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Molecular basis for manganese sequestration by calprotectin and roles in the innate immune response to invading bacterial pathogens.

Abstract：

:The S100A8/S100A9 heterodimer calprotectin (CP) functions in the host response to pathogens through a mechanism termed "nutritional immunity." CP binds Mn(2+) and Zn(2+) with high affinity and starves bacteria of these essential nutrients. Combining biophysical, structural, and microbiological analysis, we identified the molecular basis of Mn(2+) sequestration. The asymmetry of the CP heterodimer creates a single Mn(2+)-binding site from six histidine residues, which distinguishes CP from all other Mn(2+)-binding proteins. Analysis of CP mutants with altered metal-binding properties revealed that, despite both Mn(2+) and Zn(2+) being essential metals, maximal growth inhibition of multiple bacterial pathogens requires Mn(2+) sequestration. These data establish the importance of Mn(2+) sequestration in defense against infection, explain the broad-spectrum antimicrobial activity of CP relative to other S100 proteins, and clarify the impact of metal depletion on the innate immune response to infection.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Damo SM,Kehl-Fie TE,Sugitani N,Holt ME,Rathi S,Murphy WJ,Zhang Y,Betz C,Hench L,Fritz G,Skaar EP,Chazin WJ

doi

10.1073/pnas.1220341110

subject

Has Abstract

pub_date

2013-03-05 00:00:00

pages

3841-6

issue

10

eissn

0027-8424

issn

1091-6490

pii

1220341110

journal_volume

110

pub_type

杂志文章

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