Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1
<p>Abstract</p> <p>Background</p> <p>Antibacterial activity is a novel function of high-mobility group box 1 (HMGB1). However, the functional site for this new effect is presently unknown.</p> <p>Methods and Results</p> <p>In this study, recombin...
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doaj-a5e955d3c13448c8b4548c4f3af751f62020-11-24T22:57:24ZengBMCJournal of Biomedical Science1021-77701423-01272009-09-011618310.1186/1423-0127-16-83Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1Huang GangChao FanLi YuanGong WeiHe Fengtian<p>Abstract</p> <p>Background</p> <p>Antibacterial activity is a novel function of high-mobility group box 1 (HMGB1). However, the functional site for this new effect is presently unknown.</p> <p>Methods and Results</p> <p>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.</p> <p>Conclusion</p> <p>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.</p> http://www.jbiomedsci.com/content/16/1/83 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Huang Gang Chao Fan Li Yuan Gong Wei He Fengtian |
spellingShingle |
Huang Gang Chao Fan Li Yuan Gong Wei He Fengtian Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1 Journal of Biomedical Science |
author_facet |
Huang Gang Chao Fan Li Yuan Gong Wei He Fengtian |
author_sort |
Huang Gang |
title |
Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1 |
title_short |
Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1 |
title_full |
Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1 |
title_fullStr |
Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1 |
title_full_unstemmed |
Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1 |
title_sort |
amino acid residues 201-205 in c-terminal acidic tail region plays a crucial role in antibacterial activity of hmgb1 |
publisher |
BMC |
series |
Journal of Biomedical Science |
issn |
1021-7770 1423-0127 |
publishDate |
2009-09-01 |
description |
<p>Abstract</p> <p>Background</p> <p>Antibacterial activity is a novel function of high-mobility group box 1 (HMGB1). However, the functional site for this new effect is presently unknown.</p> <p>Methods and Results</p> <p>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.</p> <p>Conclusion</p> <p>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.</p> |
url |
http://www.jbiomedsci.com/content/16/1/83 |
work_keys_str_mv |
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