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BMC research notes2014; 7; 448; doi: 10.1186/1756-0500-7-448

Cleavage site and Ectodomain of HA2 sub-unit sequence of three equine influenza virus isolated in Morocco.

Abstract: The equine influenza (EI) is an infectious and contagious disease of the upper respiratory tract of horses. Two outbreaks were notified in Morocco during 1997 and 2004 respectively in Nador and Essaouira. The aims of the present study concern the amino acids sequences comparison with reference strain A/equine/Miami/1963(H3N8) of the HA2 subunit including the cleavage site of three equine influenza viruses (H3N8) isolated in Morocco: A/equine/Nador/1/1997(H3N8), A/equine/Essaouira/2/2004 (H3N8) and A/equine/Essaouira/3/2004 (H3N8). Results: The obtained results demonstrated that the substitutions were located at Ectodomain (ED) and transmembrane domain (TD), and they have only one arginine in cleavage site (HA1-PEKQI-R329-GI-HA2). In the Ectodomain, the mutation N/1542/T deleted the NGT glycosylation site at position 154 for both strains A/equine/Essaouira/2/2004(H3N8) and A/equine/Essaouira/3/2004(H3N8). Except for mutation D/1602/Y of the A/equine/Nador/1/1997(H3N8) strain, the other mutations were involved in non conserved sites. While the transmembrane domain (TM) of the strain A/equine/Essaouira/3/2004(H3N8) exhibits a substitution at residue C/1992/F. For the A/equine/Nador/1/1997(H3N8) strain the HA2 shows a mutation at residue M/2072/L. Three Moroccan strains reveals a common substitution at the residue E/2112/Q located between transmembrane domain TM and the cytoplasmic domain (CD). Conclusions: The given nature virulence of three Moroccan strains, the identified and reported mutations certainly played a permissive role of infection viral process.
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Publication Date: 2014-07-12 PubMed ID: 25016480PubMed Central: PMC4118787DOI: 10.1186/1756-0500-7-448Google Scholar: Lookup
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Summary

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The research investigates variations in the amino acid sequences of the HA2 subunit in three strains of equine influenza virus isolated in Morocco, comparing these with a reference strain. The differences observed may play a role in the virulence and the process of infection of these strains.

Objective and Study Subjects

  • The study aimed to compare the amino acid sequences of the HA2 subunit, focusing particularly on the cleavage site, of three Equine Influenza Viruses (EIVs) isolated in Morocco with a reference strain, A/equine/Miami/1963(H3N8).
  • The EIVs under investigation were A/equine/Nador/1/1997(H3N8), A/equine/Essaouira/2/2004 (H3N8), and A/equine/Essaouira/3/2004 (H3N8), which were involved in two disease outbreaks in 1997 and 2004 in Morocco.

Findings

  • Substitutions in the amino acid sequences were observed at the Ectodomain (ED) and Transmembrane Domain (TD).
  • Only one arginine was present in the cleavage site (HA1-PEKQI-R329-GI-HA2).
  • The Ectodomain of the Essaouira strains showed a mutation (N/1542/T) that removed the glycosylation site at position 154.
  • Most mutations were found in non-conserved sites, except the D/1602/Y mutation in the A/equine/Nador/1/1997(H3N8) strain.
  • The Transmembrane Domain of the A/equine/Essaouira/3/2004(H3N8) strain had a substitution at residue C/1992/F, while the A/equine/Nador/1/1997(H3N8) had a mutation at residue M/2072/L.
  • A common substitution was observed at residue E/2112/Q, between the Transmembrane Domain and the Cytoplasmic domain, across all the three Moroccan strains.

Implications

  • The variations identified in the HA2 subunit amino acid sequences of the Moroccan EIVs could play a role in enabling the virus to infect and demonstrating the virulent nature of these strains.
  • The information gathered from this study can provide insight into the molecular mechanisms of Equine Influenza virus infection and assist in designing effective antiviral strategies.

Cite This Article

APA
Boukharta M, Zakham F, Touil N, Elharrak M, Ennaji MM. (2014). Cleavage site and Ectodomain of HA2 sub-unit sequence of three equine influenza virus isolated in Morocco. BMC Res Notes, 7, 448. https://doi.org/10.1186/1756-0500-7-448

Publication

BMC research notes
ISSN: 1756-0500
NlmUniqueID: 101462768
Country: England
Language: English
Volume: 7
Pages: 448

Researcher Affiliations

Boukharta, Mohamed
    Zakham, Fathiah
      Touil, Nadia
        Elharrak, Mehdi
          Ennaji, Moulay Mustapha
          • University Hassan II, Faculty of Sciences and Techniques, Mohammedia-Casablanca, Laboratory of Virology, Microbiology and Quality/ETB, Mohammedia BP 146, (20650), Morocco. m.ennaji@yahoo.fr.

