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Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides
BACKGROUND: The antibacterial activity of host defense peptides (HDP) is largely mediated by permeabilization of bacterial membranes. The lipid membrane of enveloped viruses might also be a target of antimicrobial peptides. Therefore, we screened a panel of naturally occurring HDPs representing diff...
Autores principales: | , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2005
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC548510/ https://www.ncbi.nlm.nih.gov/pubmed/15656908 http://dx.doi.org/10.1186/1742-4690-2-2 |
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author | Steinstraesser, Lars Tippler, Bettina Mertens, Janine Lamme, Evert Homann, Heinz-Herbert Lehnhardt, Marcus Wildner, Oliver Steinau, Hans-Ulrich Überla, Klaus |
author_facet | Steinstraesser, Lars Tippler, Bettina Mertens, Janine Lamme, Evert Homann, Heinz-Herbert Lehnhardt, Marcus Wildner, Oliver Steinau, Hans-Ulrich Überla, Klaus |
author_sort | Steinstraesser, Lars |
collection | PubMed |
description | BACKGROUND: The antibacterial activity of host defense peptides (HDP) is largely mediated by permeabilization of bacterial membranes. The lipid membrane of enveloped viruses might also be a target of antimicrobial peptides. Therefore, we screened a panel of naturally occurring HDPs representing different classes for inhibition of early, Env-independent steps in the HIV replication cycle. A lentiviral vector-based screening assay was used to determine the inhibitory effect of HDPs on early steps in the replication cycle and on cell metabolism. RESULTS: Human LL37 and porcine Protegrin-1 specifically reduced lentiviral vector infectivity, whereas the reduction of luciferase activities observed at high concentrations of the other HDPs is primarily due to modulation of cellular activity and/ or cytotoxicity rather than antiviral activity. A retroviral vector was inhibited by LL37 and Protegrin-1 to similar extent, while no specific inhibition of adenoviral vector mediated gene transfer was observed. Specific inhibitory effects of Protegrin-1 were confirmed for wild type HIV-1. CONCLUSION: Although Protegrin-1 apparently inhibits an early step in the HIV-replication cycle, cytotoxic effects might limit its use as an antiviral agent unless the specificity for the virus can be improved. |
format | Text |
id | pubmed-548510 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2005 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-5485102005-02-11 Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides Steinstraesser, Lars Tippler, Bettina Mertens, Janine Lamme, Evert Homann, Heinz-Herbert Lehnhardt, Marcus Wildner, Oliver Steinau, Hans-Ulrich Überla, Klaus Retrovirology Research BACKGROUND: The antibacterial activity of host defense peptides (HDP) is largely mediated by permeabilization of bacterial membranes. The lipid membrane of enveloped viruses might also be a target of antimicrobial peptides. Therefore, we screened a panel of naturally occurring HDPs representing different classes for inhibition of early, Env-independent steps in the HIV replication cycle. A lentiviral vector-based screening assay was used to determine the inhibitory effect of HDPs on early steps in the replication cycle and on cell metabolism. RESULTS: Human LL37 and porcine Protegrin-1 specifically reduced lentiviral vector infectivity, whereas the reduction of luciferase activities observed at high concentrations of the other HDPs is primarily due to modulation of cellular activity and/ or cytotoxicity rather than antiviral activity. A retroviral vector was inhibited by LL37 and Protegrin-1 to similar extent, while no specific inhibition of adenoviral vector mediated gene transfer was observed. Specific inhibitory effects of Protegrin-1 were confirmed for wild type HIV-1. CONCLUSION: Although Protegrin-1 apparently inhibits an early step in the HIV-replication cycle, cytotoxic effects might limit its use as an antiviral agent unless the specificity for the virus can be improved. BioMed Central 2005-01-18 /pmc/articles/PMC548510/ /pubmed/15656908 http://dx.doi.org/10.1186/1742-4690-2-2 Text en Copyright © 2005 Steinstraesser et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Steinstraesser, Lars Tippler, Bettina Mertens, Janine Lamme, Evert Homann, Heinz-Herbert Lehnhardt, Marcus Wildner, Oliver Steinau, Hans-Ulrich Überla, Klaus Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
title | Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
title_full | Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
title_fullStr | Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
title_full_unstemmed | Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
title_short | Inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
title_sort | inhibition of early steps in the lentiviral replication cycle by cathelicidin host defense peptides |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC548510/ https://www.ncbi.nlm.nih.gov/pubmed/15656908 http://dx.doi.org/10.1186/1742-4690-2-2 |
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