Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin
Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA t...
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| Veröffentlicht in: | Cell research 2020-07, Vol.30 (7), p.602-609 |
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| creator | Wang, Yuxin Wang, Guopeng Li, Yaxin Zhu, Qinyu Shen, Hao Gao, Ning Xiao, Junyu |
| description | Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. How the J-chain and pIgR/SC facilitate the assembly and secretion of SIgA remains incompletely understood. Furthermore, during the infection of
Streptococcus pneumoniae
, the pneumococcal adhesin SpsA hijacks pIgR/SC and SIgA to gain entry to human cells and evade host defense. How SpsA targets pIgR/SC and SIgA also remains elusive. Here we report a cryo-electron microscopy structure of the Fc region of IgA1 (Fcα) in complex with the J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present a structure of Fcα-J-SC complexed with SpsA, which uncovers the specific interactions between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on
S. pneumoniae
pathogenesis. |
| doi_str_mv | 10.1038/s41422-020-0336-3 |
| format | Article |
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Streptococcus pneumoniae
, the pneumococcal adhesin SpsA hijacks pIgR/SC and SIgA to gain entry to human cells and evade host defense. How SpsA targets pIgR/SC and SIgA also remains elusive. Here we report a cryo-electron microscopy structure of the Fc region of IgA1 (Fcα) in complex with the J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present a structure of Fcα-J-SC complexed with SpsA, which uncovers the specific interactions between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on
S. pneumoniae
pathogenesis.</description><identifier>ISSN: 1001-0602</identifier><identifier>EISSN: 1748-7838</identifier><identifier>DOI: 10.1038/s41422-020-0336-3</identifier><identifier>PMID: 32398862</identifier><language>eng</language><publisher>Singapore: Springer Singapore</publisher><subject>101/28 ; 631/250 ; 631/535/1258/1259 ; Antibodies ; Biomedical and Life Sciences ; Cell Biology ; Electron microscopy ; Immunoglobulin A ; Immunoglobulins ; Life Sciences ; Mucosa ; Pathogenesis ; Secretory component ; Streptococcus infections ; Streptococcus pneumoniae</subject><ispartof>Cell research, 2020-07, Vol.30 (7), p.602-609</ispartof><rights>Center for Excellence in Molecular Cell Science, CAS 2020</rights><rights>Center for Excellence in Molecular Cell Science, CAS 2020.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c470t-64901b950a9939672a618616e820875abbb491c08059f9eaa8646e5e185d6cf13</citedby><cites>FETCH-LOGICAL-c470t-64901b950a9939672a618616e820875abbb491c08059f9eaa8646e5e185d6cf13</cites><orcidid>0000-0003-3067-9993 ; 0000-0003-1822-1701 ; 0000-0002-4490-3995</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7343866/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7343866/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32398862$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Yuxin</creatorcontrib><creatorcontrib>Wang, Guopeng</creatorcontrib><creatorcontrib>Li, Yaxin</creatorcontrib><creatorcontrib>Zhu, Qinyu</creatorcontrib><creatorcontrib>Shen, Hao</creatorcontrib><creatorcontrib>Gao, Ning</creatorcontrib><creatorcontrib>Xiao, Junyu</creatorcontrib><title>Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin</title><title>Cell research</title><addtitle>Cell Res</addtitle><addtitle>Cell Res</addtitle><description>Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. How the J-chain and pIgR/SC facilitate the assembly and secretion of SIgA remains incompletely understood. Furthermore, during the infection of
Streptococcus pneumoniae
, the pneumococcal adhesin SpsA hijacks pIgR/SC and SIgA to gain entry to human cells and evade host defense. How SpsA targets pIgR/SC and SIgA also remains elusive. Here we report a cryo-electron microscopy structure of the Fc region of IgA1 (Fcα) in complex with the J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present a structure of Fcα-J-SC complexed with SpsA, which uncovers the specific interactions between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on
S. pneumoniae
