Bacterial Lipoproteins Constitute the TLR2-Stimulating Activity of Serum Amyloid A | Zendy

Edward J. Burgess | Zendy; Laura R. Hoyt | Zendy; Matthew J. Randall | Zendy; Madeleine M. Mank | Zendy; Joseph J. Bivona | Zendy; Philip Eisenhauer | Zendy; Jason Botten | Zendy; Bryan A. Ballif | Zendy; YingWai Lam | Zendy; Matthew J. Wargo | Zendy; Jonathan E. Boyson | Zendy; Jennifer L. Ather | Zendy; Matthew E. Poynter | Zendy

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Bacterial Lipoproteins Constitute the TLR2-Stimulating Activity of Serum Amyloid A

Author(s) -

Edward J. Burgess,

Laura R. Hoyt,

Matthew J. Randall,

Madeleine M. Mank,

Joseph J. Bivona,

Philip Eisenhauer,

Jason Botten,

Bryan A. Ballif,

YingWai Lam,

Matthew J. Wargo,

Jonathan E. Boyson,

Jennifer L. Ather,

Matthew E. Poynter

Publication year - 2018

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.1800503

Subject(s) - recombinant dna , proinflammatory cytokine , lipopeptide , tlr2 , serum amyloid a , escherichia coli , lipoprotein , endogeny , amyloid (mycology) , function (biology) , biology , chemistry , biochemistry , microbiology and biotechnology , bacteria , immunology , inflammation , receptor , innate immune system , cholesterol , genetics , gene , botany

Studies comparing endogenous and recombinant serum amyloid A (SAA) have generated conflicting data on the proinflammatory function of these proteins. In exploring this discrepancy, we found that in contrast to commercially sourced recombinant human SAA1 (hSAA1) proteins produced in Escherichia coli , hSAA1 produced from eukaryotic cells did not promote proinflammatory cytokine production from human or mouse cells, induce Th17 differentiation, or stimulate TLR2. Proteomic analysis of E. coli -derived hSAA1 revealed the presence of numerous bacterial proteins, with several being reported or probable lipoproteins. Treatment of hSAA1 with lipoprotein lipase or addition of a lipopeptide to eukaryotic cell-derived hSAA1 inhibited or induced the production of TNF-α from macrophages, respectively. Our results suggest that a function of SAA is in the binding of TLR2-stimulating bacterial proteins, including lipoproteins, and demand that future studies of SAA employ a recombinant protein derived from eukaryotic cells.

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