Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN
Intelectin is a recently described galactofuranose-binding lectin that plays a role in innate immunity in vertebrates. Little is known about intelectin in invertebrates, including amphioxus, the transitional form between vertebrates and invertebrates. We cloned an amphioxus intelectin homolog, Amphi...
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| Veröffentlicht in: | Fish & shellfish immunology 2012-07, Vol.33 (1), p.11-20 |
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| creator | Yan, Jie Wang, Jianfeng Zhao, Yaqi Zhang, Jingye Bai, Changcun Zhang, Changqing Zhang, Chao Li, Kailin Zhang, Haiqing Du, Xiumin Feng, Lijun |
| description | Intelectin is a recently described galactofuranose-binding lectin that plays a role in innate immunity in vertebrates. Little is known about intelectin in invertebrates, including amphioxus, the transitional form between vertebrates and invertebrates.
We cloned an amphioxus intelectin homolog, AmphiITLN-like, coding 302 amino acids with a conserved fibrinogen-related domain (FReD) in the N-terminus and an Intelectin domain in the C-terminus. In situ hybridization in adult amphioxus showed that AmphiITLN-like transcripts were highly expressed in the digestive tract and the skin. Quantitative real-time PCR revealed that AmphiITLN-like is significantly up-regulated in response to Staphylococcus aureus challenge, but only modestly to Escherichia coli. In addition, recombinant AmphiITLN-like expressed in E. coli agglutinates Gram-negative and Gram-positive bacteria to different degrees in a calcium dependent manner. Recombinant AmphiITLN-like could bind lipopolysaccharide (LPS) and peptidoglycan (PGN), the major cell wall components of Gram-negative and Gram-positive bacteria, respectively, with a higher affinity to PGN.
Our work identified and characterized for the first time an amphioxus intelectin homolog, and provided insight into the evolution and function of the intelectin family.
► One homolog of intelectin named AmphiITLN-like was identified in amphioxus. ► AmphiITLN-like transcripts were mainly expressed in digestive tract. ► The up-regulation of AmphiITLN-like occurred within 2–8 h after bacteria challenge. ► Recombinant AmphiITLN-like recognized PGN, LPS and induced bacterial agglutination. ► AmphiITLN-like recognizing PGN/Staphylococcus aureus more intensely than LPS/Escherichia coli was found. |
| doi_str_mv | 10.1016/j.fsi.2012.03.023 |
| format | Article |
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We cloned an amphioxus intelectin homolog, AmphiITLN-like, coding 302 amino acids with a conserved fibrinogen-related domain (FReD) in the N-terminus and an Intelectin domain in the C-terminus. In situ hybridization in adult amphioxus showed that AmphiITLN-like transcripts were highly expressed in the digestive tract and the skin. Quantitative real-time PCR revealed that AmphiITLN-like is significantly up-regulated in response to Staphylococcus aureus challenge, but only modestly to Escherichia coli. In addition, recombinant AmphiITLN-like expressed in E. coli agglutinates Gram-negative and Gram-positive bacteria to different degrees in a calcium dependent manner. Recombinant AmphiITLN-like could bind lipopolysaccharide (LPS) and peptidoglycan (PGN), the major cell wall components of Gram-negative and Gram-positive bacteria, respectively, with a higher affinity to PGN.
Our work identified and characterized for the first time an amphioxus intelectin homolog, and provided insight into the evolution and function of the intelectin family.
