Staphylococcus aureus Mutant Screen Reveals Interaction of the Human Antimicrobial Peptide Dermcidin with Membrane Phospholipids

نویسندگان
چکیده

برای دانلود باید عضویت طلایی داشته باشید

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

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Staphylococcus aureus mutant screen reveals interaction of the human antimicrobial peptide dermcidin with membrane phospholipids.

Antimicrobial peptides (AMPs) form an important part of the innate host defense. In contrast to most AMPs, human dermcidin has an anionic net charge. To investigate whether bacteria have developed specific mechanisms of resistance to dermcidin, we screened for mutants of the leading human pathogen, Staphylococcus aureus, with altered resistance to dermcidin. To that end, we constructed a plasmi...

متن کامل

Dermcidin-α: Green Variant of Dermcidin, Human Antimicrobial Peptide in Sweat†

10.1021/bi0160516 CCC: $22.00 © 2002 American Chemical Society Published on Web 04/01/2002 ABSTRACT: Dermcidin (DCD), an recently discovered antimicrobial peptide, plays a role in the innate response by regulating human skin flora in sweat. Here we describe the isolation of the gene of a variant of dermcidin, designated as DCD-α. This variant has 75% homology to dermcidin and has been found in ...

متن کامل

Interactions of an anionic antimicrobial peptide with Staphylococcus aureus membranes.

The antimicrobial activity of the anionic peptide, AP1 (GEQGALAQFGEWL), was investigated. AP1 was found to kill Staphylococcus aureus with an MLC of 3mM and to induce maximal surface pressure changes of 3.8 mN m(-1) over 1200s in monolayers formed from lipid extract of S. aureus membranes. FTIR spectroscopy showed the peptide to be alpha-helical (100%) in the presence of vesicles formed from th...

متن کامل

Functional interrelationships between cell membrane and cell wall in antimicrobial peptide-mediated killing of Staphylococcus aureus.

Perturbation of the Staphylococcus aureus cytoplasmic membrane (CM) is felt to play a key role in the microbicidal mechanism of many antimicrobial peptides (APs). However, it is not established whether membrane permeabilization (MP) alone is sufficient to kill susceptible staphylococci or if the cell wall (CW) and/or intracellular targets contribute to AP-induced lethality. We hypothesized that...

متن کامل

Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases.

Cathelicidin LL-37 is one of the few human bactericidal peptides with potent antistaphylococcal activity. In this study we examined the susceptibility of LL-37 to proteolytic degradation by two major proteinases produced by Staphylococcus aureus, a metalloproteinase (aureolysin) and a glutamylendopeptidase (V8 protease). We found that aureolysin cleaved and inactivated LL-37 in a time- and conc...

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

ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 2009

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.00428-09