A phage-displayed peptide recognizing porcine aminopeptidase N is a potent small molecule inhibitor of PEDV entry

Virology

Volumn 456-457, Issue 1, 2014, Pages 20-27

  Meng, Fandan ^a   Suo, Siqingaowa ^a   Zarlenga, Dante S ^b   Cong, Yingying ^a   Ma, Xiaowei ^a   Zhao, Qiong ^a   Ren, Xiaofeng ^a  

^a NORTHEAST AGRICULTURAL UNIVERSITY   (China)

^b AGRICULTURAL RESEARCH SERVICE   (United States)

Author keywords

Coronavirus; PEDV; Peptides; Virus attachment

Indexed keywords

MICROSOMAL AMINOPEPTIDASE; PEPTIDE DERIVATIVE; PEPTIDE F; PEPTIDE H; S PEPTIDE; UNCLASSIFIED DRUG; VITRONECTIN;

ANIMAL CELL; ANTIVIRAL ACTIVITY; ARTICLE; CELL ADHESION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG PROTEIN BINDING; IMMUNOFLUORESCENCE; INCUBATION TIME; NONHUMAN; PHAGE DISPLAY; PORCINE EPIDEMIC DIARRHEA; PORCINE EPIDEMIC DIARRHEA VIRUS; PRIORITY JOURNAL; PSEUDORABIES HERPETOVIRUS; REAL TIME POLYMERASE CHAIN REACTION; TEMPERATURE; TRANSMISSIBLE GASTROENTERITIS VIRUS; VERO CELL; VIRUS ENTRY; VIRUS INFECTIVITY; VIRUS INHIBITION; WESTERN BLOTTING;

CORONAVIRUS; PEDV; PEPTIDES; VIRUS ATTACHMENT;

ANIMALS; ANTIGENS, CD13; ANTIVIRAL AGENTS; CERCOPITHECUS AETHIOPS; HERPESVIRUS 1, SUID; PEPTIDE LIBRARY; PEPTIDES; PORCINE EPIDEMIC DIARRHEA VIRUS; TRANSMISSIBLE GASTROENTERITIS VIRUS; VERO CELLS; VIRUS INTERNALIZATION;

EID: 84897905289     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2014.01.010     Document Type: Article

References (38)