► One homolog of intelectin named AmphiITLN-like was identified in amphioxus. ► AmphiITLN-like transcripts were mainly expressed in digestive tract. ► The up-regulation of AmphiITLN-like occurred within 2–8 h after bacteria challenge. ► Recombinant AmphiITLN-like recognized PGN, LPS and induced bacterial agglutination. ► AmphiITLN-like recognizing PGN/Staphylococcus aureus more intensely than LPS/Escherichia coli was found.</description><identifier>ISSN: 1050-4648</identifier><identifier>EISSN: 1095-9947</identifier><identifier>DOI: 10.1016/j.fsi.2012.03.023</identifier><identifier>PMID: 22475783</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Agglutination ; Amino Acid Sequence ; Amphioxus ; Animals ; Anti-Bacterial Agents - pharmacology ; Bacterial agglutination ; Branchiostoma lanceolatum ; Calcium - metabolism ; Chordata - classification ; Chordata - genetics ; Chordata - metabolism ; Chordata - microbiology ; Escherichia coli ; Escherichia coli - drug effects ; Gram-Negative Bacteria - metabolism ; Gram-Positive Bacteria - metabolism ; Intelectin ; Lectins - genetics ; Lectins - metabolism ; Lipopolysaccharides - metabolism ; LPS ; Marine ; Molecular Sequence Data ; Peptidoglycan - metabolism ; PGN ; Phylogeny ; Protein Binding ; Recombinant Proteins - genetics ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - pharmacology ; Sequence Alignment ; Staphylococcus aureus ; Staphylococcus aureus - drug effects ; Up-Regulation</subject><ispartof>Fish & shellfish immunology, 2012-07, Vol.33 (1), p.11-20</ispartof><rights>2012 Elsevier Ltd</rights><rights>Copyright © 2012 Elsevier Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-879ade822a2e5937b2e0c5026039a8965044d1db4002a7d3b9f2f1893a9203e53</citedby><cites>FETCH-LOGICAL-c386t-879ade822a2e5937b2e0c5026039a8965044d1db4002a7d3b9f2f1893a9203e53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.fsi.2012.03.023$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22475783$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yan, Jie</creatorcontrib><creatorcontrib>Wang, Jianfeng</creatorcontrib><creatorcontrib>Zhao, Yaqi</creatorcontrib><creatorcontrib>Zhang, Jingye</creatorcontrib><creatorcontrib>Bai, Changcun</creatorcontrib><creatorcontrib>Zhang, Changqing</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Li, Kailin</creatorcontrib><creatorcontrib>Zhang, Haiqing</creatorcontrib><creatorcontrib>Du, Xiumin</creatorcontrib><creatorcontrib>Feng, Lijun</creatorcontrib><title>Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN</title><title>Fish & shellfish immunology</title><addtitle>Fish Shellfish Immunol</addtitle><description>Intelectin is a recently described galactofuranose-binding lectin that plays a role in innate immunity in vertebrates. Little is known about intelectin in invertebrates, including amphioxus, the transitional form between vertebrates and invertebrates.
We cloned an amphioxus intelectin homolog, AmphiITLN-like, coding 302 amino acids with a conserved fibrinogen-related domain (FReD) in the N-terminus and an Intelectin domain in the C-terminus. In situ hybridization in adult amphioxus showed that AmphiITLN-like transcripts were highly expressed in the digestive tract and the skin. Quantitative real-time PCR revealed that AmphiITLN-like is significantly up-regulated in response to Staphylococcus aureus challenge, but only modestly to Escherichia coli. In addition, recombinant AmphiITLN-like expressed in E. coli agglutinates Gram-negative and Gram-positive bacteria to different degrees in a calcium dependent manner. Recombinant AmphiITLN-like could bind lipopolysaccharide (LPS) and peptidoglycan (PGN), the major cell wall components of Gram-negative and Gram-positive bacteria, respectively, with a higher affinity to PGN.
Our work identified and characterized for the first time an amphioxus intelectin homolog, and provided insight into the evolution and function of the intelectin family.
