Herpes Simplex Virus: Treatment with Antimicrobial Peptides

Ковальчук, Л. В.; Gankovskaya, L.V.; Gankovskaya, O. .A.; Лавров, В. Ф.

doi:10.1007/978-0-387-72005-0_39

Cited by 16 publications

(13 citation statements)

References 29 publications

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“…Recently, our group found that Mucroporin-M1 inhibited RNA viruses, including measles, SARS-CoV and influenza H5N1 viruses (16). Additionally, it has been reported that similar peptides inhibit other RNA viruses (14,17,31). These antiviral compounds were thought to function by disturbing the viral membrane.…”

Section: Discussionmentioning

confidence: 99%

Mucroporin-M1 Inhibits Hepatitis B Virus Replication by Activating the Mitogen-activated Protein Kinase (MAPK) Pathway and Down-regulating HNF4α in Vitro and in Vivo

Zhao

Hong

Zeng

et al. 2012

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Mucroporin-M1 Inhibits Hepatitis B Virus Replication by Activating the Mitogen-activated Protein Kinase (MAPK) Pathway and Down-regulating HNF4α in Vitro and in Vivo

Zhao

Hong

Zeng

et al. 2012

Journal of Biological Chemistry

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“…In addition to their direct microbicidal activities, these host defense peptides are particularly attractive because of the multiple activities that are associated with many members of this family. These include the regulation of the innate and adaptive immune systems, inflammation and wound healing [1], [2], and additional anti-infective activities such as being antifungal, antiviral, antiparasitic or anticancerous [5]–[8].…”

Section: Introductionmentioning

confidence: 99%

Serum Stabilities of Short Tryptophan- and Arginine-Rich Antimicrobial Peptide Analogs

et al. 2010

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BackgroundSeveral short antimicrobial peptides that are rich in tryptophan and arginine residues were designed with a series of simple modifications such as end capping and cyclization. The two sets of hexapeptides are based on the Trp- and Arg-rich primary sequences from the “antimicrobial centre” of bovine lactoferricin as well as an antimicrobial sequence obtained through the screening of a hexapeptide combinatorial library.Methodology/Principal FindingsHPLC, mass spectrometry and antimicrobial assays were carried out to explore the consequences of the modifications on the serum stability and microbicidal activity of the peptides. The results show that C-terminal amidation increases the antimicrobial activity but that it makes little difference to its proteolytic degradation in human serum. On the other hand, N-terminal acetylation decreases the peptide activities but significantly increases their protease resistance. Peptide cyclization of the hexameric peptides was found to be highly effective for both serum stability and antimicrobial activity. However the two cyclization strategies employed have different effects, with disulfide cyclization resulting in more active peptides while backbone cyclization results in more proteolytically stable peptides. However, the benefit of backbone cyclization did not extend to longer 11-mer peptides derived from the same region of lactoferricin. Mass spectrometry data support the serum stability assay results and allowed us to determine preferred proteolysis sites in the peptides. Furthermore, isothermal titration calorimetry experiments showed that the peptides all had weak interactions with albumin, the most abundant protein in human serum.Conclusions/SignificanceTaken together, the results provide insight into the behavior of the peptides in human serum and will therefore aid in advancing antimicrobial peptide design towards systemic applications.

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“…Thus, herpes simplex virus activates TLR dependent and independent pathways via stimulation of NF κB (TLR2, TLR3, TLR9, and others) [9]. Therefore, one of the strategies of herpesvirus behavior in the infected cell is distortion and attenuation of signals coming from the TLRs and blockade of key processes of the immune response and impaired cooperation between the cells [6].…”

Section: Pathogenetic Targets Of Herpesvirus In the Human Bodymentioning

confidence: 98%

Antiviral activity and pathogenetic targets for seaweed sulfated polysaccharides in herpesvirus infections

Беседнова¹,

Макаренкова²,

Zvyagintseva

et al. 2016

Biochem. Moscow Suppl. Ser. B

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The review summarizes results of studies of effects of sulfated polysaccharides from seaweed on herpesviruses and the course of herpesvirus infections. Importance of this problem is determined by the prev alence of herpesviruses that can persist in the human body and demonstrate a high degree of immune mimicry and resistance to antiviral drugs. A wide range of physiological action of sulfated polysaccharides, receptor agonists of innate and adaptive immune cells, which possess potent antiviral, antioxidant and anti inflamma tory activities, open the possibility of their use for creation of new generation pharmacological substances and drugs with associated activity for the treatment of herpesvirus infections.

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Herpes Simplex Virus: Treatment with Antimicrobial Peptides

Cited by 16 publications

References 29 publications

Mucroporin-M1 Inhibits Hepatitis B Virus Replication by Activating the Mitogen-activated Protein Kinase (MAPK) Pathway and Down-regulating HNF4α in Vitro and in Vivo

Mucroporin-M1 Inhibits Hepatitis B Virus Replication by Activating the Mitogen-activated Protein Kinase (MAPK) Pathway and Down-regulating HNF4α in Vitro and in Vivo

Serum Stabilities of Short Tryptophan- and Arginine-Rich Antimicrobial Peptide Analogs

Antiviral activity and pathogenetic targets for seaweed sulfated polysaccharides in herpesvirus infections

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