ArticleJournal of biomedical science2009
Amino acid residues 201-205 in C-terminal acidic tail region plays a crucial role in antibacterial activity of HMGB1.
Article in Journal of biomedical science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- The redox-sensitive protein HMGB1: intracellular and extracellular roles.Experimental & molecular medicine · 2026Review
- Structure and Functions of HMGB3 Protein.International journal of molecular sciences · 2024Review
- High Mobility Group Box 1 Protein: A Plausible Therapeutic Molecular Target in Parkinson's Disease.Current pharmaceutical biotechnology · 2024Review
- Structure and Functions of HMGB2 Protein.International journal of molecular sciences · 2023Review
- Article
- The C-Terminal Acidic Tail Modulates the Anticancer Properties of HMGB1.International journal of molecular sciences · 2022Article
- The mechanism of HMGB1 secretion and release.Experimental & molecular medicine · 2022Review
- The SIRT1-HMGB1 axis: Therapeutic potential to ameliorate inflammatory responses and tumor occurrence.Frontiers in cell and developmental biology · 2022Review
- The extracellular innate-immune effector HMGB1 limits pathogenic bacterial biofilm proliferation.The Journal of clinical investigation · 2021Article
- Role of HMGB1 in Chemotherapy-Induced Peripheral Neuropathy.International journal of molecular sciences · 2020Review
- Functional Diversity of Non-Histone Chromosomal Protein HmgB1.International journal of molecular sciences · 2020Review
- Biological functions and theranostic potential of HMGB family members in human cancers.Therapeutic advances in medical oncology · 2020Review
- Immunological Significance of HMGB1 Post-Translational Modification and Redox Biology.Frontiers in immunology · 2020Review
- HMGB1 in health and disease.Molecular aspects of medicine · 2014Review
- Antimicrobial activity of high-mobility-group box 2: a new function to a well-known protein.Antimicrobial agents and chemotherapy · 2013Article
- The C-terminal acidic tail is responsible for the inhibitory effects of HMGB1 on efferocytosis.Journal of leukocyte biology · 2010Article
- Selection and Characterization of a DNA Aptamer Recognizing High Mobility Group Box 1 Protein (HMGB1) and Enhancing Its Pro-inflammatory Activity.Iranian journal of pharmaceutical research : IJPRArticle
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundAntibacterial 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
resultsIn 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.
conclusionIn 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.
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