► One homolog of intelectin named AmphiITLN-like was identified in amphioxus. ► AmphiITLN-like transcripts were mainly expressed in digestive tract. ► The up-regulation of AmphiITLN-like occurred within 2–8 h after bacteria challenge. ► Recombinant AmphiITLN-like recognized PGN, LPS and induced bacterial agglutination. ► AmphiITLN-like recognizing PGN/Staphylococcus aureus more intensely than LPS/Escherichia coli was found.</description><subject>Agglutination</subject><subject>Amino Acid Sequence</subject><subject>Amphioxus</subject><subject>Animals</subject><subject>Anti-Bacterial Agents - pharmacology</subject><subject>Bacterial agglutination</subject><subject>Branchiostoma lanceolatum</subject><subject>Calcium - metabolism</subject><subject>Chordata - classification</subject><subject>Chordata - genetics</subject><subject>Chordata - metabolism</subject><subject>Chordata - microbiology</subject><subject>Escherichia coli</subject><subject>Escherichia coli - drug effects</subject><subject>Gram-Negative Bacteria - metabolism</subject><subject>Gram-Positive Bacteria - metabolism</subject><subject>Intelectin</subject><subject>Lectins - genetics</subject><subject>Lectins - metabolism</subject><subject>Lipopolysaccharides - metabolism</subject><subject>LPS</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Peptidoglycan - metabolism</subject><subject>PGN</subject><subject>Phylogeny</subject><subject>Protein Binding</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Sequence Alignment</subject><subject>Staphylococcus aureus</subject><subject>Staphylococcus aureus - drug effects</subject><subject>Up-Regulation</subject><issn>1050-4648</issn><issn>1095-9947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc9u1DAQxiMEoqXwAFyQj1wSxnb-ihOqSqm0gkrAOZrYk6yXJA62s2LfikfEYQtHxGlGM7_v02i-JHnJIePAyzeHrPcmE8BFBjIDIR8llxyaIm2avHq89QWkeZnXF8kz7w8AUMoSniYXQuRVUdXyMvl5p2kOpjcKg7Ezsz3DmeG07I39sXpm5kAjqWBmtreTHe3Awh4DWxz15LAbTwyHYVwjgIE8GxxO6WK9CeZIzB7JnUczDfh71KEK5Ayy0XyjqNYrsWCZNn30i6ewzszazANTuKAy4bRtd_ef41ma3d9-fJ486XH09OKhXiVf3998uf6Q7j7d3l2_26VK1mVI66pBTbUQKKhoZNUJAlWAKEE2WDdlAXmuue5yAIGVll3Ti57XjcRGgKRCXiWvz76Ls99X8qGdjFc0jjiTXX3LQUCd55KX_4HyquQFFBvKz6hy1vv4w3ZxZkJ3itDGle2hjZm2W6YtyDZmGjWvHuzXbiL9V_EnxAi8PQMU_3E05FqvDM2KtHExulZb8w_7X_ZltFU</recordid><startdate>20120701</startdate><enddate>20120701</enddate><creator>Yan, Jie</creator><creator>Wang, Jianfeng</creator><creator>Zhao, Yaqi</creator><creator>Zhang, Jingye</creator><creator>Bai, Changcun</creator><creator>Zhang, Changqing</creator><creator>Zhang, Chao</creator><creator>Li, Kailin</creator><creator>Zhang, Haiqing</creator><creator>Du, Xiumin</creator><creator>Feng, Lijun</creator><general>Elsevier Ltd</general><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>7X8</scope><scope>7QL</scope><scope>7T5</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H94</scope><scope>H95</scope><scope>H98</scope><scope>L.G</scope><scope>P64</scope></search><sort><creationdate>20120701</creationdate><title>Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN</title><author>Yan, Jie ; Wang, Jianfeng ; Zhao, Yaqi ; Zhang, Jingye ; Bai, Changcun ; Zhang, Changqing ; Zhang, Chao ; Li, Kailin ; Zhang, Haiqing ; Du, Xiumin ; Feng, Lijun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-879ade822a2e5937b2e0c5026039a8965044d1db4002a7d3b9f2f1893a9203e53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Agglutination</topic><topic>Amino Acid Sequence</topic><topic>Amphioxus</topic><topic>Animals</topic><topic>Anti-Bacterial Agents - pharmacology</topic><topic>Bacterial agglutination</topic><topic>Branchiostoma lanceolatum</topic><topic>Calcium - metabolism</topic><topic>Chordata - classification</topic><topic>Chordata - genetics</topic><topic>Chordata - metabolism</topic><topic>Chordata - microbiology</topic><topic>Escherichia coli</topic><topic>Escherichia coli - drug effects</topic><topic>Gram-Negative Bacteria - metabolism</topic><topic>Gram-Positive Bacteria - metabolism</topic><topic>Intelectin</topic><topic>Lectins - genetics</topic><topic>Lectins - metabolism</topic><topic>Lipopolysaccharides - metabolism</topic><topic>LPS</topic><topic>Marine</topic><topic>Molecular Sequence Data</topic><topic>Peptidoglycan - metabolism</topic><topic>PGN</topic><topic>Phylogeny</topic><topic>Protein Binding</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - pharmacology</topic><topic>Sequence Alignment</topic><topic>Staphylococcus