Skip to main content
Top
Published in: Virology Journal 1/2020

Open Access 01-12-2020 | Herpes Simplex Type 1 | Research

Anti-HSV-1 activity of Aspergillipeptide D, a cyclic pentapeptide isolated from fungus Aspergillus sp. SCSIO 41501

Authors: Zhaoyang Wang, Jiaoyan Jia, Lu Wang, Feng Li, Yiliang Wang, Yuzhou Jiang, Xiaowei Song, Shurong Qin, Kai Zheng, Ju Ye, Zhe Ren, Yifei Wang, Shuhua Qi

Published in: Virology Journal | Issue 1/2020

Login to get access

Abstract

Background

Herpes simplex virus 1, an enveloped DNA virus belonging to the Herpesviridae family, spreads to neurons and causes pathological changes in the central nervous system. The purpose of this study was to investigate the potency and mechanism of antiviral activity of Aspergillipeptide D, a cyclic pentapeptide isolated from a culture broth of marine gorgonian-derived fungus Aspergillus sp. SCSIO 41501, At present, there are many studies on the anti-tumor, anti-clotting, anti-oxidant and immunoinflammatory effects of Aspergillipeptide D, but little research has been done on the anti-HSV-1 activity of Aspergillipeptide D.

Methods

The anti-HSV-1 activity of Aspergillipeptide D was evaluated by plaque reduction assay. The mechanism of action against HSV-1 was determined from the effective stage. Then we assayed the viral DNA replication, viral RNA synthesis and protein expression, respectively. We also identified the proteins that interact with gB by mass spectrometry, and assayed the effect of Aspergillipeptide D on the interaction between the virus gB protein and cell proteins.

Results

Plaque reduction experiments showed that Aspergillipeptide D did not affect HSV-1 early infection events, including viral inactivation, attachment and penetration. Interestingly, Aspergillipeptide D dramatically reduced both the gene and protein levels of viral late protein gB, and suppressed its location in the endoplasmic reticulum and Golgi apparatus. In contrast, overexpression of gB restored viral production. Finally, proteomic analysis revealed that the numbers of cellular proteins that interacted with gB protein was largely decreased by Aspergillipeptide D. These results suggested that Aspergillipeptide D inhibited gB function to affect HSV-1 intercellular spread.

