Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5
The core of Cyclolinopeptide A (CLA, cyclo(LIILVPPFF)), responsible for its high immunosuppressive activity, contains a Pro-Pro-Phe-Phe sequence. A newly synthesized cyclic tetrapeptide, cyclo(Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe) (denoted as 4B8M) bearing the active sequen...
Main Authors: | , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2022-05-01
|
Series: | Molecules |
Subjects: | |
Online Access: | https://www.mdpi.com/1420-3049/27/11/3552 |
_version_ | 1797492407058563072 |
---|---|
author | Ewa Zaczyńska Krzysztof Kaczmarek Janusz Zabrocki Jolanta Artym Michał Zimecki |
author_facet | Ewa Zaczyńska Krzysztof Kaczmarek Janusz Zabrocki Jolanta Artym Michał Zimecki |
author_sort | Ewa Zaczyńska |
collection | DOAJ |
description | The core of Cyclolinopeptide A (CLA, cyclo(LIILVPPFF)), responsible for its high immunosuppressive activity, contains a Pro-Pro-Phe-Phe sequence. A newly synthesized cyclic tetrapeptide, cyclo(Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe) (denoted as 4B8M) bearing the active sequence of CLA, was recently shown to exhibit a wide array of anti-inflammatory properties in mouse models. In this investigation, we demonstrate that the peptide significantly inhibits the replication of human adenovirus C serotype 5 (HAdV-5) and <i>Herpes simplex</i> virus type-1 (HSV-1) in epithelial lung cell line A-549, applying Cidofovir and Acyclovir as reference drugs. Based on a previously established mechanism of its action, we propose that the peptide may inhibit virus replication by the induction of PGE2 acting via EP2/EP4 receptors in epithelial cells. In summary, we reveal a new, antiviral property of this anti-inflammatory peptide. |
first_indexed | 2024-03-10T01:03:20Z |
format | Article |
id | doaj.art-203bdc5400f64daea9a1c3fe29da60b7 |
institution | Directory Open Access Journal |
issn | 1420-3049 |
language | English |
last_indexed | 2024-03-10T01:03:20Z |
publishDate | 2022-05-01 |
publisher | MDPI AG |
record_format | Article |
series | Molecules |
spelling | doaj.art-203bdc5400f64daea9a1c3fe29da60b72023-11-23T14:30:36ZengMDPI AGMolecules1420-30492022-05-012711355210.3390/molecules27113552Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5Ewa Zaczyńska0Krzysztof Kaczmarek1Janusz Zabrocki2Jolanta Artym3Michał Zimecki4Department of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Laboratory of Immunobiology, R. Weigla Str. 12, 53-114 Wrocław, PolandInstitute of Organic Chemistry, Lodz University of Technology, S. Żeromskiego Str. 116, 90-924 Łódź, PolandInstitute of Organic Chemistry, Lodz University of Technology, S. Żeromskiego Str. 116, 90-924 Łódź, PolandDepartment of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Laboratory of Immunobiology, R. Weigla Str. 12, 53-114 Wrocław, PolandDepartment of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Laboratory of Immunobiology, R. Weigla Str. 12, 53-114 Wrocław, PolandThe core of Cyclolinopeptide A (CLA, cyclo(LIILVPPFF)), responsible for its high immunosuppressive activity, contains a Pro-Pro-Phe-Phe sequence. A newly synthesized cyclic tetrapeptide, cyclo(Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe) (denoted as 4B8M) bearing the active sequence of CLA, was recently shown to exhibit a wide array of anti-inflammatory properties in mouse models. In this investigation, we demonstrate that the peptide significantly inhibits the replication of human adenovirus C serotype 5 (HAdV-5) and <i>Herpes simplex</i> virus type-1 (HSV-1) in epithelial lung cell line A-549, applying Cidofovir and Acyclovir as reference drugs. Based on a previously established mechanism of its action, we propose that the peptide may inhibit virus replication by the induction of PGE2 acting via EP2/EP4 receptors in epithelial cells. In summary, we reveal a new, antiviral property of this anti-inflammatory peptide.https://www.mdpi.com/1420-3049/27/11/3552cyclic tetrapeptide cyclo(Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe)A-549HAdV-5HSV-1antiviral activity |
spellingShingle | Ewa Zaczyńska Krzysztof Kaczmarek Janusz Zabrocki Jolanta Artym Michał Zimecki Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5 Molecules cyclic tetrapeptide cyclo(Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe) A-549 HAdV-5 HSV-1 antiviral activity |
title | Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5 |
title_full | Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5 |
title_fullStr | Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5 |
title_full_unstemmed | Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5 |
title_short | Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5 |
title_sort | antiviral activity of a cyclic pro pro i β sup 3 sup i hophe phe tetrapeptide against hsv 1 and hadv 5 |
topic | cyclic tetrapeptide cyclo(Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe) A-549 HAdV-5 HSV-1 antiviral activity |
url | https://www.mdpi.com/1420-3049/27/11/3552 |
work_keys_str_mv | AT ewazaczynska antiviralactivityofacyclicproproibsup3supihophephetetrapeptideagainsthsv1andhadv5 AT krzysztofkaczmarek antiviralactivityofacyclicproproibsup3supihophephetetrapeptideagainsthsv1andhadv5 AT januszzabrocki antiviralactivityofacyclicproproibsup3supihophephetetrapeptideagainsthsv1andhadv5 AT jolantaartym antiviralactivityofacyclicproproibsup3supihophephetetrapeptideagainsthsv1andhadv5 AT michałzimecki antiviralactivityofacyclicproproibsup3supihophephetetrapeptideagainsthsv1andhadv5 |