Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori
C‐type lectins (CTLs) play a variety of roles in plants and animals. They are involved in animal development, pathogen recognition, and the activation of immune responses. CTLs carry one or more non‐catalytic carbohydrate‐recognition domains (CRDs) to bind specific carbohydrates reversibly. Here, we...
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| Veröffentlicht in: | Archives of insect biochemistry and physiology 2017-07, Vol.95 (3), p.n/a |
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| container_title | Archives of insect biochemistry and physiology |
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| creator | Shahzad, Toufeeq Zhan, Ming‐Yue Yang, Pei‐Jin Yu, Xiao‐Qiang Rao, Xiang‐Jun |
| description | C‐type lectins (CTLs) play a variety of roles in plants and animals. They are involved in animal development, pathogen recognition, and the activation of immune responses. CTLs carry one or more non‐catalytic carbohydrate‐recognition domains (CRDs) to bind specific carbohydrates reversibly. Here, we report the molecular cloning and functional analysis of a single‐CRD CTL, named C‐type lectin‐S2 (BmCTL‐S2) from the domesticated silkmoth Bombyx mori (Lepidoptera: Bombycidae). The ORF of CTL‐S2 is 666 bp, which encodes a putative protein of 221 amino acids. BmCTL‐S2 is expressed in a variety of immune‐related tissues, including hemocytes and fat body among others. BmCTL‐S2 mRNA level in the midgut and the fat body was significantly increased by bacterial challenges. The recombinant protein (rBmCTL‐S2) bound different bacterial cell wall components and bacterial cells. rBmCTL‐S2 also inhibited the growth of Bacillus subtilis and Staphylococcus aureus. Taken together, we infer that BmCTL‐S2 is a pattern‐recognition receptor with antibacterial activities. |
| doi_str_mv | 10.1002/arch.21391 |
| format | Article |
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They are involved in animal development, pathogen recognition, and the activation of immune responses. CTLs carry one or more non‐catalytic carbohydrate‐recognition domains (CRDs) to bind specific carbohydrates reversibly. Here, we report the molecular cloning and functional analysis of a single‐CRD CTL, named C‐type lectin‐S2 (BmCTL‐S2) from the domesticated silkmoth Bombyx mori (Lepidoptera: Bombycidae). The ORF of CTL‐S2 is 666 bp, which encodes a putative protein of 221 amino acids. BmCTL‐S2 is expressed in a variety of immune‐related tissues, including hemocytes and fat body among others. BmCTL‐S2 mRNA level in the midgut and the fat body was significantly increased by bacterial challenges. The recombinant protein (rBmCTL‐S2) bound different bacterial cell wall components and bacterial cells. rBmCTL‐S2 also inhibited the growth of Bacillus subtilis and Staphylococcus aureus. Taken together, we infer that BmCTL‐S2 is a pattern‐recognition receptor with antibacterial activities.</description><identifier>ISSN: 0739-4462</identifier><identifier>EISSN: 1520-6327</identifier><identifier>DOI: 10.1002/arch.21391</identifier><identifier>PMID: 28618068</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Activation ; Amino Acid Sequence ; Amino acids ; Animals ; Bacillus subtilis ; Base Sequence ; Bombyx - genetics ; Bombyx - immunology ; Bombyx - metabolism ; Bombyx mori ; Carbohydrates ; Catalysis ; Cell walls ; Cloning ; C‐type lectin ; Fat body ; Fat Body - metabolism ; Functional analysis ; Hemocytes ; Immune response ; insect immunity ; Insect Proteins - isolation & purification ; Insect Proteins - physiology ; Larva - immunology ; Larva - metabolism ; Lectins ; Lectins, C-Type - isolation & purification ; Lectins, C-Type - physiology ; Microbial Sensitivity Tests ; Midgut ; mRNA ; Pathogen-Associated Molecular Pattern Molecules - metabolism ; Pathogens ; Pattern recognition ; Sequence Analysis, DNA ; silkworm ; Staphylococcus aureus ; Tissues</subject><ispartof>Archives of insect biochemistry and physiology, 2017-07, Vol.95 (3), p.n/a</ispartof><rights>2017 Wiley Periodicals, Inc.