Unknown

Dataset Information

0

Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1.


ABSTRACT: 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.

SUBMITTER: Gong W 

PROVIDER: S-EPMC2754419 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

altmetric image

Publications

Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1.

Gong Wei W   Li Yuan Y   Chao Fan F   Huang Gang G   He Fengtian F  

Journal of biomedical science 20090914


<h4>Background</h4>Antibacterial activity is a novel function of high-mobility group box 1 (HMGB1). However, the functional site for this new effect is presently unknown.<h4>Methods and results</h4>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  ...[more]

Similar Datasets

| S-EPMC9319070 | biostudies-literature
| S-EPMC5642108 | biostudies-literature
| S-EPMC8327309 | biostudies-literature
| S-EPMC5838153 | biostudies-literature
| S-EPMC7261955 | biostudies-literature
| S-EPMC2600807 | biostudies-literature
| S-EPMC4007426 | biostudies-literature
| S-EPMC6016865 | biostudies-literature
| S-EPMC8954191 | biostudies-literature
| S-EPMC4090703 | biostudies-literature