Perspective of Use of Antiviral Peptides against Influenza Virus
Abstract
:1. Introduction
2. Design and Characteristics of Antiviral Peptides
Influenza Virus Replication Cycle
3. Mode of Action of Various Antimicrobial Peptides with Antiviral Activity
3.1. The Peptides Inhibiting Virus Attachment and Virus-Cell Membrane Fusion
The Peptides Inhibiting Virus Attachment and Virus-Cell Membrane Fusion | |||||||
Peptide | Influenza Serotype | Sequence | Conformation | Net Charge * | Hydrophobic Residue * | IC50 | Reference |
EB peptide | Broad spectrum | RRKKAAVALLPAVLLALLAP | linear | 4 | 70 | 3 to 20 µM | [37] |
Derived EB peptide | Broad spectrum | RRKKLAVLLALLA | linear | 4 | 69 | 3.5 µM | [38] |
P1 | H9N2 | NDFRSKT | linear | 1 | 14 | 48 µM | [39] |
P1 cyclic | H9N3 | CNDFRSKTC | cyclic | 1 | 33 | 71 µM | [39] |
FluPep 1 | H1N1 | WLVFFVIFYFFR | α-helix | 1 | 83 | 0.093 µM | [40] |
FluPep 2 | H1N1 | WLVFFVIAYFAR | α-helix | 1 | 83 | 0.0009 µM | [40] |
FluPep 3 | H1N1 | WLVFFVIFYFFRRRKK | α-helix | 5 | 62 | 0.00003 µM | [40] |
FluPep 4 | H1N1 | RRKKWLVFFVIFYFFR | α-helix | 5 | 62 | 0.00004 µM | [40] |
FluPep 7 | H1N1 | RRKKIFYFFR | α-helix | 5 | 40 | 0.15 µM | [40] |
FluPep 8 | H1N1 | WLVFFVRRKK | α-helix | 4 | 60 | 0.63 µM | [40] |
FluPep 9 | H1N1 | FFVIFYRRKK | α-helix | 4 | 50 | 1.48 µM | [40] |
C18-s2 | H1N1, H3N2 | C17H35CO-ARLPRTMVHPKPAQP-NH2 | - | 3 | 33 | 11–15 µM | [41] |
Pal L1 | H5N1 | C16-ARLPRTMVHPKPAQP | micelle | 3 | 33 | - | [42] |
Pal M1 | H5N1 | C16-ARLPRTMV | micelle | 2 | 50 | - | [42] |
Pal S1 | H5N1 | C16-ARLPR | micelle | 2 | 40 | - | [42] |
Flufirvitide | Broad spectrum | - | - | - | - | - | [43] |
PEP 19-2.5 | H7N7, H3N2, H1N1 | GCKKYRRFRWKFKGKFWFWG | α-helix | 8 | 40 | - | [44] |
PEP 19-4 | H7N7, H3N2, H1N1 | GKKYRRFRWKFKGKWFWFG | α-helix | 8 | 36 | - | [44] |
PEP 19-8D | H7N7, H3N2, H1N1 | GFWFKGKWRFKKYRGGRYKKFRWKGKFWFG | α-helix | 12 | 33 | - | [44] |
PEP 19-CP | H7N7, H3N2, H1N1 | SSNKSTTGSGETTTA | α-helix | 0 | 6 | - | [44] |
Defensins | H1N1, H3N2 | ACYCRIPACIAGERRYGTCIYQGRLWAFCC | β-sheet | 3 | 53 | - | [45] |
The Peptides Disrupting Viral Envelope | |||||||
Peptide | Influenza Serotype | Sequence | Conformation | Net Charge * | Hydrophobic Residue * | IC50 | Reference |
LF C-lobe peptide 1 | H1H1, H3N2 | SKHSSLDCVLRP | α-helix | 1 | 33 | 4–6 pM | [46] |
LF C-lobe peptide 2 | H1H1, H3N2 | AGDDQGLDKCVPNSKEK | α-helix | −1 | 23 | 4–7 pM | [46] |
LF C-lobe peptide 3 | H1H1, H3N2 | NGESSADWAKN | α-helix | −1 | 27 | 22–225 pM | [46] |
Mucroporin-M1 | H5N1, H1N1 | LFRLIKSLIKRLVSAFK | α-helix | 5 | 58 | 1.03 μM | [47] |
LL-37 | H1N1, H3N2 | LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES | α-helix | 6 | 35 | - | [48] |
The Peptides Inhibiting Viral Replication | |||||||
Peptide | Influenza Serotype | Sequence | Conformation | Net Charge* | Hydrophobic Residue* | IC50 | Reference |
PB11-25 | Broad spectrum | MDVNPTLLFLKVPAQNAISTTFPYT | α-helix | 0 | 44 | - | [49] |
PB21-37 | H1N1, H5N1 | MERIKELRDLMSWSRTREILTKTTVDHMAIIKKYTSG | α-helix | 3 | 35 | 375 nM | [50] |
PB1731–757 | H5N1 | ESGRIKKEEFAEIMKICSTIEELGRQK | α-helix | 0 | 33 | - | [51] |
PB11–25AT6Y | H1N1, H5N1 | MDVNPYLLFLKVPAQ | α-helix | 0 | 53 | 22–107 nM | [52] |
Killer peptide | H7N1 | AKVTMTCSAS | α-helix | 1 | 50 | 2.6 µM | [53] |
HNP-1 | H3N2 | CYCRIPACIAGERRYGTCIYQGRLWAFCC | β-sheet | 3 | 51 | - | [54] |
Peptid 6 | H1N1, H3N2 | CATCEQIADSQHRSHRQMV | Zn-finger | 0 | 36 | 0.7 nM | [55,56] |
3.2. The Peptides Disrupting Viral Envelope
3.3. The Peptides Inhibiting Viral Replication
3.4. Other Possible Mechanisms of Influenza Virus Inhibition
4. Conclusions
Acknowledgments
Author Contributions
Conflicts of Interest
References
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Skalickova, S.; Heger, Z.; Krejcova, L.; Pekarik, V.; Bastl, K.; Janda, J.; Kostolansky, F.; Vareckova, E.; Zitka, O.; Adam, V.; et al. Perspective of Use of Antiviral Peptides against Influenza Virus. Viruses 2015, 7, 5428-5442. https://doi.org/10.3390/v7102883
Skalickova S, Heger Z, Krejcova L, Pekarik V, Bastl K, Janda J, Kostolansky F, Vareckova E, Zitka O, Adam V, et al. Perspective of Use of Antiviral Peptides against Influenza Virus. Viruses. 2015; 7(10):5428-5442. https://doi.org/10.3390/v7102883
Chicago/Turabian StyleSkalickova, Sylvie, Zbynek Heger, Ludmila Krejcova, Vladimir Pekarik, Karel Bastl, Jozef Janda, Frantisek Kostolansky, Eva Vareckova, Ondrej Zitka, Vojtech Adam, and et al. 2015. "Perspective of Use of Antiviral Peptides against Influenza Virus" Viruses 7, no. 10: 5428-5442. https://doi.org/10.3390/v7102883