aureus</topic><topic>Staphylococcus aureus - drug effects</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yan, Jie</creatorcontrib><creatorcontrib>Wang, Jianfeng</creatorcontrib><creatorcontrib>Zhao, Yaqi</creatorcontrib><creatorcontrib>Zhang, Jingye</creatorcontrib><creatorcontrib>Bai, Changcun</creatorcontrib><creatorcontrib>Zhang, Changqing</creatorcontrib><creatorcontrib>Zhang, Chao</creatorcontrib><creatorcontrib>Li, Kailin</creatorcontrib><creatorcontrib>Zhang, Haiqing</creatorcontrib><creatorcontrib>Du, Xiumin</creatorcontrib><creatorcontrib>Feng, Lijun</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Aquaculture Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Fish & shellfish immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yan, Jie</au><au>Wang, Jianfeng</au><au>Zhao, Yaqi</au><au>Zhang, Jingye</au><au>Bai, Changcun</au><au>Zhang, Changqing</au><au>Zhang, Chao</au><au>Li, Kailin</au><au>Zhang, Haiqing</au><au>Du, Xiumin</au><au>Feng, Lijun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN</atitle><jtitle>Fish & shellfish immunology</jtitle><addtitle>Fish Shellfish Immunol</addtitle><date>2012-07-01</date><risdate>2012</risdate><volume>33</volume><issue>1</issue><spage>11</spage><epage>20</epage><pages>11-20</pages><issn>1050-4648</issn><eissn>1095-9947</eissn><abstract>Intelectin is a recently described galactofuranose-binding lectin that plays a role in innate immunity in vertebrates. Little is known about intelectin in invertebrates, including amphioxus, the transitional form between vertebrates and invertebrates.
We cloned an amphioxus intelectin homolog, AmphiITLN-like, coding 302 amino acids with a conserved fibrinogen-related domain (FReD) in the N-terminus and an Intelectin domain in the C-terminus. In situ hybridization in adult amphioxus showed that AmphiITLN-like transcripts were highly expressed in the digestive tract and the skin. Quantitative real-time PCR revealed that AmphiITLN-like is significantly up-regulated in response to Staphylococcus aureus challenge, but only modestly to Escherichia coli. In addition, recombinant AmphiITLN-like expressed in E. coli agglutinates Gram-negative and Gram-positive bacteria to different degrees in a calcium dependent manner. Recombinant AmphiITLN-like could bind lipopolysaccharide (LPS) and peptidoglycan (PGN), the major cell wall components of Gram-negative and Gram-positive bacteria, respectively, with a higher affinity to PGN.
Our work identified and characterized for the first time an amphioxus intelectin homolog, and provided insight into the evolution and function of the intelectin family.
► One homolog of intelectin named AmphiITLN-like was identified in amphioxus. ► AmphiITLN-like transcripts were mainly expressed in digestive tract. ► The up-regulation of AmphiITLN-like occurred within 2–8 h after bacteria challenge. ► Recombinant AmphiITLN-like recognized PGN, LPS and induced bacterial agglutination. ► AmphiITLN-like recognizing PGN/Staphylococcus aureus more intensely than LPS/Escherichia coli was found.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>22475783</pmid><doi>10.1016/j.fsi.2012.03.023</doi><tpages>10</tpages></addata></record> |
| fulltext | fulltext |
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| ispartof | Fish & shellfish immunology, 2012-07, Vol.33 (1), p.11-20 |
| issn | 1050-4648 1095-9947 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Agglutination Amino Acid Sequence Amphioxus Animals Anti-Bacterial Agents - pharmacology Bacterial agglutination Branchiostoma lanceolatum Calcium - metabolism Chordata - classification Chordata - genetics Chordata - metabolism Chordata - microbiology Escherichia coli Escherichia coli - drug effects Gram-Negative Bacteria - metabolism Gram-Positive Bacteria - metabolism Intelectin Lectins - genetics Lectins - metabolism Lipopolysaccharides - metabolism LPS Marine Molecular Sequence Data Peptidoglycan - metabolism PGN Phylogeny Protein Binding Recombinant Proteins - genetics Recombinant Proteins - isolation & purification Recombinant Proteins - pharmacology Sequence Alignment Staphylococcus aureus Staphylococcus aureus - drug effects Up-Regulation |
| title | Identification of an amphioxus intelectin homolog that preferably agglutinates gram-positive over gram-negative bacteria likely due to different binding capacity to LPS and PGN |
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