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- Title
α-Helical domain is essential for antimicrobial activity of high mobility group nucleosomal binding domain 2 (HMGN2).
- Authors
Yun Feng; Ning Huang; Qi Wu; Lang Bao; Ba-yao Wang
- Abstract
To examine the antimicrobial spectrum and functional structure of high mobility group nucleosomal binding domain 2(HMGN2). OMIGA protein structure software was used to analyze the two-dimensional structure of HMGN2. Synthetic short peptides were generated for studying the relationship between function and structure. Prokaryotic expression vectors were constructed for the holo-HMGN2 and its helical domain. Their E coli-based products were also prepared for antimicrobial testing. The antimicrobial assay included minimal effective concentration, minimal inhibitory concentration, and minimal bactericidal concentration. OMIGA protein structure software analysis revealed a transmembrane α-helical structure (the putative antimicrobial domain) located from position 18 to 48 of the HMGN2 protein sequence. The antimicrobial assay showed that the MIC of the recombinant holo-HMGN2 against E coli ML-35p (an ampicillin-resistance strain), Pseudomonas aeruginosa ATCC 27853 and Candida albicans ATCC 10231 were 12.5, 25, and 100 mg/L, respectively. Against the same microorganisms, the MIC of the synthetic HMGN2 α-helical domain were 12.5, 25, and 100 mg/L, respectively, that is, the same as with the recombinant form of HMGN2. In contrast, recombinant holo-HMGN2 was inactive against Staphylococcus aureus ATCC 25923. The synthetic N-terminal and C-terminal fragments of HMGN2 had no antimicrobial activity against E coli ML-35p, P aeruginosa ATCC 27853 or C albicans ATCC 10231. HMGN2 showed potent antimicrobial activity against E coli ML-35p, P aeruginosa ATCC 27853 and, to some extent, against C albicans ATCC 10231, but was inactive against S aureus ATCC 25923 in these assay systems. Its α-helical structure may be essential for the antimicrobial activity of HMGN2.
- Subjects
ANTI-infective agents; DRUGS; PROTEINS; COMPUTER software; PEPTIDES
- Publication
Acta Pharmacologica Sinica, 2005, Vol 26, Issue 9, p1087
- ISSN
1671-4083
- Publication type
Article
- DOI
10.1111/j.1745-7254.2005.00132.x