immobilization of Escherichia coli and Legionella pneumophila on biofunctionalized surfaces of GaAs

Biointerphases. 2016 Jun 20;11(2):021004. doi: 10.1116/1.4947048.

Abstract

The authors have investigated the effect of chemotaxis on immobilization of bacteria on the surface of biofunctionalized GaAs (001) samples. Escherichia coli K12 bacteria were employed to provide a proof-of-concept of chemotaxis-enhanced bacterial immobilization, and then, these results were confirmed using Legionella pneumophila. The recognition layer was based on a self-assembled monolayer of thiol functionalized with specific antibodies directed toward E. coli or L. pneumophila, together with the enzyme beta-galactosidase (β-gal). The authors hypothesized that this enzyme together with its substrate lactose would produce a gradient of glucose which would attract bacteria toward the biochip surface. The chemotaxis effect was monitored by comparing the number of bacteria bound to the biochip surface with and without attractant. The authors have observed that β-gal plus lactose enhanced the immobilization of bacteria on our biochips with a higher effect at low bacterial concentrations. At 100 and 10 bacteria/ml, respectively, for E. coli and L. pneumophila, the authors observed up to 11 and 8 times more bacteria bound to biochip surfaces assisted with the chemotaxis effect in comparison to biochips without chemotaxis. At 10(4) bacteria/ml, the immobilization enhancement rate did not exceed two times.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Bacterial / metabolism
  • Arsenicals*
  • Bacterial Adhesion*
  • Cells, Immobilized / physiology*
  • Chemotaxis*
  • Enzymes, Immobilized / metabolism
  • Escherichia coli K12 / drug effects
  • Escherichia coli K12 / physiology*
  • Gallium*
  • Glucose / metabolism
  • Legionella pneumophila / drug effects
  • Legionella pneumophila / physiology*
  • beta-Galactosidase / metabolism

Substances

  • Antibodies, Bacterial
  • Arsenicals
  • Enzymes, Immobilized
  • gallium arsenide
  • Gallium
  • beta-Galactosidase
  • Glucose