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Disease Outbreaks
          • Hemagglutinin Glycoproteins, Influenza Virus / classification
          • Hemagglutinin Glycoproteins, Influenza Virus / genetics
          • Horse Diseases / epidemiology
          • Horse Diseases / virology
          • Horses
          • Influenza A Virus, H3N8 Subtype / genetics
          • Influenza A Virus, H3N8 Subtype / isolation & purification
          • Molecular Sequence Data
          • Morocco / epidemiology
          • Mutation
          • Orthomyxoviridae Infections / epidemiology
          • Orthomyxoviridae Infections / veterinary
          • Orthomyxoviridae Infections / virology
          • Phylogeny
          • Protein Structure, Tertiary
          • Protein Subunits / classification
          • Protein Subunits / genetics
          • Proteolysis
          • Sequence Alignment

          References

          This article includes 42 references
          1. van Maanen C, Cullinane A. Equine influenza virus infections: an update.. Vet Q 2002 Jun;24(2):79-94.
            doi: 10.1080/01652176.2002.9695127pubmed: 12095083google scholar: lookup
          2. Myers C, Wilson D. Equine Influenza Virus. Clin Tech Equine Pract 2006;5:187–196.
            doi: 10.1053/j.ctep.2006.03.013google scholar: lookup
          3. Timoney PJ. Equine influenza.. Comp Immunol Microbiol Infect Dis 1996 Jun;19(3):205-11.
            doi: 10.1016/0147-9571(96)00006-9pubmed: 8800546google scholar: lookup
          4. Lai AC, Rogers KM, Glaser A, Tudor L, Chambers T. Alternate circulation of recent equine-2 influenza viruses (H3N8) from two distinct lineages in the United States.. Virus Res 2004 Mar 15;100(2):159-64.
            doi: 10.1016/j.virusres.2003.11.019pubmed: 15019234google scholar: lookup
          5. SOVINOVA O, TUMOVA B, POUSKA F, NEMEC J. Isolation of a virus causing respiratory disease in horses.. Acta Virol 1958 Jan-Mar;2(1):52-61.
            pubmed: 13533033
          6. WADDELL GH, TEIGLAND MB, SIGEL MM. A NEW INFLUENZA VIRUS ASSOCIATED WITH EQUINE RESPIRATORY DISEASE.. J Am Vet Med Assoc 1963 Sep 15;143:587-90.
            pubmed: 14077956
          7. Zientara S. Epidémiologie moléculaire: l’exemple de la grippe des équidés. Epidémiologie Et Santé Animale 2001;39:69–74.
          8. Daly JM, Newton JR, Mumford JA. Current perspectives on control of equine influenza.. Vet Res 2004 Jul-Aug;35(4):411-23.
            doi: 10.1051/vetres:2004023pubmed: 15236674google scholar: lookup
          9. Daly JM, Lai AC, Binns MM, Chambers TM, Barrandeguy M, Mumford JA. Antigenic and genetic evolution of equine H3N8 influenza A viruses.. J Gen Virol 1996 Apr;77 ( Pt 4):661-71.
            doi: 10.1099/0022-1317-77-4-661pubmed: 8627254google scholar: lookup
          10. Daly JM, MacRae S, Newton JR, Wattrang E, Elton DM. Equine influenza: a review of an unpredictable virus.. Vet J 2011 Jul;189(1):7-14.
            doi: 10.1016/j.tvjl.2010.06.026pubmed: 20685140google scholar: lookup
          11. Zhirnov OP, Vorobjeva IV, Saphonova OA, Poyarkov SV, Ovcharenko AV, Anhlan D, Malyshev NA. Structural and evolutionary characteristics of HA, NA, NS and M genes of clinical influenza A/H3N2 viruses passaged in human and canine cells.. J Clin Virol 2009 Aug;45(4):322-33.
            doi: 10.1016/j.jcv.2009.05.030pubmed: 19546028google scholar: lookup
          12. Chen W, Calvo PA, Malide D, Gibbs J, Schubert U, Bacik I, Basta S, O'Neill R, Schickli J, Palese P, Henklein P, Bennink JR, Yewdell JW. A novel influenza A virus mitochondrial protein that induces cell death.. Nat Med 2001 Dec;7(12):1306-12.
            doi: 10.1038/nm1201-1306pubmed: 11726970google scholar: lookup
          13. Wright PF, Neumann G, Kawaoka Y. Orthomyxoviruses. Fields Virology 2007;Volume 2, 5: pp. 1691–1740.