1. Baldick C.J., Wichroski M.J., Pendri A., Walsh A.W., Fang J., Mazzucco C.E., Pokornowski K.A., Rose R.E., Eggers B.J., Hsu M., Zhai W., Zhai G., Gerritz S.W., Poss M.A., Meanwell N.A., Cockett M.I., Tenney D.J. A novel small molecule inhibitor of Hepatitis C virus entry. PLoS Pathog. 2010, 6:e1001086.
2. Bishop-Hurley S.L., Mounter S.A., Laskey J., Morris R.O., Elder J., Roop P., Rouse C., Schmidt F.J., English J.T. Phage-displayed peptides as developmental agonists for Phytophthora capsici zoospores. Appl. Environ. Microbiol. 2002, 68:3315-3320.
3. Bishop-Hurley S.L., Rea P.J., McSweeney C.S. Phage-displayed peptides selected for binding to Campylobacter jejuni are antimicrobial. Protein Eng. Des. Sel. 2010, 23:751-757.
4. Bishop-Hurley S.L., Schmidt F.J., Erwin A.L., Smith A.L. Peptides selected for binding to a virulent strain of Haemophilus influenzae by phage display are bactericidal. Antimicrob. Agents Chemother. 2005, 49:2972-2978.
5. Bosch B.J., van der Zee R., de Haan C.A., Roitter P.J. The coronavirus spike protein is a class I virus fusion protein: structural and functional characterization of the fusion core complex. J. Virol. 2003, 77:8801-8811.
6. Bridgen A., Duarte M., Tobler K., Laude H., Ackermann M. Sequence determination of the nucleocapsid protein gene of the porcine epidemic diarrhoea virus confirms that this virus is a coronavirus related to human coronavirus 229E and porcine transmissible gastroenteritis virus. J.Gen.Virol. 1993, 74:1795-1804.
7. Carnazza S., Foti C., Gioffre G., Felici F., Guglielmino S. Specific and selective probes for Pseudomonas aeruginosa from phage-displayed random peptide libraries. Biosens. Bioelectron. 2008, 23:1137-1144.
8. Cavanagh D. Nidovirales, a new order comprising Coronaviridae and Arteriviridae. Arch. Virol. 1997, 142:629-633.
9. Delmas B., Gelfi J., L'Haridon R., Vogel L.K., Sjöström H., Norén O., Laude H. Aminopeptidase N is a major receptor for the enteropathogenic coronavirus TGEV. Nature 1992, 357:417-420.
10. Fang Z.D., Laskey J.G., Huang S., Bilyeu K.D., Morris R.O., Schmidt F.J., English J.T. Combinatorially selected defense peptides protect plant roots from pathogen infection. Proc. Natl. Acad. Sci. USA 2006, 103:18444-18449.
11. Ferrer M., Harrison S.C. Peptide ligands to human immunodeficiency virus type 1 gp120 identified from phage display libraries. J. Virol. 1999, 3:5795-5802.
12. Gallagher T.M., Buchmeier M.J. Coronavirus spike proteins in viral entry and pathogenesis. Virology 2001, 279:371-374.
13. Hofmann M., Wyler R. Propagation of the virus of porcine epidemic diarrhea in cell culture. J. Clin. Microbiol. 1988, 26:2235-2239.
14. Kenny A.J., Maroux S. Topology of microvillar membrance hydrolases of kidney and intestine. Physiol. Rev. 1982, 62:91-128.
15. Kwon H.J., Kim H.H., Yoon S.Y., Ryu Y.B., Chang J.S., Cho K.O., Rho M.C., Park S.J., Lee W.S. In vitro inhibitory activity of Alpinia katsumadai extracts against influenza virus infection and hemagglutination. Virol. J. 2010, 7:2-9.
16. Lai M.M.C., Perlman S., Anderson L.J. Coronaviridae. Fields Virology 2007, 1305-1336. Lippincott, Williams and Wilkins, Philadelphia. D.M. Knipe, P.M. Howley, D.E. Griffin, M.A. Martin, R.A. Lamb, B. Roizman, S.E. Straus (Eds.).
17. Lendeckel U., Kähne T., Riemann D., Neubert K., Arndt M., Reinhold D. Review: the role of membrane peptidases in immune functions. Adv. Exp. Med. Biol. 2000, 477:1-24.
18. Li B.X., Ge J.W., Li Y.J. Porcine aminopeptidase N is a functional receptor for the PEDV coronavirus. Virology 2007, 365:166-172.
19. Li P., Ren X. Reverse transcription loop-mediated isothermal amplification for rapid detection of transmissible gastroenteritis virus. Curr. Microbiol. 2011, 62:1074-1080. 10.1007/s00284-010-9825-9.
20. Liu B., Li G., Sui X., Yin J., Wang H., Ren X. Expression and functional analysis of porcine aminopeptidase N produced in prokaryotic expression system. J. Biotechnol. 2009, 141:91-96.
