Bacterial moonlighting proteins and bacterial virulence

Curr Top Microbiol Immunol. 2013;358:155-213. doi: 10.1007/82_2011_188.


Implicit in the central dogma is the hypothesis that each protein gene product has but one function. However, over the past decade, it has become clear that many proteins have one or more unique functions, over-and-above the principal biological action of the specific protein. This phenomenon is now known as protein moonlighting and many well-known proteins such as metabolic enzymes and molecular chaperones are now recognised as moonlighting proteins. A growing number of bacterial species are being found to have moonlighting proteins and the moonlighting activities of such proteins can contribute to bacterial virulence behaviour. The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPD) and enolase, and the cell stress proteins: chaperonin 60, Hsp70 and peptidyl prolyl isomerase, are among the most common of the bacterial moonlighting proteins which play a role in bacterial virulence. Moonlighting activities include adhesion and modulation of cell signalling processes. It is likely that only the tip of the bacterial moonlighting iceberg has been sighted and the next decade will bring with it many new discoveries of bacterial moonlighting proteins with a role in bacterial virulence.

Publication types

  • Review

MeSH terms

  • Adhesins, Bacterial / chemistry
  • Adhesins, Bacterial / genetics
  • Adhesins, Bacterial / metabolism
  • Animals
  • Bacteria / genetics
  • Bacteria / metabolism*
  • Bacteria / pathogenicity*
  • Bacterial Infections / microbiology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Humans
  • Virulence


  • Adhesins, Bacterial
  • Bacterial Proteins