Recent findings on the viable but nonculturable state in pathogenic bacteria

FEMS Microbiol Rev. 2010 Jul;34(4):415-25. doi: 10.1111/j.1574-6976.2009.00200.x. Epub 2009 Nov 24.

Abstract

Many bacteria, including a variety of important human pathogens, are known to respond to various environmental stresses by entry into a novel physiological state, where the cells remain viable, but are no longer culturable on standard laboratory media. On resuscitation from this 'viable but nonculturable' (VBNC) state, the cells regain culturability and the renewed ability to cause infection. It is likely that the VBNC state is a survival strategy, although several interesting alternative explanations have been suggested. This review describes the VBNC state, the various chemical and physical factors known to induce cells into this state, the cellular traits and gene expression exhibited by VBNC cells, their antibiotic resistance, retention of virulence and ability to attach and persist in the environment, and factors that have been found to allow resuscitation of VBNC cells. Along with simple reversal of the inducing stresses, a variety of interesting chemical and biological factors have been shown to allow resuscitation, including extracellular resuscitation-promoting proteins, a novel quorum-sensing system (AI-3) and interactions with amoeba. Finally, the central role of catalase in the VBNC response of some bacteria, including its genetic regulation, is described.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Animals
  • Bacteria / growth & development
  • Bacteria / isolation & purification*
  • Bacteria / pathogenicity*
  • Bacterial Adhesion
  • Bacterial Infections / microbiology*
  • Bacterial Physiological Phenomena*
  • Bacterial Proteins / metabolism
  • Catalase / metabolism
  • Drug Resistance, Bacterial
  • Gene Expression Profiling
  • Gene Expression Regulation, Bacterial
  • Humans
  • Microbial Viability*
  • Quorum Sensing

Substances

  • Bacterial Proteins
  • Catalase