pathogenesis.</description><subject>101/28</subject><subject>631/250</subject><subject>631/535/1258/1259</subject><subject>Antibodies</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Electron microscopy</subject><subject>Immunoglobulin A</subject><subject>Immunoglobulins</subject><subject>Life Sciences</subject><subject>Mucosa</subject><subject>Pathogenesis</subject><subject>Secretory component</subject><subject>Streptococcus infections</subject><subject>Streptococcus pneumoniae</subject><issn>1001-0602</issn><issn>1748-7838</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kcuLFDEQxsOiuC__AC9LwIuX1sqj08lFWAZdhQUP6jmkM5mZLN3JmMfK_vdm6H24gqcqqF99VR8fQm8IvCfA5IfMCae0AwodMCY6doROyMBlN0gmX7QegHQggB6j05xvAGjPe_IKHTPKlJSCniD7vaRqS01mwj5kv92V3JoScXY2uRLTHfbzXEPcTnGskw_4Epuwxn7hXDK2-Bjwb1922OB9cHWONlrbBM1657IP5-jlxkzZvb6vZ-jn508_Vl-6629XX1eX153lA5ROcAVkVD0YpZgSAzWCSEGEkxTk0JtxHLkiFiT0aqOcMVJw4XpHZL8WdkPYGfq46O7rOLu1daE0W3qf_GzSnY7G6-eT4Hd6G2_1wDiTQjSBd_cCKf6qLhc9-2zdNJngYs2acqCcMSoOt97-g97EmkKz1yhKGkZ6aBRZKJtizsltHp8hoA8R6iVC3SLUhwg1azsXf7t43HjIrAF0AXIbha1LT6f_r_oHOQSnxA</recordid><startdate>20200701</startdate><enddate>20200701</enddate><creator>Wang, Yuxin</creator><creator>Wang, Guopeng</creator><creator>Li, Yaxin</creator><creator>Zhu, Qinyu</creator><creator>Shen, Hao</creator><creator>Gao, Ning</creator><creator>Xiao, Junyu</creator><general>Springer Singapore</general><general>Nature Publishing Group</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-3067-9993</orcidid><orcidid>https://orcid.org/0000-0003-1822-1701</orcidid><orcidid>https://orcid.org/0000-0002-4490-3995</orcidid></search><sort><creationdate>20200701</creationdate><title>Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin</title><author>Wang, Yuxin ; Wang, Guopeng ; Li, Yaxin ; Zhu, Qinyu ; Shen, Hao ; Gao, Ning ; Xiao, Junyu</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c470t-64901b950a9939672a618616e820875abbb491c08059f9eaa8646e5e185d6cf13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>101/28</topic><topic>631/250</topic><topic>631/535/1258/1259</topic><topic>Antibodies</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Electron microscopy</topic><topic>Immunoglobulin A</topic><topic>Immunoglobulins</topic><topic>Life Sciences</topic><topic>Mucosa</topic><topic>Pathogenesis</topic><topic>Secretory component</topic><topic>Streptococcus infections</topic><topic>Streptococcus pneumoniae</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Yuxin</creatorcontrib><creatorcontrib>Wang, Guopeng</creatorcontrib><creatorcontrib>Li, Yaxin</creatorcontrib><creatorcontrib>Zhu, Qinyu</creatorcontrib><creatorcontrib>Shen, Hao</creatorcontrib><creatorcontrib>Gao, Ning</creatorcontrib><creatorcontrib>Xiao, Junyu</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Yuxin</au><au>Wang, Guopeng</au><au>Li, Yaxin</au><au>Zhu, Qinyu</au><au>Shen, Hao</au><au>Gao, Ning</au><au>Xiao, Junyu</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin</atitle><jtitle>Cell research</jtitle><stitle>Cell Res</stitle><addtitle>Cell Res</addtitle><date>2020-07-01</date><risdate>2020</risdate><volume>30</volume><issue>7</issue><spage>602</spage><epage>609</epage><pages>602-609</pages><issn>1001-0602</issn><eissn>1748-7838</eissn><abstract>Secretory Immunoglobulin A (SIgA) is the most abundant antibody at the mucosal surface. It possesses two additional subunits besides IgA: the joining chain (J-chain) and secretory component (SC). SC is the ectodomain of the polymeric immunoglobulin receptor (pIgR), which functions to transport IgA to the mucosa. How the J-chain and pIgR/SC facilitate the assembly and secretion of SIgA remains incompletely understood. Furthermore, during the infection of
Streptococcus pneumoniae
, the pneumococcal adhesin SpsA hijacks pIgR/SC and SIgA to gain entry to human cells and evade host defense. How SpsA targets pIgR/SC and SIgA also remains elusive. Here we report a cryo-electron microscopy structure of the Fc region of IgA1 (Fcα) in complex with the J-chain and SC (Fcα-J-SC), which reveals the organization principle of SIgA. We also present a structure of Fcα-J-SC complexed with SpsA, which uncovers the specific interactions between SpsA and human pIgR/SC. These results advance the molecular understanding of SIgA and shed light on
S. pneumoniae
pathogenesis.</abstract><cop>Singapore</cop><pub>Springer Singapore</pub><pmid>32398862</pmid><doi>10.1038/s41422-020-0336-3</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0003-3067-9993</orcidid><orcidid>https://orcid.org/0000-0003-1822-1701</orcidid><orcidid>https://orcid.org/0000-0002-4490-3995</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; SpringerLink Journals - AutoHoldings |
| subjects | 101/28 631/250 631/535/1258/1259 Antibodies Biomedical and Life Sciences Cell Biology Electron microscopy Immunoglobulin A Immunoglobulins Life Sciences Mucosa Pathogenesis Secretory component Streptococcus infections Streptococcus pneumoniae |
| title | Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin |
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