Putting life on ice: Bacteria that bind to frozen water

Maya Bar Dolev, Reut Bernheim, Shuaiqi Guo, Peter L. Davies, Ido Braslavsky*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

53 Scopus citations


Ice-binding proteins (IBPs) are typically small, soluble proteins produced by cold-adapted organisms to help them avoid ice damage by either resisting or tolerating freezing. By contrast, the IBP of the Antarctic bacterium Marinomonas primoryensis is an extremely long, 1.5 MDa protein consisting of five different regions. The fourth region, a 34 kDa domain, is the only part that confers ice binding. Bioinformatic studies suggest that this IBP serves as an adhesin that attaches the bacteria to ice to keep it near the top of the water column, where oxygen and nutrients are available. Using temperature-controlled cells and a microfluidic apparatus, we show that M. primoryensis adheres to ice and is only released when melting occurs. Binding is dependent on the mobility of the bacterium and the functionality of the IBP domain. A polyclonal antibody raised against the IBP region blocks bacterial ice adhesion. This concept may be the basis for blocking biofilm formation in other bacteria, including pathogens. Currently, this IBP is the only known example of an adhesin that has evolved to bind ice.

Original languageAmerican English
Article number20160210
JournalJournal of the Royal Society Interface
Issue number121
StatePublished - 1 Aug 2016

Bibliographical note

Publisher Copyright:
© 2016 The Authors.


  • Antifreeze proteins
  • Biofilm
  • Cold adaptation
  • Ice-binding proteins
  • Microfluidic cold finger
  • RTX adhesin


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