Conclusions

Our results indicated that Aspergillipeptide D might be a potential candidate for HSV-1 therapy, especially for ACV-resistant strains.
Literature
1.
go back to reference Victor Shahin WH. The genome of HSV-1 translocates through the nuclear pore as a condensed rod-like structure. J Cell Sci. 2006;119:23–30.CrossRef Victor Shahin WH. The genome of HSV-1 translocates through the nuclear pore as a condensed rod-like structure. J Cell Sci. 2006;119:23–30.CrossRef
2.
go back to reference Mettenleiter TC, Klupp BG, Granzow H. Herpesvirus assembly: an update. Virus Res. 2009;143:222–34.CrossRef Mettenleiter TC, Klupp BG, Granzow H. Herpesvirus assembly: an update. Virus Res. 2009;143:222–34.CrossRef
3.
go back to reference Loret S, Guay G, Lippe R. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol. 2008;82:8605–18.CrossRef Loret S, Guay G, Lippe R. Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol. 2008;82:8605–18.CrossRef
4.
go back to reference Spear PG, Longnecker R. Herpesvirus entry: an update. J Virol. 2003;77:10179–85.CrossRef Spear PG, Longnecker R. Herpesvirus entry: an update. J Virol. 2003;77:10179–85.CrossRef
5.
go back to reference Browne H, Bruun B, Whiteley A, Minson T. Analysis of the role of the membrane-spanning and cytoplasmic tail domains of herpes simplex virus type 1 glycoprotein D in membrane fusion. J Gen Virol. 2003;84:1085–9.CrossRef Browne H, Bruun B, Whiteley A, Minson T. Analysis of the role of the membrane-spanning and cytoplasmic tail domains of herpes simplex virus type 1 glycoprotein D in membrane fusion. J Gen Virol. 2003;84:1085–9.CrossRef
6.
go back to reference Pertel PE, Fridberg A, Parish ML, Spear PG. Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate. Virology. 2001;279:313–24.CrossRef Pertel PE, Fridberg A, Parish ML, Spear PG. Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate. Virology. 2001;279:313–24.CrossRef
7.
go back to reference Farnsworth A, Wisner TW, Webb M, Roller R, Cohen G, Eisenberg R, Johnson DC. Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane. Proc Natl Acad Sci U S A. 2007;104:10187–92.CrossRef Farnsworth A, Wisner TW, Webb M, Roller R, Cohen G, Eisenberg R, Johnson DC. Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane. Proc Natl Acad Sci U S A. 2007;104:10187–92.CrossRef
8.
go back to reference Akhtar J, Shukla D. Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry. FEBS J. 2009;276:7228–36.CrossRef Akhtar J, Shukla D. Viral entry mechanisms: cellular and viral mediators of herpes simplex virus entry. FEBS J. 2009;276:7228–36.CrossRef
9.
go back to reference Backovic M, Jardetzky TS. Class III viral membrane fusion proteins. Curr Opin Struct Biol. 2009;19:189–96.CrossRef Backovic M, Jardetzky TS. Class III viral membrane fusion proteins. Curr Opin Struct Biol. 2009;19:189–96.CrossRef
10.
go back to reference Piret J, Boivin G. Resistance of herpes simplex viruses to nucleoside analogues: mechanisms, prevalence, and management. Antimicrob Agents Chemother. 2011;55:459–72.CrossRef Piret J, Boivin G. Resistance of herpes simplex viruses to nucleoside analogues: mechanisms, prevalence, and management. Antimicrob Agents Chemother. 2011;55:459–72.CrossRef
11.
go back to reference Kang HK, Seo CH, Park Y. Marine peptides and their anti-infective activities. Mar Drugs. 2015;13:618–54.CrossRef Kang HK, Seo CH, Park Y. Marine peptides and their anti-infective activities. Mar Drugs. 2015;13:618–54.CrossRef
12.
go back to reference Ngo DH, Vo TS, Ngo DN, Wijesekara I, Kim SK. Biological activities and potential health benefits of bioactive peptides derived from marine organisms. Int J Biol Macromol. 2012;51:378–83.CrossRef Ngo DH, Vo TS, Ngo DN, Wijesekara I, Kim SK. Biological activities and potential health benefits of bioactive peptides derived from marine organisms. Int J Biol Macromol. 2012;51:378–83.CrossRef
13.
go back to reference Kim S-K, Wijesekara I. Development and biological activities of marine-derived bioactive peptides: a review. J Funct Foods. 2010;2:1–9.CrossRef Kim S-K, Wijesekara I. Development and biological activities of marine-derived bioactive peptides: a review. J Funct Foods. 2010;2:1–9.CrossRef
14.
go back to reference Ma X, Nong X-H, Ren Z, Wang J, Liang X, Wang L, Qi S-H. Antiviral peptides from marine gorgonian-derived fungus Aspergillus sp. SCSIO 41501. Tetrahedron Lett. 2017;58:1151–5.CrossRef Ma X, Nong X-H, Ren Z, Wang J, Liang X, Wang L, Qi S-H. Antiviral peptides from marine gorgonian-derived fungus Aspergillus sp. SCSIO 41501. Tetrahedron Lett. 2017;58:1151–5.CrossRef
15.
go back to reference Wang Y, Wang Q, Zhu Q, Zhou R, Liu J, Peng T. Identification and characterization of acyclovir-resistant clinical HSV-1 isolates from children. J Clin Virol. 2011;52:107–12.CrossRef Wang Y, Wang Q, Zhu Q, Zhou R, Liu J, Peng T. Identification and characterization of acyclovir-resistant clinical HSV-1 isolates from children. J Clin Virol. 2011;52:107–12.CrossRef
16.
go back to reference Ramakrishnan MA. Determination of 50% endpoint titer using a simple formula. World J Virol. 2016;5:85.CrossRef Ramakrishnan MA. Determination of 50% endpoint titer using a simple formula. World J Virol. 2016;5:85.CrossRef
