Antiviral Activity of a Cyclic Pro-Pro-<i>β<sup>3</sup></i>-HoPhe-Phe Tetrapeptide against HSV-1 and HAdV-5
Ewa Zaczyńska,
Krzysztof Kaczmarek,
Janusz Zabrocki,
Jolanta Artym,
Michał Zimecki
Affiliations
Ewa Zaczyńska
Department of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Laboratory of Immunobiology, R. Weigla Str. 12, 53-114 Wrocław, Poland
Krzysztof Kaczmarek
Institute of Organic Chemistry, Lodz University of Technology, S. Żeromskiego Str. 116, 90-924 Łódź, Poland
Janusz Zabrocki
Institute of Organic Chemistry, Lodz University of Technology, S. Żeromskiego Str. 116, 90-924 Łódź, Poland
Jolanta Artym
Department of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Laboratory of Immunobiology, R. Weigla Str. 12, 53-114 Wrocław, Poland
Michał Zimecki
Department of Experimental Therapy, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Laboratory of Immunobiology, R. Weigla Str. 12, 53-114 Wrocław, Poland
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-β3-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 Herpes simplex 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.
