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

The Journal of Immunology : Official Journal of the American Association of Immunologists
Edward J BurgessMatthew E Poynter

Abstract

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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Citations

May 29, 2019·Current Opinion in Lipidology·Preetha Shridas, Lisa R Tannock
Jun 2, 2020·Frontiers in Immunology·Sara Abouelasrar SalamaSofie Struyf
Nov 10, 2018·Scientific Reports·Jennifer L AtherMatthew E Poynter
Dec 15, 2020·Immunology·Sara Abouelasrar SalamaSofie Struyf
Nov 14, 2019·Cytokine & Growth Factor Reviews·Sara Abouelasrar SalamaSofie Struyf
Jan 16, 2021·Current Atherosclerosis Reports·Nancy R Webb
Dec 19, 2020·Scientific Reports·Mauricio CastellanoAna María Ferreira
Nov 19, 2020·Journal of Leukocyte Biology·Mitchell R WhiteKevan L Hartshorn

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