Duck and Human Pandemic Influenza A Viruses Retain Sialidase Activity under Low pH Conditions
The majority of influenza A viruses isolated from wild birds, but not humans, can replicate in the duck intestinal tract. Here we demonstrate that all duck isolates tested universally retain sialidase activities under low pH conditions independent of their neu-raminidase (NA) subtypes. In contrast,...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 2001-08, Vol.130 (2), p.279-283 |
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| container_end_page | 283 |
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| container_title | Journal of biochemistry (Tokyo) |
| container_volume | 130 |
| creator | Takahashi, Tadanobu Suzuki, Yasuo Nishinaka, Daisuke Kawase, Nana Kobayashi, Yukiko Hindari, Kazuya I.-P.Jwa Miyamoto, Daisei Guo, Chan-Tan Shortridge, Kennedy F. Suzuki, Takashi |
| description | The majority of influenza A viruses isolated from wild birds, but not humans, can replicate in the duck intestinal tract. Here we demonstrate that all duck isolates tested universally retain sialidase activities under low pH conditions independent of their neu-raminidase (NA) subtypes. In contrast, the sialidase activities of most isolates from humans and pigs practically disappear below pH 4.5, with the exception of four human pandemic viruses isolated in 1957 and 1968. Sequence comparisons among duck, human, and swine N2 NA subtypes indicate that amino acids at positions 153, 253, 307, 329, 344, 347, 356, 368, 390, and 431 may be associated with the low pH stability of duck and human pandemic N2 NAs. This finding suggests that the low pH stability of duck influenza A virus NA may be a critical factor for replication in the intestinal tract through the digestive tract of ducks, and that the properties of NAs are important for understanding the epidemiology of the influenza virus. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a002983 |
| format | Article |
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Here we demonstrate that all duck isolates tested universally retain sialidase activities under low pH conditions independent of their neu-raminidase (NA) subtypes. In contrast, the sialidase activities of most isolates from humans and pigs practically disappear below pH 4.5, with the exception of four human pandemic viruses isolated in 1957 and 1968. Sequence comparisons among duck, human, and swine N2 NA subtypes indicate that amino acids at positions 153, 253, 307, 329, 344, 347, 356, 368, 390, and 431 may be associated with the low pH stability of duck and human pandemic N2 NAs. This finding suggests that the low pH stability of duck influenza A virus NA may be a critical factor for replication in the intestinal tract through the digestive tract of ducks, and that the properties of NAs are important for understanding the epidemiology of the influenza virus.</description><identifier>ISSN: 0021-924X</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a002983</identifier><identifier>PMID: 11481046</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Ducks ; Enzyme Stability ; Humans ; Hydrogen-Ion Concentration ; Influenza A virus - enzymology ; Influenza A virus - physiology ; influenza virus ; Influenza, Human - transmission ; Influenza, Human - virology ; neuraminidase ; Neuraminidase - metabolism ; pH stability ; Phylogeny ; Sequence Analysis ; sialidase ; Swine</subject><ispartof>Journal of biochemistry (Tokyo), 2001-08, Vol.130 (2), p.279-283</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c606t-2d905755d64976677cc527d391073ac279d73bd5b0359497ad8139fad9ca5efd3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11481046$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Takahashi, Tadanobu</creatorcontrib><creatorcontrib>Suzuki, Yasuo</creatorcontrib><creatorcontrib>Nishinaka, Daisuke</creatorcontrib><creatorcontrib>Kawase, Nana</creatorcontrib><creatorcontrib>Kobayashi, Yukiko</creatorcontrib><creatorcontrib>Hindari, Kazuya I.-P.Jwa</creatorcontrib><creatorcontrib>Miyamoto, Daisei</creatorcontrib><creatorcontrib>Guo, Chan-Tan</creatorcontrib><creatorcontrib>Shortridge, Kennedy F.</creatorcontrib><creatorcontrib>Suzuki, Takashi</creatorcontrib><title>Duck and Human Pandemic Influenza A Viruses Retain Sialidase Activity under Low pH Conditions</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>The majority of influenza A viruses isolated from wild birds, but not humans, can replicate in the duck intestinal tract. Here we demonstrate that all duck isolates tested universally retain sialidase activities under low pH conditions independent of their neu-raminidase (NA) subtypes. In contrast, the sialidase activities of most isolates from humans and pigs practically disappear below pH 4.5, with the exception of four human pandemic viruses isolated in 1957 and 1968. Sequence comparisons among duck, human, and swine N2 NA subtypes indicate that amino acids at positions 153, 253, 307, 329, 344, 347, 356, 368, 390, and 431 may be associated with the low pH stability of duck and human pandemic N2 NAs. This finding suggests that the low pH stability of duck influenza A virus NA may be a critical factor for replication in the intestinal tract through the digestive tract of ducks, and that the properties of NAs are important for understanding the epidemiology of the influenza virus.