- 作者: Wei Gong, Yuan Li, Fan Chao, Gang Huang, Fengtian He
- 作者服務機構: Department of Biochemistry and Molecular Biology, College of Basic Medical Sciences, Third Military Medical University, Chongqing, China
- 中文摘要: --
- 英文摘要:
Background :
Antibacterial activity is a novel function of high-mobility group box 1 (HMGB1). However,
the functional site for this new effect is presently unknown.
Methods and Results :
In this study, recombinant human HMGB1 A box and B box (rHMGB1 A box, rHMGB1 B
box), recombinant human HMGB1 (rHMGB1) and the truncated C-terminal acidic tail
mutant (tHMGB1) were prepared by the prokaryotic expression system. The C-terminal
acidic tail (C peptide) was synthesized, which was composed of 30 amino acid residues.
Antibacterial assays showed that both the full length rHMGB1 and the synthetic C peptide
alone could efficiently inhibit bacteria proliferation, but rHMGB1 A box and B box, and
tHMGB1 lacking the C-terminal acidic tail had no antibacterial function. These results
suggest that C-terminal acidic tail is the key region for the antibacterial activity of HMGB1.
Furthermore, we prepared eleven different deleted mutants lacking several amino acid
residues in C-terminal acidic tail of HMGB1. Antibacterial assays of these mutants
demonstrate that the amino acid residues 201-205 in C-terminal acidic tail region is the core
functional site for the antibacterial activity of the molecule.
Conclusion :
In sum, these results define the key region and the crucial site in HMGB1 for its antibacterial
function, which is helpful to illustrating the antibacterial mechanisms of HMGB1. - 中文關鍵字: --
- 英文關鍵字: --