If you are experiencing problems downloading PDF or HTML fulltext, our helpdesk recommend clearing your browser cache and trying again. If you need help in clearing your cache, please click here . Still need help? Email help@ingentaconnect.com

Modulation of exogenous antibiotic activity by host cathelicidin LL-37

$48.00 plus tax (Refund Policy)

Download / Buy Article:

Abstract:

Leszczyńska K, Namiot A, Janmey PA, Bucki R. Modulation of exogenous antibiotic activity by host cathelicidin LL-37. APMIS 2010; 118: 830–6.

The increasing number of infections caused by drug-resistant bacteria has spurred efforts to develop new therapeutic strategies. When applied locally, exogenous antibiotics work in an environment rich in endogenous antibacterial molecules such as the cathelicidin peptide LL-37, which has increased expression at infection sites because of the stimulatory effects of bacterial wall products on neutrophils and other cell types. To test for possible additive effects of exogenous and endogenous antibacterial agents, we evaluated the minimal inhibitory concentration (MIC) to assess the antibacterial activity of amoxicillin with clavulanic acid (AMC), tetracycline (T), erythromycin (E) and amikacin (AN) against different clinical isolates of Staphyloccocus aureus in combination with synthetic LL-37. These studies revealed that the antibacterial activity of AMC was strongly potentiated when added in combination with LL-37. However, in the presence of LL-37, we did not observe any decrease in the MIC values of T and E, particularly against methicillin-resistant S. aureus and macrolide-lincosamide-streptogramin B (MLSB) (+)/β-lactamase (+) strains, indicating a lack of synergistic action between these molecules. Interaction between exogenous antibiotics and host antibacterial molecules should be considered to provide optimal treatment, especially in cases of topical infections accompanied by increasing expression of host antibacterial molecules.

Keywords: Antibiotics; bacteria; cathelicidin LL-37; human

Document Type: Research Article

DOI: http://dx.doi.org/10.1111/j.1600-0463.2010.02667.x

Affiliations: 1: Departments of Diagnostic Microbiology 2: Anatomy, Medical University of Białystok, Białystok, Poland 3: Department of Physiology and the Institute for Medicine and Engineering, Vagelos Research Laboratories, University of Pennsylvania, Philadelphia, PA, USA

Publication date: November 1, 2010

Related content

Tools

Favourites

Share Content

Access Key

Free Content
Free content
New Content
New content
Open Access Content
Open access content
Subscribed Content
Subscribed content
Free Trial Content
Free trial content
Cookie Policy
X
Cookie Policy
ingentaconnect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more