Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens
Membrane-bound alkaline phosphatases (mALPs, EC 3.1.3.1) in the insect midgut have been reported as functional receptors for Cry toxins from the bacterium Bacillus thuringiensis. We previously reported the identification of HvALP in the midgut of Heliothis virescens larvae as a Cry1Ac-binding protei...
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| Veröffentlicht in: | Insect biochemistry and molecular biology 2009-04, Vol.39 (4), p.294-302 |
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| creator | Perera, Omaththage P. Willis, Jonathan D. Adang, Michael J. Jurat-Fuentes, Juan L. |
| description | Membrane-bound alkaline phosphatases (mALPs, EC 3.1.3.1) in the insect midgut have been reported as functional receptors for Cry toxins from the bacterium Bacillus thuringiensis. We previously reported the identification of HvALP in the midgut of Heliothis virescens larvae as a Cry1Ac-binding protein that is down-regulated in Cry1Ac-resistant insects. To further characterize HvALP, we localized mALP protein to foregut and midgut tissues using anti-mALP serum and then cloned five mALPs from H. virescens larval midgut. All five clones displayed high levels of sequence identity (above 90%), suggesting that they may represent allelic variants, and grouped with other lepidopteran mALPs in sequence alignments. All these cloned ALPs were predicted to contain a glycosylphosphatidylinositol (GPI) anchor and were named HvmALP1–5. We expressed two of the most diverse HvmALPs in a heterologous system to test binding of Cry1Ac and recognition by HvALP cross-reacting antiserum. Our data highlight the importance of glycosylation for Cry1Ac binding to HvALP and suggest that, depending on glycosylation, all the identified HvmALPs may be synonymous with HvALP, the Cry1Ac-binding phosphatase identified in H. virescens midgut epithelium. |
| doi_str_mv | 10.1016/j.ibmb.2009.01.006 |
| format | Article |
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We previously reported the identification of HvALP in the midgut of Heliothis virescens larvae as a Cry1Ac-binding protein that is down-regulated in Cry1Ac-resistant insects. To further characterize HvALP, we localized mALP protein to foregut and midgut tissues using anti-mALP serum and then cloned five mALPs from H. virescens larval midgut. All five clones displayed high levels of sequence identity (above 90%), suggesting that they may represent allelic variants, and grouped with other lepidopteran mALPs in sequence alignments. All these cloned ALPs were predicted to contain a glycosylphosphatidylinositol (GPI) anchor and were named HvmALP1–5. We expressed two of the most diverse HvmALPs in a heterologous system to test binding of Cry1Ac and recognition by HvALP cross-reacting antiserum. Our data highlight the importance of glycosylation for Cry1Ac binding to HvALP and suggest that, depending on glycosylation, all the identified HvmALPs may be synonymous with HvALP, the Cry1Ac-binding phosphatase identified in H. virescens midgut epithelium.</description><identifier>ISSN: 0965-1748</identifier><identifier>EISSN: 1879-0240</identifier><identifier>DOI: 10.1016/j.ibmb.2009.01.006</identifier><identifier>PMID: 19552892</identifier><language>eng</language><publisher>England: Elsevier Ltd</publisher><subject>Alkaline phosphatase ; Alkaline Phosphatase - chemistry ; Alkaline Phosphatase - genetics ; Alkaline Phosphatase - metabolism ; Amino Acid Sequence ; amino acid sequences ; Animals ; Bacillus thuringiensis ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; binding proteins ; brush border membrane vesicles ; Cloning, Molecular ; complementary DNA ; Cry toxins ; Cry1Ac binding ; crystal proteins ; delta-endotoxins ; Endotoxins - genetics ; Endotoxins - metabolism ; gene expression ; Glycosylation ; Heliothis virescens ; Hemolysin Proteins - genetics ; Hemolysin Proteins - metabolism ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Lepidoptera ; midgut ; molecular cloning ; Molecular Sequence Data ; Moths - chemistry ; Moths - classification ; Moths - genetics ; Moths - metabolism ; nucleotide sequences ; Phylogeny ; Protein Transport ; Sequence Alignment ; sequence homology ; toxin binding</subject><ispartof>Insect biochemistry and molecular biology, 2009-04, Vol.39 (4), p.294-302</ispartof><rights>2009 Elsevier Ltd</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-9c6b02e965d55ed5ea93345302cb68e3ba7284881d8f6a9ca60d7ae2c860db893</citedby><cites>FETCH-LOGICAL-c409t-9c6b02e965d55ed5ea93345302cb68e3ba7284881d8f6a9ca60d7ae2c860db893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.ibmb.2009.01.006$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3541,27915,27916,45986</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19552892$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Perera, Omaththage P.