          14. Louisirirotchanakul S, Lerdsamran H, Wiriyarat W, Sangsiriwut K, Chaichoune K, Pooruk P, Songserm T, Kitphati R, Sawanpanyalert P, Komoltri C, Auewarakul P, Puthavathana P. Erythrocyte binding preference of avian influenza H5N1 viruses.. J Clin Microbiol 2007 Jul;45(7):2284-6.
            doi: 10.1128/JCM.00921-07pmc: PMC1933005pubmed: 17522271google scholar: lookup
          15. Isin B, Doruker P, Bahar I. Functional motions of influenza virus hemagglutinin: a structure-based analytical approach.. Biophys J 2002 Feb;82(2):569-81.
            doi: 10.1016/S0006-3495(02)75422-2pmc: PMC1301869pubmed: 11806902google scholar: lookup
          16. Bullough PA, Hughson FM, Treharne AC, Ruigrok RW, Skehel JJ, Wiley DC. Crystals of a fragment of influenza haemagglutinin in the low pH induced conformation.. J Mol Biol 1994 Mar 4;236(4):1262-5.
            doi: 10.1016/0022-2836(94)90027-2pubmed: 8120902google scholar: lookup
          17. Chen J, Skehel JJ, Wiley DC. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil.. Proc Natl Acad Sci U S A 1999 Aug 3;96(16):8967-72.
            doi: 10.1073/pnas.96.16.8967pmc: PMC17716pubmed: 10430879google scholar: lookup
          18. Skehel JJ, Wiley DC. Influenza haemagglutinin.. Vaccine 2002 May 15;20 Suppl 2:S51-4.
            pubmed: 12110258doi: 10.1016/s0264-410x(02)00131-7google scholar: lookup
          19. Munster VJ, Schrauwen EJ, de Wit E, van den Brand JM, Bestebroer TM, Herfst S, Rimmelzwaan GF, Osterhaus AD, Fouchier RA. Insertion of a multibasic cleavage motif into the hemagglutinin of a low-pathogenic avian influenza H6N1 virus induces a highly pathogenic phenotype.. J Virol 2010 Aug;84(16):7953-60.
            doi: 10.1128/JVI.00449-10pmc: PMC2916526pubmed: 20519405google scholar: lookup
          20. Klenk HD, Garten W. Host cell proteases controlling virus pathogenicity.. Trends Microbiol 1994 Feb;2(2):39-43.
            doi: 10.1016/0966-842X(94)90123-6pubmed: 8162439google scholar: lookup
          21. Stieneke-Gröber A, Vey M, Angliker H, Shaw E, Thomas G, Roberts C, Klenk HD, Garten W. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease.. EMBO J 1992 Jul;11(7):2407-14.
            pmc: PMC556715pubmed: 1628614doi: 10.1002/j.1460-2075.1992.tb05305.xgoogle scholar: lookup
          22. Walker JA, Molloy SS, Thomas G, Sakaguchi T, Yoshida T, Chambers TM, Kawaoka Y. Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus.. J Virol 1994 Feb;68(2):1213-8.
            pmc: PMC236564pubmed: 8289354doi: 10.1128/jvi.68.2.1213-1218.1994google scholar: lookup
          23. Cross KJ, Langley WA, Russell RJ, Skehel JJ, Steinhauer DA. Composition and functions of the influenza fusion peptide.. Protein Pept Lett 2009;16(7):766-78.
            doi: 10.2174/092986609788681715pubmed: 19601906google scholar: lookup
          24. Roberts B. Influenza: biology, infection, and control. Emerging Infections in Asia 2008; pp. 3–30.
            doi: 10.1007/978-0-387-75722-3_1#page-1google scholar: lookup
          25. Varecková E, Mucha V, Kostolanský F, Gubareva LV, Klimov A. HA2-specific monoclonal antibodies as tools for differential recognition of influenza A virus antigenic subtypes.. Virus Res 2008 Mar;132(1-2):181-6.
            doi: 10.1016/j.virusres.2007.10.004pubmed: 18037184google scholar: lookup
          26. Nobusawa E, Aoyama T, Kato H, Suzuki Y, Tateno Y, Nakajima K. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses.. Virology 1991 Jun;182(2):475-85.
            doi: 10.1016/0042-6822(91)90588-3pubmed: 2024485google scholar: lookup
          27. Macosko JC, Kim CH, Shin YK. The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR.. J Mol Biol 1997 Apr 18;267(5):1139-48.
            doi: 10.1006/jmbi.1997.0931pubmed: 9150402google scholar: lookup
          28. Skehel JJ, Waterfield MD. Studies on the primary structure of the influenza virus hemagglutinin.. Proc Natl Acad Sci U S A 1975 Jan;72(1):93-7.
