کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10800984 | 1054720 | 2005 | 13 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Processing of lysozyme at distinct loops by pepsin: A novel action for generating multiple antimicrobial peptide motifs in the newborn stomach
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کلمات کلیدی
MuramidaseN-phenyl-1-naphthylamineNPNCFDACLZDCFH-DA2′,7′-dichlorodihydrofluorescein diacetate - 2 '، 7'-dichlorodihydrofluorescein diacetateMembrane damage - آسیب غشاءSodium dodecylsulfate-polyacrylamide gel electrophoresis - الکتروفورز ژل سدیم دودسیل سولفات - پلی آکریل آمیدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدHuman breast milk - شیر مادر انسانیOuter membrane - غشای خارجیCytoplasmic membrane - غشای سیتوپلاسمیAntimicrobial activity - فعالیت ضدمیکروبیlysozyme - لیزوزیم MALDI-TOF-MS - مالدی TOF-MSGastrointestinal mucosa - مخاطی دستگاه گوارشpeptide motif - موتیف پپتیدProteolysis - پروتئولیزPepsin - پپسین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Processing of lysozyme at distinct loops by pepsin: A novel action for generating multiple antimicrobial peptide motifs in the newborn stomach Processing of lysozyme at distinct loops by pepsin: A novel action for generating multiple antimicrobial peptide motifs in the newborn stomach](/preview/png/10800984.png)
چکیده انگلیسی
C-type lysozyme (cLZ) is an antimicrobial enzyme that plays a major defense role in many human secretions. Recently, we have identified a helix-loop-helix antimicrobial peptide fragment of cLZ. This finding suggests that processing by coexisting proteases might be a relevant physiological process for generating peptides that contribute to the in vivo mucosal defense role of cLZ. In this study, we found that pepsin, under condition relevant to the newborn stomach (pH 4.0), generated various peptides from cLZ with potent bactericidal activity against several strains of Gram-negative and Gram-positive bacteria. Microsequencing and mass spectral analysis revealed that pepsin cleavage occurred at conserved loops within the α-domain of cLZ. We found that the bactericidal domain, which was isolated by gel filtration and reversed-phase HPLC, contains two cationic α-helical peptides generated from a helix-loop-helix domain (residues 1-38 of cLZ) by nicking at leucine17. A third peptide consisting of an α-helix (residues 18-38) and a two-stranded β-sheet (residues 39-56) structure was also identified. These peptides share structural motifs commonly found in different innate immune defenses. Functional cellular studies with outer membrane-, cytoplasmic membrane vitality- and redox-specific fluorescence dyes revealed that the lethal effect of the isolated antimicrobial peptides is due to membrane permeabilization and inhibition of redox-driven bacterial respiration. The results provide the first demonstration that pepsin can fine-tune the antimicrobial potency of cLZ by generating multiple antimicrobial peptide motifs, delineating a new molecular switch of cLZ in the mucosal defense systems. Finally, this finding offers a new strategy for the design of antibiotic peptide drugs with potential use in the treatment of infectious diseases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1726, Issue 1, 30 October 2005, Pages 102-114
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1726, Issue 1, 30 October 2005, Pages 102-114
نویسندگان
Hisham R. Ibrahim, Daisuke Inazaki, Adham Abdou, Takayoshi Aoki, Mujo Kim,