</description><subject>Animals</subject><subject>Ducks</subject><subject>Enzyme Stability</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>Influenza A virus - enzymology</subject><subject>Influenza A virus - physiology</subject><subject>influenza virus</subject><subject>Influenza, Human - transmission</subject><subject>Influenza, Human - virology</subject><subject>neuraminidase</subject><subject>Neuraminidase - metabolism</subject><subject>pH stability</subject><subject>Phylogeny</subject><subject>Sequence Analysis</subject><subject>sialidase</subject><subject>Swine</subject><issn>0021-924X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkM1uGyEURlkkan6aV4jYpLtxYBhgWHRh2W0d1VItN4miSBXCwCg4M-DA0CR9-o5lq1FWXXER57uXewC4wGiEkSCX4aUJ0axDjl61abRe6QfbjRRCpajJATgeClyIsro7AicprbfXkpAP4AjjqsaoYsfg1zTrR6i8gbPcKQ8XQ2k7p-GVb9ps_R8Fx_DWxZxsgkvbK-fhT6daZ1SycKx799v1rzAPqQjn4RluZnASvHG9Cz59BIfN8DN7tj9Pwc3XL9eTWTH_8e1qMp4XmiHWF6URiHJKDasEZ4xzrWnJDREYcaJ0yYXhZGXoChEqBkSZGhPRKCO0orYx5BR82vXdxPCUbepl55K2bau8DTlJPiwrKkr-C-K6woyyLfh5B-oYUoq2kZvoOhVfJUZyK1--ly938uVe_pA_3w_Kq86at_Te_AAUO8Cl3r78e1fxUTJOOJWzu3t5_70u6XQxlUvyF6aQmTQ</recordid><startdate>20010801</startdate><enddate>20010801</enddate><creator>Takahashi, Tadanobu</creator><creator>Suzuki, Yasuo</creator><creator>Nishinaka, Daisuke</creator><creator>Kawase, Nana</creator><creator>Kobayashi, Yukiko</creator><creator>Hindari, Kazuya I.-P.Jwa</creator><creator>Miyamoto, Daisei</creator><creator>Guo, Chan-Tan</creator><creator>Shortridge, Kennedy F.</creator><creator>Suzuki, Takashi</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20010801</creationdate><title>Duck and Human Pandemic Influenza A Viruses Retain Sialidase Activity under Low pH Conditions</title><author>Takahashi, Tadanobu ; Suzuki, Yasuo ; Nishinaka, Daisuke ; Kawase, Nana ; Kobayashi, Yukiko ; Hindari, Kazuya I.-P.Jwa ; Miyamoto, Daisei ; Guo, Chan-Tan ; Shortridge, Kennedy F. ; Suzuki, Takashi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c606t-2d905755d64976677cc527d391073ac279d73bd5b0359497ad8139fad9ca5efd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>Ducks</topic><topic>Enzyme Stability</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>Influenza A virus - enzymology</topic><topic>Influenza A virus - physiology</topic><topic>influenza virus</topic><topic>Influenza, Human - transmission</topic><topic>Influenza, Human - virology</topic><topic>neuraminidase</topic><topic>Neuraminidase - metabolism</topic><topic>pH stability</topic><topic>Phylogeny</topic><topic>Sequence Analysis</topic><topic>sialidase</topic><topic>Swine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Takahashi, Tadanobu</creatorcontrib><creatorcontrib>Suzuki, Yasuo</creatorcontrib><creatorcontrib>Nishinaka, Daisuke</creatorcontrib><creatorcontrib>Kawase, Nana</creatorcontrib><creatorcontrib>Kobayashi, Yukiko</creatorcontrib><creatorcontrib>Hindari, Kazuya I.-P.Jwa</creatorcontrib><creatorcontrib>Miyamoto, Daisei</creatorcontrib><creatorcontrib>Guo, Chan-Tan</creatorcontrib><creatorcontrib>Shortridge, Kennedy F.</creatorcontrib><creatorcontrib>Suzuki, Takashi</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Takahashi, Tadanobu</au><au>Suzuki, Yasuo</au><au>Nishinaka, Daisuke</au><au>Kawase, Nana</au><au>Kobayashi, Yukiko</au><au>Hindari, Kazuya I.-P.Jwa</au><au>Miyamoto, Daisei</au><au>Guo, Chan-Tan</au><au>Shortridge, Kennedy F.</au><au>Suzuki, Takashi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Duck and Human Pandemic Influenza A Viruses Retain Sialidase Activity under Low pH Conditions</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>2001-08-01</date><risdate>2001</risdate><volume>130</volume><issue>2</issue><spage>279</spage><epage>283</epage><pages>279-283</pages><issn>0021-924X</issn><abstract>The majority of influenza A viruses isolated from wild birds, but not humans, can replicate in the duck intestinal tract. Here we demonstrate that all duck isolates tested universally retain sialidase activities under low pH conditions independent of their neu-raminidase (NA) subtypes. In contrast, the sialidase activities of most isolates from humans and pigs practically disappear below pH 4.5, with the exception of four human pandemic viruses isolated in 1957 and 1968. Sequence comparisons among duck, human, and swine N2 NA subtypes indicate that amino acids at positions 153, 253, 307, 329, 344, 347, 356, 368, 390, and 431 may be associated with the low pH stability of duck and human pandemic N2 NAs. This finding suggests that the low pH stability of duck influenza A virus NA may be a critical factor for replication in the intestinal tract through the digestive tract of ducks, and that the properties of NAs are important for understanding the epidemiology of the influenza virus.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>11481046</pmid><doi>10.1093/oxfordjournals.jbchem.a002983</doi><tpages>5</tpages></addata></record> |
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| source | J-STAGE (Free - Japanese); MEDLINE; Oxford Journals Online; Free Full-Text Journals in Chemistry |
| subjects | Animals Ducks Enzyme Stability Humans Hydrogen-Ion Concentration Influenza A virus - enzymology Influenza A virus - physiology influenza virus Influenza, Human - transmission Influenza, Human - virology neuraminidase Neuraminidase - metabolism pH stability Phylogeny Sequence Analysis sialidase Swine |
| title | Duck and Human Pandemic Influenza A Viruses Retain Sialidase Activity under Low pH Conditions |
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