Variability of tropism and replicative capacity of two naturally occurring influenza A H9N2 viruses in cell cultures from different tissues.
Identifieur interne : 000312 ( Hal/Corpus ); précédent : 000311; suivant : 000313Variability of tropism and replicative capacity of two naturally occurring influenza A H9N2 viruses in cell cultures from different tissues.
Auteurs : Wafa Tombari ; Imen Elbehi ; Faten Amouna ; Abdeljelil GhramSource :
- Avian Pathology [ 0307-9457 ] ; 2016.
English descriptors
- mix :
Abstract
Studies carried out on cell permissivity are of great interest to understand virus replication and pathogenicity. We described the results of a comparative analysis of replication efficiency of two naturally occurring influenza A H9N2 variants isolated from poultry and wild birds, differing by only two substitutions Q226L and T384N, in the receptor-binding site of haemagglutinin and the 380 loop region of NA proteins, respectively. Considering the overall growth of both viruses, lung cultures ensured the most efficient growth of TUN12L226N384 strain with titres up to 10(9) TCID50/ml whereas small intestine culture was highly susceptible to the TUN51Q226T384 virus reaching a titre of 10(6) TCID50/ml. The lowest replication was shown in liver cells. The addition of trypsin was essential for the replication of either virus in primary fibroblasts, but it had a marginal positive effect on virus replication in the four other culture types with maximum titres of 10(8) TCID50/ml. This means that in chicken, the proteolytic activation of the H9N2 viruses with the cleavage motif RSSR may be mediated by other endoproteases than trypsin. Further investigations should concentrate on the production of the appropriate set of viruses by a reverse genetics approach and the examination of cellular protease expression in chicken tissues. This would lead to a more complete understanding of the tropism of low-pathogenic Influenza A viruses.
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DOI: 10.1080/03079457.2016.1143086
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Hal:pasteur-01374981Le document en format XML
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<front><div type="abstract" xml:lang="en"> <p>Studies carried out on cell permissivity are of great interest to understand virus replication and pathogenicity. We described the results of a comparative analysis of replication efficiency of two naturally occurring influenza A H9N2 variants isolated from poultry and wild birds, differing by only two substitutions Q226L and T384N, in the receptor-binding site of haemagglutinin and the 380 loop region of NA proteins, respectively. Considering the overall growth of both viruses, lung cultures ensured the most efficient growth of TUN12L226N384 strain with titres up to 10(9) TCID50/ml whereas small intestine culture was highly susceptible to the TUN51Q226T384 virus reaching a titre of 10(6) TCID50/ml. The lowest replication was shown in liver cells. The addition of trypsin was essential for the replication of either virus in primary fibroblasts, but it had a marginal positive effect on virus replication in the four other culture types with maximum titres of 10(8) TCID50/ml. This means that in chicken, the proteolytic activation of the H9N2 viruses with the cleavage motif RSSR may be mediated by other endoproteases than trypsin. Further investigations should concentrate on the production of the appropriate set of viruses by a reverse genetics approach and the examination of cellular protease expression in chicken tissues. This would lead to a more complete understanding of the tropism of low-pathogenic Influenza A viruses.</p>
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<idno type="issn">0307-9457</idno>
<idno type="eissn">1465-3338</idno>
<title level="j">Avian Pathology</title>
<imprint> <publisher>Taylor & Francis</publisher>
<biblScope unit="volume">45</biblScope>
<biblScope unit="issue">2</biblScope>
<biblScope unit="pp">212-20</biblScope>
<date type="datePub">2016</date>
</imprint>
</monogr>
<idno type="doi">10.1080/03079457.2016.1143086</idno>
<idno type="pubmed">26813086</idno>
</biblStruct>
</sourceDesc>
<profileDesc> <langUsage> <language ident="en">English</language>
</langUsage>
<textClass> <keywords scheme="author"> <term xml:lang="en">virus host range</term>
<term xml:lang="en">low pathogenicity influenza virus</term>
<term xml:lang="en">kinetic replication</term>
<term xml:lang="en">cell tropism</term>
<term xml:lang="en">Culture cells</term>
</keywords>
<classCode scheme="mesh">Amino Acid Motifs</classCode>
<classCode scheme="mesh">Amino Acid Substitution</classCode>
<classCode scheme="mesh">Influenza in Birds</classCode>
<classCode scheme="mesh">Mutation</classCode>
<classCode scheme="mesh">Neuraminidase</classCode>
<classCode scheme="mesh">Specific Pathogen-Free Organisms</classCode>
<classCode scheme="mesh">Tropism</classCode>
<classCode scheme="mesh">Virus Replication</classCode>
<classCode scheme="mesh">Animals</classCode>
<classCode scheme="mesh">Birds</classCode>
<classCode scheme="mesh">Cells, Cultured</classCode>
<classCode scheme="mesh">Chick Embryo</classCode>
<classCode scheme="mesh">Chickens</classCode>
<classCode scheme="mesh">Female</classCode>
<classCode scheme="mesh">Hemagglutinin Glycoproteins, Influenza Virus</classCode>
<classCode scheme="mesh">Influenza A Virus, H9N2 Subtype</classCode>
<classCode scheme="halDomain" n="sdv">Life Sciences [q-bio]</classCode>
<classCode scheme="halDomain" n="sdv.bc">Life Sciences [q-bio]/Cellular Biology</classCode>
<classCode scheme="halDomain" n="sdv.mp.vir">Life Sciences [q-bio]/Microbiology and Parasitology/Virology</classCode>
<classCode scheme="halTypology" n="ART">Journal articles</classCode>
</textClass>
<abstract xml:lang="en"> <p>Studies carried out on cell permissivity are of great interest to understand virus replication and pathogenicity. We described the results of a comparative analysis of replication efficiency of two naturally occurring influenza A H9N2 variants isolated from poultry and wild birds, differing by only two substitutions Q226L and T384N, in the receptor-binding site of haemagglutinin and the 380 loop region of NA proteins, respectively. Considering the overall growth of both viruses, lung cultures ensured the most efficient growth of TUN12L226N384 strain with titres up to 10(9) TCID50/ml whereas small intestine culture was highly susceptible to the TUN51Q226T384 virus reaching a titre of 10(6) TCID50/ml. The lowest replication was shown in liver cells. The addition of trypsin was essential for the replication of either virus in primary fibroblasts, but it had a marginal positive effect on virus replication in the four other culture types with maximum titres of 10(8) TCID50/ml. This means that in chicken, the proteolytic activation of the H9N2 viruses with the cleavage motif RSSR may be mediated by other endoproteases than trypsin. Further investigations should concentrate on the production of the appropriate set of viruses by a reverse genetics approach and the examination of cellular protease expression in chicken tissues. This would lead to a more complete understanding of the tropism of low-pathogenic Influenza A viruses.</p>
</abstract>
</profileDesc>
</hal>
</record>
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