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Home / Equine Research Bank / BMC Res Notes / Cleavage site and Ectodomain of HA2 sub-unit sequence of thr...
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

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