17.
go back to reference Jin F, Zhuo C, He Z, Wang H, Liu W, Zhang R, Wang Y. Anti-herpes simplex virus activity of polysaccharides from Eucheuma gelatinae. World J Microbiol Biotechnol. 2015;31:453–60.CrossRef Jin F, Zhuo C, He Z, Wang H, Liu W, Zhang R, Wang Y. Anti-herpes simplex virus activity of polysaccharides from Eucheuma gelatinae. World J Microbiol Biotechnol. 2015;31:453–60.CrossRef
18.
go back to reference Alvarez AL, Habtemariam S, Abdel Moneim AE, Melon S, Dalton KP, Parra F. A spiroketal-enol ether derivative from Tanacetum vulgare selectively inhibits HSV-1 and HSV-2 glycoprotein accumulation in Vero cells. Antivir Res. 2015;119:8–18.CrossRef Alvarez AL, Habtemariam S, Abdel Moneim AE, Melon S, Dalton KP, Parra F. A spiroketal-enol ether derivative from Tanacetum vulgare selectively inhibits HSV-1 and HSV-2 glycoprotein accumulation in Vero cells. Antivir Res. 2015;119:8–18.CrossRef
19.
go back to reference Jin F, Ma K, Chen M, Zou M, Wu Y, Li F, Wang Y. Pentagalloylglucose blocks the nuclear transport and the process of Nucleocapsid egress to inhibit HSV-1 infection. Jpn J Infect Dis. 2016;69:135–42.CrossRef Jin F, Ma K, Chen M, Zou M, Wu Y, Li F, Wang Y. Pentagalloylglucose blocks the nuclear transport and the process of Nucleocapsid egress to inhibit HSV-1 infection. Jpn J Infect Dis. 2016;69:135–42.CrossRef
20.
go back to reference Harden EA, Falshaw R, Carnachan SM, Kern ER, Prichard MN. Virucidal activity of polysaccharide extracts from four algal species against herpes simplex virus. Antivir Res. 2009;83:282–9.CrossRef Harden EA, Falshaw R, Carnachan SM, Kern ER, Prichard MN. Virucidal activity of polysaccharide extracts from four algal species against herpes simplex virus. Antivir Res. 2009;83:282–9.CrossRef
21.
go back to reference Mayer A, Rodríguez A, Taglialatela-Scafati O, Fusetani N. Marine Pharmacology in 2009–2011: Marine compounds with antibacterial, Antidiabetic, antifungal, anti-inflammatory, antiprotozoal, Antituberculosis, and antiviral activities; affecting the immune and nervous systems, and other miscellaneous mechanisms of action. Marine Drugs. 2013;11:2510–73.CrossRef Mayer A, Rodríguez A, Taglialatela-Scafati O, Fusetani N. Marine Pharmacology in 2009–2011: Marine compounds with antibacterial, Antidiabetic, antifungal, anti-inflammatory, antiprotozoal, Antituberculosis, and antiviral activities; affecting the immune and nervous systems, and other miscellaneous mechanisms of action. Marine Drugs. 2013;11:2510–73.CrossRef
22.
go back to reference Blunt JW, Copp BR, Munro MH, Northcote PT, Prinsep MR. Marine natural products. Nat Prod Rep. 2011;28:196–268.CrossRef Blunt JW, Copp BR, Munro MH, Northcote PT, Prinsep MR. Marine natural products. Nat Prod Rep. 2011;28:196–268.CrossRef
23.
go back to reference Bao J, Zhang X-Y, Xu X-Y, He F, Nong X-H, Qi S-H. New cyclic tetrapeptides and asteltoxins from gorgonian-derived fungus Aspergillus sp. SCSGAF 0076. Tetrahedron. 2013;69:2113–7.CrossRef Bao J, Zhang X-Y, Xu X-Y, He F, Nong X-H, Qi S-H. New cyclic tetrapeptides and asteltoxins from gorgonian-derived fungus Aspergillus sp. SCSGAF 0076. Tetrahedron. 2013;69:2113–7.CrossRef
24.
25.
go back to reference Baquero E, Albertini AA, Gaudin Y. Recent mechanistic and structural insights on class III viral fusion glycoproteins. Curr Opin Struct Biol. 2015;33:52–60.CrossRef Baquero E, Albertini AA, Gaudin Y. Recent mechanistic and structural insights on class III viral fusion glycoproteins. Curr Opin Struct Biol. 2015;33:52–60.CrossRef
26.
go back to reference Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol. 2011;9:369–81.CrossRef Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol. 2011;9:369–81.CrossRef
27.
go back to reference Gahmberg CG, Fagerholm SC, Nurmi SM, Chavakis T, Marchesan S, Gronholm M. Regulation of integrin activity and signalling. Biochim Biophys Acta. 1790;2009:431–44. Gahmberg CG, Fagerholm SC, Nurmi SM, Chavakis T, Marchesan S, Gronholm M. Regulation of integrin activity and signalling. Biochim Biophys Acta. 1790;2009:431–44.
28.
go back to reference Hirohata Y, Arii J, Liu Z, Shindo K, Oyama M, Kozuka-Hata H, Sagara H, Kato A, Kawaguchi Y. Herpes simplex virus 1 recruits CD98 heavy chain and beta1 integrin to the nuclear membrane for viral De-envelopment. J Virol. 2015;89:7799–812.CrossRef Hirohata Y, Arii J, Liu Z, Shindo K, Oyama M, Kozuka-Hata H, Sagara H, Kato A, Kawaguchi Y. Herpes simplex virus 1 recruits CD98 heavy chain and beta1 integrin to the nuclear membrane for viral De-envelopment. J Virol. 2015;89:7799–812.CrossRef
Metadata
Title
Anti-HSV-1 activity of Aspergillipeptide D, a cyclic pentapeptide isolated from fungus Aspergillus sp. SCSIO 41501
Authors
Zhaoyang Wang
Jiaoyan Jia
Lu Wang
Feng Li
Yiliang Wang
Yuzhou Jiang
Xiaowei Song
Shurong Qin
Kai Zheng
Ju Ye
Zhe Ren
Yifei Wang
Shuhua Qi
Publication date
01-12-2020
Publisher
BioMed Central
Published in
Virology Journal / Issue 1/2020
Electronic ISSN: 1743-422X
DOI
https://doi.org/10.1186/s12985-020-01315-z

Other articles of this Issue 1/2020

Virology Journal 1/2020 Go to the issue