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...

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Main Authors: Ewa Zaczyńska, Krzysztof Kaczmarek, Janusz Zabrocki, Jolanta Artym, Michał Zimecki
Format: Article
Language:English
Published: MDPI AG 2022-05-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/27/11/3552
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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.
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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
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