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

被引：24

作者：

Burgess, Edward J. ^{[1
,2
,3
]}

Hoyt, Laura R. ^{[1
,3
]}

Randall, Matthew J. ^{[1
,3
]}

Mank, Madeleine M. ^{[1
,3
]}

Bivona, Joseph J., III ^{[1
,2
,3
]}

Eisenhauer, Philip L. ^{[4
]}

Botten, Jason W. ^{[1
,2
,4
,5
]}

Ballif, Bryan A. ^{[6
]}

Lam, Ying-Wai ^{[6
]}

Wargo, Matthew J. ^{[1
,2
,5
]}

Boyson, Jonathan E. ^{[1
,2
,7
]}

Ather, Jennifer L. ^{[1
,3
]}

Poynter, Matthew E. ^{[1
,2
,3
]}

机构：

[1] Univ Vermont, Vermont Lung Ctr, Burlington, VT 05405 USA

[2] Univ Vermont, Cellular Mol & Biomed Sci Program, Burlington, VT 05405 USA

[3] Univ Vermont, Dept Med, Div Pulm Dis & Crit Care, Burlington, VT 05405 USA

[4] Univ Vermont, Dept Med, Immunobiol Div, Burlington, VT 05405 USA

[5] Univ Vermont, Dept Microbiol & Mol Genet, Burlington, VT 05405 USA

[6] Univ Vermont, Dept Biol, Burlington, VT 05405 USA

[7] Univ Vermont, Dept Surg, Burlington, VT 05405 USA

来源：

JOURNAL OF IMMUNOLOGY | 2018年 / 201卷 / 08期

基金：

美国国家卫生研究院;

关键词：

MEMBRANE PROTEIN-A; HEPATITIS-C VIRUS; ALLERGIC SENSITIZATION; NLRP3; INFLAMMASOME; CUTTING EDGE; RECEPTOR; EXPRESSION; SAA; ACTIVATION; CELLS;

D O I：

10.4049/jimmunol.1800503

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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-alpha 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.

引用

页码：2377 / 2384

页数：8

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