            doi: 10.1073/pnas.72.1.93pmc: PMC432247pubmed: 1054518google scholar: lookup
          29. Smirnova YA, Fedorova NV, Ksenofontov AL, Kordyukova LV, Serebryakova MV, Baratova LA, Vaskovsky BV. Isolation of the influenza A HA2 C-terminal segment by combination of nonionic detergents.. Adv Exp Med Biol 2009;611:311-2.
            doi: 10.1007/978-0-387-73657-0_139pubmed: 19400206google scholar: lookup
          30. Boukharta M, Touil N, El Fahim E, Terta M, Kissi B, Loutfi C, El Harrak M, Ennaji MM. Phylogenetic and molecular characterization of the equine influenza virus A (H3N8) causing the 1997 and 2004 outbreaks in Morocco. J Equine Vet Sci 2013.
            doi: 10.1016/j.jevs.2013.10.174google scholar: lookup
          31. Laabassi F, Lecouturier F, Amelot G, Gaudaire D, Mamache B, Laugier C, Legrand L, Zientara S, Hans A. Epidemiology and Genetic Characterization of H3N8 Equine Influenza Virus Responsible for Clinical Disease in Algeria in 2011.. Transbound Emerg Dis 2015 Dec;62(6):623-31.
            pubmed: 24472362doi: 10.1111/tbed.12209google scholar: lookup
          32. Kissi B, Daoudi N, El Kantour A, Id Sidi Yahia K, Benazzou H. Premier isolement au Maroc du virus de la grippe équine baptisé A/Equi/Maroc/1/97. Espace Vétérinaire 1998;14:10.
          33. World Organization for Animal Health OIE. World Animal Health Information Database (WAHID) 2004. ftp://ftp.oie.int/SAM/2004/MAR_F.pdf.
          34. World Organization for Animal Health OIE. 2012. http://www.oie.int/fr/normes-internationales/manuel-terrestre/acces-en-ligne/ (Vaccines MoSfDTa ed., vol. Chapter 2.5.7.
          35. Tissier O. Etude comparative de séquences du virus de la grippe équine en France. 2008.
          36. Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees.. Mol Biol Evol 1987 Jul;4(4):406-25.
            pubmed: 3447015doi: 10.1093/oxfordjournals.molbev.a040454google scholar: lookup
          37. Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0.. Mol Biol Evol 2007 Aug;24(8):1596-9.
            doi: 10.1093/molbev/msm092pubmed: 17488738google scholar: lookup
          38. Gohrbandt S, Veits J, Hundt J, Bogs J, Breithaupt A, Teifke JP, Weber S, Mettenleiter TC, Stech J. Amino acids adjacent to the haemagglutinin cleavage site are relevant for virulence of avian influenza viruses of subtype H5.. J Gen Virol 2011 Jan;92(Pt 1):51-9.
            doi: 10.1099/vir.0.023887-0pubmed: 20881092google scholar: lookup
          39. Bogs J, Veits J, Gohrbandt S, Hundt J, Stech O, Breithaupt A, Teifke JP, Mettenleiter TC, Stech J. Highly pathogenic H5N1 influenza viruses carry virulence determinants beyond the polybasic hemagglutinin cleavage site.. PLoS One 2010 Jul 27;5(7):e11826.
            doi: 10.1371/journal.pone.0011826pmc: PMC2910732pubmed: 20676399google scholar: lookup
          40. Sui J, Hwang WC, Perez S, Wei G, Aird D, Chen LM, Santelli E, Stec B, Cadwell G, Ali M, Wan H, Murakami A, Yammanuru A, Han T, Cox NJ, Bankston LA, Donis RO, Liddington RC, Marasco WA. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses.. Nat Struct Mol Biol 2009 Mar;16(3):265-73.
            doi: 10.1038/nsmb.1566pmc: PMC2692245pubmed: 19234466google scholar: lookup
          41. Du L, Zhou Y, Jiang S. Research and development of universal influenza vaccines.. Microbes Infect 2010 Apr;12(4):280-6.
            doi: 10.1016/j.micinf.2010.01.001pubmed: 20079871google scholar: lookup
          42. Keleta L, Ibricevic A, Bovin NV, Brody SL, Brown EG. Experimental evolution of human influenza virus H3 hemagglutinin in the mouse lung identifies adaptive regions in HA1 and HA2.. J Virol 2008 Dec;82(23):11599-608.
            doi: 10.1128/JVI.01393-08pmc: PMC2583651pubmed: 18829764google scholar: lookup

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