</creatorcontrib><creatorcontrib>Willis, Jonathan D.</creatorcontrib><creatorcontrib>Adang, Michael J.</creatorcontrib><creatorcontrib>Jurat-Fuentes, Juan L.</creatorcontrib><title>Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens</title><title>Insect biochemistry and molecular biology</title><addtitle>Insect Biochem Mol Biol</addtitle><description>Membrane-bound alkaline phosphatases (mALPs, EC 3.1.3.1) in the insect midgut have been reported as functional receptors for Cry toxins from the bacterium Bacillus thuringiensis. We previously reported the identification of HvALP in the midgut of Heliothis virescens larvae as a Cry1Ac-binding protein that is down-regulated in Cry1Ac-resistant insects. To further characterize HvALP, we localized mALP protein to foregut and midgut tissues using anti-mALP serum and then cloned five mALPs from H. virescens larval midgut. All five clones displayed high levels of sequence identity (above 90%), suggesting that they may represent allelic variants, and grouped with other lepidopteran mALPs in sequence alignments. All these cloned ALPs were predicted to contain a glycosylphosphatidylinositol (GPI) anchor and were named HvmALP1–5. We expressed two of the most diverse HvmALPs in a heterologous system to test binding of Cry1Ac and recognition by HvALP cross-reacting antiserum. Our data highlight the importance of glycosylation for Cry1Ac binding to HvALP and suggest that, depending on glycosylation, all the identified HvmALPs may be synonymous with HvALP, the Cry1Ac-binding phosphatase identified in H. virescens midgut epithelium.</description><subject>Alkaline phosphatase</subject><subject>Alkaline Phosphatase - chemistry</subject><subject>Alkaline Phosphatase - genetics</subject><subject>Alkaline Phosphatase - metabolism</subject><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>Bacillus thuringiensis</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>binding proteins</subject><subject>brush border membrane vesicles</subject><subject>Cloning, Molecular</subject><subject>complementary DNA</subject><subject>Cry toxins</subject><subject>Cry1Ac binding</subject><subject>crystal proteins</subject><subject>delta-endotoxins</subject><subject>Endotoxins - genetics</subject><subject>Endotoxins - metabolism</subject><subject>gene expression</subject><subject>Glycosylation</subject><subject>Heliothis virescens</subject><subject>Hemolysin Proteins - genetics</subject><subject>Hemolysin Proteins - metabolism</subject><subject>Insect Proteins - chemistry</subject><subject>Insect Proteins - genetics</subject><subject>Insect Proteins - metabolism</subject><subject>Lepidoptera</subject><subject>midgut</subject><subject>molecular cloning</subject><subject>Molecular Sequence Data</subject><subject>Moths - chemistry</subject><subject>Moths - classification</subject><subject>Moths - genetics</subject><subject>Moths - metabolism</subject><subject>nucleotide sequences</subject><subject>Phylogeny</subject><subject>Protein Transport</subject><subject>Sequence Alignment</subject><subject>sequence homology</subject><subject>toxin binding</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkUGP0zAQhS0EYsvCH-AAPiE4JIwdO7GlvVQVu0WqBBLs2XKcycYljYudVlp-PS6txA1xmjl88-bpPUJeMygZsPrjtvTtri05gC6BlQD1E7JgqtEFcAFPyQJ0LQvWCHVFXqS0BQAhZPOcXDEtJVeaL8iwGsPkpwdqp466wUbrZoz-l519mGjo6TwgXcVHtnRF66fuDzr-sKOfkO6HkPaDnW1C-n59XG6-fqB9DDu6xtGHefCJHn3E5HBKL8mz3o4JX13mNbm__fR9tS42X-4-r5abwgnQc6Fd3QLHbLyTEjuJVleVkBVw19YKq9Y2XAmlWKf62mpna-gai9ypvLRKV9fk3Vl3H8PPA6bZ7Hw2MI52wnBIpm4EE-w_QA6iVhJEBvkZdDGkFLE3--h3Nj4aBuZUhNmaUxHmVIQBZnIR-ejNRf3Q7rD7e3JJPgNvz0Bvg7EP0Sdz_40Dq7IgU7I5_b05E5jjOnqMJjmPk8MuZ-pm0wX_Lwe_ARqgot0</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Perera, Omaththage P.</creator><creator>Willis, Jonathan D.</creator><creator>Adang, Michael J.</creator><creator>Jurat-Fuentes, Juan L.