</rights><rights>Copyright © 2017 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3571-548715710125faabb12e8e6e7756a75cca1e6f0f83ba3a6c5b02ba2f9c8b623d3</citedby><cites>FETCH-LOGICAL-c3571-548715710125faabb12e8e6e7756a75cca1e6f0f83ba3a6c5b02ba2f9c8b623d3</cites><orcidid>0000-0002-3591-6698</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Farch.21391$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Farch.21391$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,27926,27927,45576,45577</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28618068$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shahzad, Toufeeq</creatorcontrib><creatorcontrib>Zhan, Ming‐Yue</creatorcontrib><creatorcontrib>Yang, Pei‐Jin</creatorcontrib><creatorcontrib>Yu, Xiao‐Qiang</creatorcontrib><creatorcontrib>Rao, Xiang‐Jun</creatorcontrib><title>Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori</title><title>Archives of insect biochemistry and physiology</title><addtitle>Arch Insect Biochem Physiol</addtitle><description>C‐type lectins (CTLs) play a variety of roles in plants and animals. They are involved in animal development, pathogen recognition, and the activation of immune responses. CTLs carry one or more non‐catalytic carbohydrate‐recognition domains (CRDs) to bind specific carbohydrates reversibly. Here, we report the molecular cloning and functional analysis of a single‐CRD CTL, named C‐type lectin‐S2 (BmCTL‐S2) from the domesticated silkmoth Bombyx mori (Lepidoptera: Bombycidae). The ORF of CTL‐S2 is 666 bp, which encodes a putative protein of 221 amino acids. BmCTL‐S2 is expressed in a variety of immune‐related tissues, including hemocytes and fat body among others. BmCTL‐S2 mRNA level in the midgut and the fat body was significantly increased by bacterial challenges. The recombinant protein (rBmCTL‐S2) bound different bacterial cell wall components and bacterial cells. rBmCTL‐S2 also inhibited the growth of Bacillus subtilis and Staphylococcus aureus. Taken together, we infer that BmCTL‐S2 is a pattern‐recognition receptor with antibacterial activities.</description><subject>Activation</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Bacillus subtilis</subject><subject>Base Sequence</subject><subject>Bombyx - genetics</subject><subject>Bombyx - immunology</subject><subject>Bombyx - metabolism</subject><subject>Bombyx mori</subject><subject>Carbohydrates</subject><subject>Catalysis</subject><subject>Cell walls</subject><subject>Cloning</subject><subject>C‐type lectin</subject><subject>Fat body</subject><subject>Fat Body - metabolism</subject><subject>Functional analysis</subject><subject>Hemocytes</subject><subject>Immune response</subject><subject>insect immunity</subject><subject>Insect Proteins - isolation & purification</subject><subject>Insect Proteins - physiology</subject><subject>Larva - immunology</subject><subject>Larva - metabolism</subject><subject>Lectins</subject><subject>Lectins, C-Type - isolation & purification</subject><subject>Lectins, C-Type - physiology</subject><subject>Microbial Sensitivity Tests</subject><subject>Midgut</subject><subject>mRNA</subject><subject>Pathogen-Associated Molecular Pattern Molecules - metabolism</subject><subject>Pathogens</subject><subject>Pattern recognition</subject><subject>Sequence Analysis, DNA</subject><subject>silkworm</subject><subject>Staphylococcus aureus</subject><subject>Tissues</subject><issn>0739-4462</issn><issn>1520-6327</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90E9LwzAYBvAgipvTix9AAl5E6MyfJmmPs6gTNgTRc0mzVDvTZiYrszc_gp_RT2K2qQcPHl7e9_DjgfcB4BijIUaIXEinnocE0xTvgD5mBEWcErEL-kjQNIpjTnrgwPs5QijlONkHPZKEjXjSB9OpNVq1RjqojG2q5gnKZhZGms5XHtoSSph9vn8su4WGgS6rBpbO1tBX5mVlXQ0vbV10b7C2rjoEe6U0Xh997wF4vL56yMbR5O7mNhtNIkWZwBGLE4HDgTBhpZRFgYlONNdCMC4FU0pizUtUJrSQVHLFCkQKScpUJQUndEYH4Gybu3D2tdV-mdeVV9oY2Wjb-hynGIk0JigN9PQPndvWhfc2igoS84QFdb5VylnvnS7zhatq6boco3xdcr4uOd-UHPDJd2Rb1Hr2S39aDQBvwaoyuvsnKh_dZ-Nt6BcEtIbH</recordid><startdate>201707</startdate><enddate>201707</enddate><creator>Shahzad, Toufeeq</creator><creator>Zhan, Ming‐Yue</creator><creator>Yang, Pei‐Jin</creator><creator>Yu, Xiao‐Qiang</creator><creator>Rao, Xiang‐Jun</creator><general>Wiley Subscription Services, Inc</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>7QR</scope><scope>7SS</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3591-6698</orcidid></search><sort><creationdate>201707</creationdate><title>Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori</title><author>Shahzad, Toufeeq ; Zhan, Ming‐Yue ; Yang, Pei‐Jin ; Yu, Xiao‐Qiang ; Rao, Xiang‐Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3571-548715710125faabb12e8e6e7756a75cca1e6f0f83ba3a6c5b02ba2f9c8b623d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Activation</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Bacillus subtilis</topic><topic>Base Sequence</topic><topic>Bombyx - genetics</topic><topic>Bombyx - immunology</topic><topic>Bombyx - metabolism</topic><topic>Bombyx mori</topic><topic>Carbohydrates</topic><topic>Catalysis</topic><topic>Cell walls</topic><topic>Cloning</topic><topic>C‐type lectin</topic><topic>Fat body</topic><topic>Fat Body - metabolism</topic><topic>Functional analysis</topic><topic>Hemocytes</topic><topic>Immune response</topic><topic>insect immunity</topic><topic>Insect Proteins - isolation & purification</topic><topic>Insect Proteins - physiology</topic><topic>Larva - immunology</topic><topic>Larva - metabolism</topic><topic>Lectins</topic><topic>Lectins, C-Type - isolation & purification</topic><topic>Lectins, C-Type - physiology</topic><topic>Microbial Sensitivity Tests</topic><topic>Midgut</topic><topic>mRNA</topic><topic>Pathogen-Associated Molecular Pattern Molecules - metabolism</topic><topic>Pathogens</topic><topic>Pattern recognition</topic><topic>Sequence Analysis, DNA</topic><topic>silkworm</topic><topic>Staphylococcus aureus</topic><topic>Tissues</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shahzad, Toufeeq</creatorcontrib><creatorcontrib>Zhan, Ming‐Yue</creatorcontrib><creatorcontrib>Yang, Pei‐Jin</creatorcontrib><creatorcontrib>Yu, Xiao‐Qiang</creatorcontrib><creatorcontrib>Rao, Xiang‐Jun</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Chemoreception Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of insect biochemistry and physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shahzad, Toufeeq</au><au>Zhan, Ming‐Yue</au><au>Yang, Pei‐Jin</au><au>Yu, Xiao‐Qiang</au><au>Rao, Xiang‐Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori</atitle><jtitle>Archives of insect biochemistry and physiology</jtitle><addtitle>Arch Insect Biochem Physiol</addtitle><date>2017-07</date><risdate>2017</risdate><volume>95</volume><issue>3</issue><epage>n/a</epage><issn>0739-4462</issn><eissn>1520-6327</eissn><abstract>C‐type lectins (CTLs) play a variety of roles in plants and animals. They are involved in animal development, pathogen recognition, and the activation of immune responses. CTLs carry one or more non‐catalytic carbohydrate‐recognition domains (CRDs) to bind specific carbohydrates reversibly. Here, we report the molecular cloning and functional analysis of a single‐CRD CTL, named C‐type lectin‐S2 (BmCTL‐S2) from the domesticated silkmoth Bombyx mori (Lepidoptera: Bombycidae). The ORF of CTL‐S2 is 666 bp, which encodes a putative protein of 221 amino acids. BmCTL‐S2 is expressed in a variety of immune‐related tissues, including hemocytes and fat body among others. BmCTL‐S2 mRNA level in the midgut and the fat body was significantly increased by bacterial challenges. The recombinant protein (rBmCTL‐S2) bound different bacterial cell wall components and bacterial cells. rBmCTL‐S2 also inhibited the growth of Bacillus subtilis and Staphylococcus aureus. Taken together, we infer that BmCTL‐S2 is a pattern‐recognition receptor with antibacterial activities.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>28618068</pmid><doi>10.1002/arch.21391</doi><tpages>14</tpages><orcidid>https://orcid.org/0000-0002-3591-6698</orcidid></addata></record> |
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| subjects | Activation Amino Acid Sequence Amino acids Animals Bacillus subtilis Base Sequence Bombyx - genetics Bombyx - immunology Bombyx - metabolism Bombyx mori Carbohydrates Catalysis Cell walls Cloning C‐type lectin Fat body Fat Body - metabolism Functional analysis Hemocytes Immune response insect immunity Insect Proteins - isolation & purification Insect Proteins - physiology Larva - immunology Larva - metabolism Lectins Lectins, C-Type - isolation & purification Lectins, C-Type - physiology Microbial Sensitivity Tests Midgut mRNA Pathogen-Associated Molecular Pattern Molecules - metabolism Pathogens Pattern recognition Sequence Analysis, DNA silkworm Staphylococcus aureus Tissues |
| title | Molecular cloning and analysis of a C‐type lectin from silkworm Bombyx mori |
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