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Biology (Basel). 2014 Mar 10;3(1):178-204. doi: 10.3390/biology3010178.

Dancing to another tune-adhesive moonlighting proteins in bacteria.

Author information

1
Department of Veterinary Biosciences, University of Helsinki, P.O. Box 66, FI-00014 Helsinki, Finland. veera.kainulainen@helsinki.fi.
2
General Microbiology, Department of Biosciences, University of Helsinki, P.O. Box 56, FI-00014 Helsinki, Finland. timo.korhonen@helsinki.fi.

Abstract

Biological moonlighting refers to proteins which express more than one function. Moonlighting proteins occur in pathogenic and commensal as well as in Gram-positive and Gram-negative bacteria. The canonical functions of moonlighting proteins are in essential cellular processes, i.e., glycolysis, protein synthesis, chaperone activity, and nucleic acid stability, and their moonlighting functions include binding to host epithelial and phagocytic cells, subepithelia, cytoskeleton as well as to mucins and circulating proteins of the immune and hemostatic systems. Sequences of the moonlighting proteins do not contain known motifs for surface export or anchoring, and it has remained open whether bacterial moonlighting proteins are actively secreted to the cell wall or whether they are released from traumatized cells and then rebind onto the bacteria. In lactobacilli, ionic interactions with lipoteichoic acids and with cell division sites are important for surface localization of the proteins. Moonlighting proteins represent an abundant class of bacterial adhesins that are part of bacterial interactions with the environment and in responses to environmental changes. Multifunctionality in bacterial surface proteins appears common: the canonical adhesion proteins fimbriae express also nonadhesive functions, whereas the mobility organelles flagella as well as surface proteases express adhesive functions.

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