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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Main Authors: Huang Gang, Chao Fan, Li Yuan, Gong Wei, He Fengtian
Format: Article
Language:English
Published: BMC 2009-09-01
Series:Journal of Biomedical Science
Online Access:http://www.jbiomedsci.com/content/16/1/83
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spelling 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
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