21. Müller V., Chávez J., Reginatto H., Zucolotto F.H., Niero S.M., Navarro R., Yunes D., Schenkel R.A., Barardi E.P., Zanetti C.R.M., Simoes, C.M.O. Evaluation of antiviral activity of South American plant extracts against Herpes Simplex Virus Type 1 and Rabies Virus. Phytother. Res. 2007, 21:970-974.
22. Nam E., Lee C. Contribution of the porcine aminopeptidase N (CD13) receptor density to porcine epidemic diarrhea virus infection. Vet. Microbiol. 2010, 144:41-50.
23. Oh J.S., Song D.S., Park B.H. Identification of a putative cellular receptor 150kDa polypeptide for porcine epidemic diarrhea virus in porcine enterocytes. J. Vet. Sci. 2003, 4:269-275.
24. Paeshuyse J., Leyssen P., Mabery E., Boddeker N., Vrancken R., Froeyen M., Ansari I.H., Dutartre H., Rozenski J., Gil L.H.V.G., Letellier C., Lanford R., Canard B., Koenen F., Kerkhofs P., Donis R.O., Herdewijn P., Watson J., Clercq E.D., Puerstinger G., Neyts J. A novel, highly selective inhibitor of Pestivirus replication that targets the viral RNA-dependent RNA polymerase. J. Virol. 2006, 80:149-160.
25. Pensaert M.B., Yeo S.G. Porcine epidemic diarrhea. Diseases of Swine 2006, 367-372. Wiley-Blackwell, Ames. B.E. Straw, J.J. Zimmerman, S. D[U+05F3]Allaire, D.J. Taylor (Eds.).
26. Ren X., Glende J., Yin J., Schwegmann-Wessels C., Herrler G. Importance of cholesterol for infection of cells by transmissible gastroenteritis virus. Virus Res. 2008, 137:220-224.
27. Ren X., Liu B., Yin J., Zhang H., Li G. Phage displayed peptides recognizing porcine aminopeptidase N inhibit transmissible gastroenteritis coronavirus infection in vitro. Virology 2011, 410:299-306.
28. Ren X., Meng F., Yin J., Li G., Li X., Wang C., Herrler G. Action mechanisms of lithium chloride on cell infection by transmissible gastroenteritis Coronavirus. PloS One 2011, 6:e18669.
29. Ren X., Suo S., Jang Y.S. Development of a porcine epidemic diarrhea virus M protein-based ELISA for virus detection. Biotechnol. Lett. 2011, 33:215-220.
30. Ren X., Wang M., Yin J., Li G. Phages harboring specific peptides that recognize the N protein of the porcine reproductive and respiratory syndrome virus distinguish the virus from other viruses. J. Clin. Microbiol. 2010, 48:1875-1881.
31. Ren X., Yin J., Li G., Herrler G. Cholesterol dependence of pseudorabies herpesvirus entry. Curr. Microbiol. 2011, 62:261-266.
32. Sanchez C., Gebauer M.F., Sune C., Mendez A., Dopazo J., Enjuanes L. Genetic evolution and tropism of transmissible gastroenteritis Coronavirus. Virology. 1992, 190:92-105.
33. Spaan W.J.M., Brian D., Cavanagh D., Groot R.J., Enjuanes L., Gorbalenya A.E., Holmes K.V., Masters P.S., Rottier P.J., Taguchi F., Talbot P. Family Coronaviridae. Virus Taxonomy, Eighth Report of the International Committee on Taxonomy of Viruses 2005, 947-964. Elsevier Academic Press, London. C.M. Fauquet, M.A. Mayo, J. Maniloff, U. Desselberg, L.A. Ball (Eds.).
34. Weiss S.R., Navas-Martin S. Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus. Microbiol. Mol. Biol. Rev. 2005, 69:635-664.
35. Welch B.D., VanDemark A.P., Heroux A., Hill C.P., Kay M.S. Potent D-peptide inhibitors of HIV-1 entry. Proc. Natl. Acad. Sci. USA 2007, 104:16828-16833.
36. Wu D., Li G., Qin C., Ren X. Phage displayed peptides to Avian H5N1 virus distinguished the virus from other viruses. PloS One 2011, 6:e23058.
37. Yang B., Gao L., Li L., Lu Z., Fan X., Patel C.A., Pomerantz R.J., DuBois G.C., Zhang H. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency Virus type I (HIV-1) Vif proteins. J. Biol. Chem. 2003, 278:6596-6602.
38. Yin J., Glende J., Schwegmann-Wessels C., Enjuanes L., Herrler G., Ren X. Cholesterol is important for a post-adsorption step in the entry process of transmissible gastroenteritis virus. Antivir Res. 2010, 88:311-316.