Amino acids adjacent to the haemagglutinin cleavage site are relevant for virulence of avian influenza viruses of subtype H5.
Identifieur interne : 000318 ( Main/Corpus ); précédent : 000317; suivant : 000319Amino acids adjacent to the haemagglutinin cleavage site are relevant for virulence of avian influenza viruses of subtype H5.
Auteurs : Sandra Gohrbandt ; Jutta Veits ; Jana Hundt ; Jessica Bogs ; Angele Breithaupt ; Jens P. Teifke ; Siegfried Weber ; Thomas C. Mettenleiter ; Jürgen StechSource :
- The Journal of general virology [ 1465-2099 ] ; 2011.
English descriptors
- KwdEn :
- Amino Acid Motifs (genetics), Amino Acid Substitution (genetics), Animals, Chickens, Germany, Hemagglutinins, Viral (genetics), Hemagglutinins, Viral (metabolism), Influenza A Virus, H5N1 Subtype (genetics), Influenza A Virus, H5N1 Subtype (pathogenicity), Influenza in Birds (mortality), Influenza in Birds (pathology), Influenza in Birds (virology), Mutagenesis, Insertional, Mutation, Missense, Respiratory System (pathology), Respiratory System (virology), Survival Analysis, Virulence.
- MESH :
- chemical , genetics : Hemagglutinins, Viral.
- chemical , metabolism : Hemagglutinins, Viral.
- geographic : Germany.
- genetics : Amino Acid Motifs, Amino Acid Substitution, Influenza A Virus, H5N1 Subtype.
- mortality : Influenza in Birds.
- pathogenicity : Influenza A Virus, H5N1 Subtype.
- pathology : Influenza in Birds, Respiratory System.
- virology : Influenza in Birds, Respiratory System.
- Animals, Chickens, Mutagenesis, Insertional, Mutation, Missense, Survival Analysis, Virulence.
Abstract
The prime virulence determinant of highly pathogenic avian influenza viruses (HPAIVs) is the polybasic haemagglutinin (HA) cleavage site. However, engineering of a polybasic cleavage site into an avian influenza virus of low pathogenicity does not result in transformation into an HPAIV, indicating the importance of other adaptations. Here, the influence of amino acids adjacent to the HA cleavage site on virulence was studied. Most HPAIVs of subtype H5 carry serine or threonine at position 346 (corresponding to position 323 according to H3 numbering), whereas almost all low-pathogenic H5 viruses have valine. Moreover, all H5 low-pathogenic strains carry threonine at position 351 (corresponding to position 328 according to H3 numbering), suggesting that acquisition of a polybasic cleavage site involves several steps. This study generated a virus mutant derived from HPAIV A/Swan/Germany/R65/06 H5N1 (R65) with a monobasic cleavage site, R65(mono)-S-ER, and the following additional mutants: R65(mono)-V-ER with serine changed to valine at position 346, and R65(mono)-S-ETR and R65(mono)-V-ETR with threonine inserted at position 351. Moreover, in the R65 HA, serine was replaced with valine at position 346 (R65-V). Infection of chickens with R65(mono)-S-ETR or R65(mono)-S-ER led to slight transient respiratory symptoms, whereas R65-infected animals died within 2 days. However, chickens infected with R65-V survived longer than R65-infected animals, indicating that serine 346 in R65 HA contributes to virulence. These data suggest that evolution of H5 HPAIVs from low-pathogenic precursors, besides acquisition of a polybasic cleavage site, involves adaptation of neighbouring regions.
DOI: 10.1099/vir.0.023887-0
PubMed: 20881092
Links to Exploration step
pubmed:20881092Le document en format XML
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<term>Influenza A Virus, H5N1 Subtype (genetics)</term>
<term>Influenza A Virus, H5N1 Subtype (pathogenicity)</term>
<term>Influenza in Birds (mortality)</term>
<term>Influenza in Birds (pathology)</term>
<term>Influenza in Birds (virology)</term>
<term>Mutagenesis, Insertional</term>
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<front><div type="abstract" xml:lang="en">The prime virulence determinant of highly pathogenic avian influenza viruses (HPAIVs) is the polybasic haemagglutinin (HA) cleavage site. However, engineering of a polybasic cleavage site into an avian influenza virus of low pathogenicity does not result in transformation into an HPAIV, indicating the importance of other adaptations. Here, the influence of amino acids adjacent to the HA cleavage site on virulence was studied. Most HPAIVs of subtype H5 carry serine or threonine at position 346 (corresponding to position 323 according to H3 numbering), whereas almost all low-pathogenic H5 viruses have valine. Moreover, all H5 low-pathogenic strains carry threonine at position 351 (corresponding to position 328 according to H3 numbering), suggesting that acquisition of a polybasic cleavage site involves several steps. This study generated a virus mutant derived from HPAIV A/Swan/Germany/R65/06 H5N1 (R65) with a monobasic cleavage site, R65(mono)-S-ER, and the following additional mutants: R65(mono)-V-ER with serine changed to valine at position 346, and R65(mono)-S-ETR and R65(mono)-V-ETR with threonine inserted at position 351. Moreover, in the R65 HA, serine was replaced with valine at position 346 (R65-V). Infection of chickens with R65(mono)-S-ETR or R65(mono)-S-ER led to slight transient respiratory symptoms, whereas R65-infected animals died within 2 days. However, chickens infected with R65-V survived longer than R65-infected animals, indicating that serine 346 in R65 HA contributes to virulence. These data suggest that evolution of H5 HPAIVs from low-pathogenic precursors, besides acquisition of a polybasic cleavage site, involves adaptation of neighbouring regions.</div>
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<Abstract><AbstractText>The prime virulence determinant of highly pathogenic avian influenza viruses (HPAIVs) is the polybasic haemagglutinin (HA) cleavage site. However, engineering of a polybasic cleavage site into an avian influenza virus of low pathogenicity does not result in transformation into an HPAIV, indicating the importance of other adaptations. Here, the influence of amino acids adjacent to the HA cleavage site on virulence was studied. Most HPAIVs of subtype H5 carry serine or threonine at position 346 (corresponding to position 323 according to H3 numbering), whereas almost all low-pathogenic H5 viruses have valine. Moreover, all H5 low-pathogenic strains carry threonine at position 351 (corresponding to position 328 according to H3 numbering), suggesting that acquisition of a polybasic cleavage site involves several steps. This study generated a virus mutant derived from HPAIV A/Swan/Germany/R65/06 H5N1 (R65) with a monobasic cleavage site, R65(mono)-S-ER, and the following additional mutants: R65(mono)-V-ER with serine changed to valine at position 346, and R65(mono)-S-ETR and R65(mono)-V-ETR with threonine inserted at position 351. Moreover, in the R65 HA, serine was replaced with valine at position 346 (R65-V). Infection of chickens with R65(mono)-S-ETR or R65(mono)-S-ER led to slight transient respiratory symptoms, whereas R65-infected animals died within 2 days. However, chickens infected with R65-V survived longer than R65-infected animals, indicating that serine 346 in R65 HA contributes to virulence. These data suggest that evolution of H5 HPAIVs from low-pathogenic precursors, besides acquisition of a polybasic cleavage site, involves adaptation of neighbouring regions.</AbstractText>
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