</creator><general>Elsevier Ltd</general><scope>FBQ</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>7QL</scope><scope>7SS</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20090401</creationdate><title>Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens</title><author>Perera, Omaththage P. ; Willis, Jonathan D. ; Adang, Michael J. ; Jurat-Fuentes, Juan L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-9c6b02e965d55ed5ea93345302cb68e3ba7284881d8f6a9ca60d7ae2c860db893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Alkaline phosphatase</topic><topic>Alkaline Phosphatase - chemistry</topic><topic>Alkaline Phosphatase - genetics</topic><topic>Alkaline Phosphatase - metabolism</topic><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Animals</topic><topic>Bacillus thuringiensis</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>binding proteins</topic><topic>brush border membrane vesicles</topic><topic>Cloning, Molecular</topic><topic>complementary DNA</topic><topic>Cry toxins</topic><topic>Cry1Ac binding</topic><topic>crystal proteins</topic><topic>delta-endotoxins</topic><topic>Endotoxins - genetics</topic><topic>Endotoxins - metabolism</topic><topic>gene expression</topic><topic>Glycosylation</topic><topic>Heliothis virescens</topic><topic>Hemolysin Proteins - genetics</topic><topic>Hemolysin Proteins - metabolism</topic><topic>Insect Proteins - chemistry</topic><topic>Insect Proteins - genetics</topic><topic>Insect Proteins - metabolism</topic><topic>Lepidoptera</topic><topic>midgut</topic><topic>molecular cloning</topic><topic>Molecular Sequence Data</topic><topic>Moths - chemistry</topic><topic>Moths - classification</topic><topic>Moths - genetics</topic><topic>Moths - metabolism</topic><topic>nucleotide sequences</topic><topic>Phylogeny</topic><topic>Protein Transport</topic><topic>Sequence Alignment</topic><topic>sequence homology</topic><topic>toxin binding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Perera, Omaththage P.</creatorcontrib><creatorcontrib>Willis, Jonathan D.</creatorcontrib><creatorcontrib>Adang, Michael J.</creatorcontrib><creatorcontrib>Jurat-Fuentes, Juan L.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Insect biochemistry and molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Perera, Omaththage P.</au><au>Willis, Jonathan D.</au><au>Adang, Michael J.</au><au>Jurat-Fuentes, Juan L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>39</volume><issue>4</issue><spage>294</spage><epage>302</epage><pages>294-302</pages><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>Membrane-bound alkaline phosphatases (mALPs, EC 3.1.3.1) in the insect midgut have been reported as functional receptors for Cry toxins from the bacterium Bacillus thuringiensis. We previously reported the identification of HvALP in the midgut of Heliothis virescens larvae as a Cry1Ac-binding protein that is down-regulated in Cry1Ac-resistant insects. To further characterize HvALP, we localized mALP protein to foregut and midgut tissues using anti-mALP serum and then cloned five mALPs from H. virescens larval midgut. All five clones displayed high levels of sequence identity (above 90%), suggesting that they may represent allelic variants, and grouped with other lepidopteran mALPs in sequence alignments. All these cloned ALPs were predicted to contain a glycosylphosphatidylinositol (GPI) anchor and were named HvmALP1–5. We expressed two of the most diverse HvmALPs in a heterologous system to test binding of Cry1Ac and recognition by HvALP cross-reacting antiserum. Our data highlight the importance of glycosylation for Cry1Ac binding to HvALP and suggest that, depending on glycosylation, all the identified HvmALPs may be synonymous with HvALP, the Cry1Ac-binding phosphatase identified in H. virescens midgut epithelium.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>19552892</pmid><doi>10.1016/j.ibmb.2009.01.006</doi><tpages>9</tpages></addata></record> |
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| ispartof | Insect biochemistry and molecular biology, 2009-04, Vol.39 (4), p.294-302 |
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| subjects | Alkaline phosphatase Alkaline Phosphatase - chemistry Alkaline Phosphatase - genetics Alkaline Phosphatase - metabolism Amino Acid Sequence amino acid sequences Animals Bacillus thuringiensis Bacterial Proteins - genetics Bacterial Proteins - metabolism binding proteins brush border membrane vesicles Cloning, Molecular complementary DNA Cry toxins Cry1Ac binding crystal proteins delta-endotoxins Endotoxins - genetics Endotoxins - metabolism gene expression Glycosylation Heliothis virescens Hemolysin Proteins - genetics Hemolysin Proteins - metabolism Insect Proteins - chemistry Insect Proteins - genetics Insect Proteins - metabolism Lepidoptera midgut molecular cloning Molecular Sequence Data Moths - chemistry Moths - classification Moths - genetics Moths - metabolism nucleotide sequences Phylogeny Protein Transport Sequence Alignment sequence homology toxin binding |
| title | Cloning and characterization of the Cry1Ac-binding alkaline phosphatase (HvALP) from Heliothis virescens |
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