Zinc sequestration by the neutrophil protein calprotectin enhances salmonella growth in the inflamed gut

Janet Z. Liu, Stefan Jellbauer, Adam J. Poe, Vivian Ton, Michele Pesciaroli, Thomas E. Kehl-Fie, Nicole A. Restrepo, Martin P. Hosking, Robert A. Edwards, Andrea Battistoni, Paolo Pasquali, Thomas E. Lane, Walter J. Chazin, Thomas Vogl, Johannes Roth, Eric P. Skaar, Manuela Raffatellu

Research output: Contribution to journalArticlepeer-review


Neutrophils are innate immune cells that counter pathogens by many mechanisms, including release of antimicrobial proteins such as calprotectin to inhibit bacterial growth. Calprotectin sequesters essential micronutrient metals such as zinc, thereby limiting their availability to microbes, a process termed nutritional immunity. We find that while calprotectin is induced by neutrophils during infection with the gut pathogen Salmonella Typhimurium, calprotectin-mediated metal sequestration does not inhibit S. Typhimurium proliferation. Remarkably, S. Typhimurium overcomes calprotectin-mediated zinc chelation by expressing a high affinity zinc transporter (ZnuABC). A S. Typhimurium znuA mutant impaired for growth in the inflamed gut was rescued in the absence of calprotectin. ZnuABC was also required to promote the growth of S. Typhimurium over that of competing commensal bacteria. Thus, our findings indicate that Salmonella thrives in the inflamed gut by overcoming the zinc sequestration of calprotectin and highlight the importance of zinc acquisition in bacterial intestinal colonization.

Original languageEnglish (US)
Pages (from-to)227-239
Number of pages13
JournalCell Host and Microbe
Issue number3
StatePublished - Mar 15 2012
Externally publishedYes

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Virology


Dive into the research topics of 'Zinc sequestration by the neutrophil protein calprotectin enhances salmonella growth in the inflamed gut'. Together they form a unique fingerprint.

Cite this