Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 295, Issue 9, Pages 2570-2581Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.RA119.010626
Keywords
antimicrobial peptide (AMP); lipid-binding protein; Staphylococcus aureus (S; aureus); host defense; phospholipid vesicle; acute-phase proteins; bactericidal mechanism; cutaneous infection; serum amyloid A
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Funding
- National Science and Technology Major Project [2013ZX10004608]
- National Key Research and Development Grant [2018YFC1004702]
- National Natural Science Foundation of China [NSFC31970802, NSFC31071316, NSFC81261130024]
- Natural Science Foundation of Beijing Grant [20G10613]
- State Key Laboratory of Agrobiotechnology, China Agricultural University [2018SKLAB6-18]
- project for Extramural Scientists of State Key Laboratory of Agrobiotechnology Grant [2015SKLAB6-2]
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Serum amyloid A (SAA), one of the major highly conserved acute-phase proteins in most mammals, is predominantly produced by hepatocytes and also by a variety of cells in extrahepatic tissues. It is well-known that the expression of SAA is sharply increased in bacterial infections. However, the exact physiological function of SAA during bacterial infection remains unclear. Herein, we showed that SAA expression significantly increased in abscesses of Staphylococcus aureus cutaneous infected mice, which exert direct antibacterial effects by binding to the bacterial cell surface and disrupting the cell membrane in acidic conditions. Mechanically, SAA disrupts anionic liposomes by spontaneously forming small vesicles or micelles under acidic conditions. Especially, the N-terminal region of SAA is necessary for membrane disruption and bactericidal activity. Furthermore, we found that mice deficient in SAA1/2 were more susceptible to infection by S. aureus. In addition, the expression of SAA in infected skin was regulated by interleukin-6. Taken together, these findings support a key role of the SAA in host defense and may provide a novel therapeutic strategy for cutaneous bacterial infection.
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