Identification of sequence mutations affecting hemagglutinin specificity to sialic acid receptor in influenza A virus subtypes
Identifieur interne : 000082 ( 1957/Analysis ); précédent : 000081; suivant : 000083Identification of sequence mutations affecting hemagglutinin specificity to sialic acid receptor in influenza A virus subtypes
Auteurs : Usman Sumo Friend TambunanSource :
- Bioinformation [ 0973-2063 ] ; 2010.
Abstract
The attachment of the hemagglutinin protein of the H1N1 subtype of the pandemic influenza A virus to the sialic acid receptor Sia(α2-6)Gal has contributed to the ability of the virus to replicate in the human body and transmit among humans. In view of the pandemic caused by the replication and transmission of the H1N1 virus, more studies on the specificity of hemagglutinin towards sialic acid and how it affects the replication and transmission ability of this virus among humans are needed. In this study, we have applied sequence, structural and functional analyses to the hemagglutinin protein of the pandemic H1N1 virus, with the aim of identifying amino acid mutation patterns that affect its specificity to sialic acid. We have also employed a molecular docking method to evaluate the complex formed between hemagglutinin protein and the sialic acid receptor. Based on our results, we suggest two possible mutation patterns, namely (1) positions 190 and 225 from glutamic acid and glycine to aspartic acid (E190D in A/Brevig Mission/1/18 (H1N1), A/New York/1/18(H1N1) and A/South Carolina/1/1918(H1N1) and G225D in A/South Carolina/1/1918(H1N1), A/South Carolina/1/1918(H1N1), and A/Puerto Rico/8/34(H1N1)), and (2) positions 226 and 228 from glutamine and glycine to leucine and serine, respectively (Q226L and G228S in A/Guiyang/1/1957(H2N2), A/Kayano/57(H2N2), A/Aichi/2/1968(H3N2), A/Hong Kong/1/1968(H3N2) and A/Memphis/1/68(H3N2)) that can potentially contribute to the specificity of hemagglutinin to Sia(α2-6)Gal, thereby enabling the replication and transmission of virus within and among humans.
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PubMed: 21364825
PubMed Central: 3055699
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contributed to the ability of the virus to replicate in the human body and transmit among humans. In view of the pandemic caused by the replication and
transmission of the H1N1 virus, more studies on the specificity of hemagglutinin towards sialic acid and how it affects the replication and transmission
ability of this virus among humans are needed. In this study, we have applied sequence, structural and functional analyses to the hemagglutinin protein of
the pandemic H1N1 virus, with the aim of identifying amino acid mutation patterns that affect its specificity to sialic acid. We have also employed a
molecular docking method to evaluate the complex formed between hemagglutinin protein and the sialic acid receptor. Based on our results, we suggest
two possible mutation patterns, namely (1) positions 190 and 225 from glutamic acid and glycine to aspartic acid (E190D in A/Brevig Mission/1/18 (H1N1),
A/New York/1/18(H1N1) and A/South Carolina/1/1918(H1N1) and G225D in A/South Carolina/1/1918(H1N1), A/South Carolina/1/1918(H1N1), and
A/Puerto Rico/8/34(H1N1)), and (2) positions 226 and 228 from glutamine and glycine to leucine and serine, respectively (Q226L and G228S in
A/Guiyang/1/1957(H2N2), A/Kayano/57(H2N2), A/Aichi/2/1968(H3N2), A/Hong Kong/1/1968(H3N2) and A/Memphis/1/68(H3N2)) that can potentially
contribute to the specificity of hemagglutinin to Sia(α2-6)Gal, thereby enabling the replication and transmission of virus within and among humans.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Subbarao, K" uniqKey="Subbarao K">k Subbarao</name></author><author><name sortKey="Ross, Lg" uniqKey="Ross L">LG Ross</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Webster, Rg" uniqKey="Webster R">RG Webster</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Kilbourne, Ed" uniqKey="Kilbourne E">ED Kilbourne</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ungchusak" uniqKey="Ungchusak">Ungchusak</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Neumann, G" uniqKey="Neumann G">G Neumann</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Noah, Dl" uniqKey="Noah D">DL Noah</name></author><author><name sortKey="Krug, Rm" uniqKey="Krug R">RM Krug</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Li, M" uniqKey="Li M">M Li</name></author><author><name sortKey="Wang, B" uniqKey="Wang B">B Wang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Miotto, O" uniqKey="Miotto O">O Miotto</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tumpey, Tm" uniqKey="Tumpey T">TM Tumpey</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gambaryan, A" uniqKey="Gambaryan A">A Gambaryan</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Larkin, Ma" uniqKey="Larkin M">MA Larkin</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Pedretti, A" uniqKey="Pedretti A">A Pedretti</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gibrat, Jf" uniqKey="Gibrat J">JF Gibrat</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Glaser" uniqKey="Glaser">Glaser</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Tambunan, Usman Sumo Friend" sort="Tambunan, Usman Sumo Friend" uniqKey="Tambunan U" first="Usman Sumo Friend" last="Tambunan">Usman Sumo Friend Tambunan</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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