1 In vivo cluster formation of nisin and Lipid II is correlated with membrane

نویسندگان

  • Menno B. Tol
  • Danae Morales Angeles
  • Dirk-Jan Scheffers
چکیده

In vivo cluster formation of nisin and Lipid II is correlated with membrane 1 depolarization 2 3 Menno B. Tol, Danae Morales Angeles, Dirk-Jan Scheffers 4 5 Department of Molecular Microbiology, Groningen Biomolecular Sciences and 6 Biotechnology Institute, University of Groningen, The Netherlands 7 8 Running Title: Nisin-Lipid II clusters and membrane depolarization 9 10 #Address correspondence to Dirk-Jan Scheffers, [email protected] 11 a M.B.T. and D.M.A. contributed equally to this work. 12 13 keywords: lantibiotics, mechanism-of-action, antimicrobial peptide, Gram-positive 14 bacteria, Bacillus subtilis, peptidoglycan synthesis. 15 AAC Accepted Manuscript Posted Online 13 April 2015 Antimicrob. Agents Chemother. doi:10.1128/AAC.04781-14 Copyright © 2015, American Society for Microbiology. All Rights Reserved.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity.

Unlike numerous pore-forming amphiphilic peptide antibiotics, the lantibiotic nisin is active in nanomolar concentrations, which results from its ability to use the lipid-bound cell wall precursor lipid II as a docking molecule for subsequent pore formation. Here we use genetically engineered nisin variants to identify the structural requirements for the interaction of the peptide with lipid II...

متن کامل

The lantibiotic nisin induces lipid II aggregation, causing membrane instability and vesicle budding.

The antimicrobial peptide nisin exerts its activity by a unique dual mechanism. It permeates the cell membranes of Gram-positive bacteria by binding to the cell wall precursor Lipid II and inhibits cell wall synthesis. Binding of nisin to Lipid II induces the formation of large nisin-Lipid II aggregates in the membrane of bacteria as well as in Lipid II-doped model membranes. Mechanistic detail...

متن کامل

Lipid II-mediated pore formation by the peptide antibiotic nisin: a black lipid membrane study.

The antibiotic peptide nisin is the first known lantibiotic that uses a docking molecule within the bacterial cytoplasmic membrane for pore formation. Through specific interaction with the cell wall precursor lipid II, nisin forms defined pores which are stable for seconds and have pore diameters of 2 to 2.5 nm.

متن کامل

Mechanism of Inhibition of Bacillus anthracis Spore Outgrowth by the Lantibiotic Nisin

The lantibiotic nisin inhibits growth of vegetative Gram-positive bacteria by binding to lipid II, which disrupts cell wall biosynthesis and facilitates pore formation. Nisin also inhibits the outgrowth of bacterial spores, including spores of Bacillus anthracis, whose structural and biochemical properties are fundamentally different from those of vegetative bacteria. The molecular basis of nis...

متن کامل

Lantibiotic Immunity: Inhibition of Nisin Mediated Pore Formation by NisI

Nisin, a 3.4 kDa antimicrobial peptide produced by some Lactococcus lactis strains is the most prominent member of the lantibiotic family. Nisin can inhibit cell growth and penetrates the target Gram-positive bacterial membrane by binding to Lipid II, an essential cell wall synthesis precursor. The assembled nisin-Lipid II complex forms pores in the target membrane. To gain immunity against its...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2015