Isolation of the Influenza A HA2 C-terminal segment by combination of nonionic detergents

Smirnova, Yu. A.; Fedorova, N. V.; Ksenofontov, Alexander L.; Kordyukova, Larisa V.; Serebryakova, Marina V.; Baratova, Ludmila A.; Vaskovsky, B. V.

doi:10.1007/978-0-387-73657-0_139

Cited by 5 publications

(2 citation statements)

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“…The NP forms the viral ribonucleoprotein complex for each segment (vRNP,~250 kD), which is essential for the transcription and replication of viral genome (Klaus, Ruigrok, & Baudin, 1997;Mena et al, 1999;Voeten et al, 2000) The infection cycle begins with the attachment of the viral particle to the sialic acids of the cell membrane (Temoltzin-Palacios & Thomas, 1994). Endosomal acidification causes a three-dimensional modification of HA, which is crucial for the fusion of the viral and the endosomal membranes (Chen, Skehel, & Wiley, 1999;Skehel & Waterfield, 1975;Smirnova et al, 2009). Activation of the proton channels of the virion (M2) results in the dissociation of the vRNP complexes from the M1 matrix proteins that provide the stability to the viral architecture via the interaction with the envelope and the viral nucleocapsid (Castrucci & Kawaoka, 1995;Elton, Medcalf, Bishop, Harrison, & Digard, 1999;Ito et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Prediction of genetic mutations of equine influenza virus related to adaptive determination nuclear export ribonucleoprotein complex

Boukharta

Kasmi

Zakham

et al. 2019

JoBAZ

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Background: Segment eight (08) of equine influenza virus strain (H3N8) encodes for two non-structural proteins: NS1 (non-structural protein number 1) and NS2, also called NEP (nuclear export protein), via alternative splicing of the pre-messenger RNA transcripts. The NS1 inhibits the cell defense system, while the NEP activates the translocation of the ribonucleoprotein complex to the cytoplasm, a key step in viral assembly. Mutations in this protein could influence viral multiplication. Results: In this present study, we used computational and in silico tools to investigate the impact of mutations on the three-dimensional structure of the CRM1 of NEP proteins of three equine influenza strains (H3N8) isolated in Morocco (A/equine/Nador/1/1997 (H3N8), A/equine/Essaouira/2/2004 (H3N8), and A/equine/Essaouira/3/2004 (H3N8)). Compared to the reference strain, the two strains of Essaouira showed no mutations in the domain-binding CRM1 of the NEP protein, while the A/equine/Nador/1/1997 strain (H3N8) had two mutations at the T/33/I and Q/34/R residues. These two mutations corresponded to adaptation phenomenon of the equine cellular environment, since they enhance the interaction between the protein NEP and CRM1 proteins with a greater affinity compared to the reference strain. Conclusion: The three-dimensional modification of the NEP protein of the A/equine/Nador/1/1997 strain further facilitates nucleocytoplasmic trafficking in equine species.

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Section: Introductionmentioning

confidence: 99%

Prediction of genetic mutations of equine influenza virus related to adaptive determination nuclear export ribonucleoprotein complex

Boukharta

Kasmi

Zakham

et al. 2019

JoBAZ

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“…Residues 1–185 are the ectodomain (ED) within the N-terminal extremity of 22 amino acid representing the “fusion peptide (PF)”[28], the residues 185–211 are the transmembrane domain (TM) and finally residues 211–221 form the cytoplasmic domain (CD) embedded within the viral particle [17,29]. …”

Section: Introductionmentioning

confidence: 99%

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

et al. 2014

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BackgroundThe 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).ResultsThe 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/154 2 /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/199 2 /F. For the A/equine/Nador/1/1997(H3N8) strain the HA2 shows a mutation at residue M/207 2 /L. Three Moroccan strains reveals a common substitution at the residue E/211 2 /Q located between transmembrane domain TM and the cytoplasmic domain (CD).ConclusionThe 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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Role of Genetic and Molecular Dynamics in the Emergence, Reemergence, and Interspecies Transmission of Equine Influenza Viruses

Boukharta

Amri

Zakham

et al. 2020

Emerging and Reemerging Viral Pathogens

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Isolation of the Influenza A HA2 C-terminal segment by combination of nonionic detergents

Cited by 5 publications

References 1 publication

Prediction of genetic mutations of equine influenza virus related to adaptive determination nuclear export ribonucleoprotein complex

Prediction of genetic mutations of equine influenza virus related to adaptive determination nuclear export ribonucleoprotein complex

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

Role of Genetic and Molecular Dynamics in the Emergence, Reemergence, and Interspecies Transmission of Equine Influenza Viruses

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