The hemolymph proteome of Anopheles gambiae
We used two-dimensional SDS–PAGE and microsequencing or peptide mass fingerprinting to identify major proteins in the hemolymph of Anopheles gambiae. We found approximately 280 protein spots in hemolymph and identified 28 spots, representing 26 individual proteins. Most of these proteins have known...
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| Veröffentlicht in: | Insect biochemistry and molecular biology 2005-08, Vol.35 (8), p.815-824 |
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| creator | Paskewitz, Susan M. Shi, Lei |
| description | We used two-dimensional SDS–PAGE and microsequencing or peptide mass fingerprinting to identify major proteins in the hemolymph of
Anopheles gambiae. We found approximately 280 protein spots in hemolymph and identified 28 spots, representing 26 individual proteins. Most of these proteins have known or predicted functions in immunity, iron transport, or lipid biology. Many of the proteins have been found in hemolymph in other insects but one protein is novel: a new member of the ML family (involved in lipid recognition). Three of the identified proteins increased in spot intensity or appeared de novo following bacterial injection: a phenoloxidase, and two chitinase-like proteins. A subset of proteins decreased following bacterial injections: these included the light and heavy chains of ferritin. Several proteins appeared in hemolymph following any wound or injection. Most of these are metabolic enzymes lacking signal peptides that are likely to be released as a result of damage to muscles and other tissues by injury. The map will provide a useful tool for examining changes in hemolymph proteins following blood feeding and infection by parasites. |
| doi_str_mv | 10.1016/j.ibmb.2005.03.002 |
| format | Article |
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Anopheles gambiae. We found approximately 280 protein spots in hemolymph and identified 28 spots, representing 26 individual proteins. Most of these proteins have known or predicted functions in immunity, iron transport, or lipid biology. Many of the proteins have been found in hemolymph in other insects but one protein is novel: a new member of the ML family (involved in lipid recognition). Three of the identified proteins increased in spot intensity or appeared de novo following bacterial injection: a phenoloxidase, and two chitinase-like proteins. A subset of proteins decreased following bacterial injections: these included the light and heavy chains of ferritin. Several proteins appeared in hemolymph following any wound or injection. Most of these are metabolic enzymes lacking signal peptides that are likely to be released as a result of damage to muscles and other tissues by injury. The map will provide a useful tool for examining changes in hemolymph proteins following blood feeding and infection by parasites.</description><subject>amino acid sequences</subject><subject>animal injuries</subject><subject>Animals</subject><subject>Anopheles - genetics</subject><subject>Anopheles - immunology</subject><subject>Anopheles gambiae</subject><subject>Bacteria - pathogenicity</subject><subject>bacterial infections</subject><subject>Culicidae</subject><subject>DNA Fingerprinting</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>hemolymph</subject><subject>Hemolymph - chemistry</subject><subject>hemolymph proteins</subject><subject>Immunity</subject><subject>injection</subject><subject>Injury</subject><subject>insect immunity</subject><subject>insect proteins</subject><subject>Iron</subject><subject>Lipid</subject><subject>protein synthesis</subject><subject>Proteome</subject><subject>proteomics</subject><subject>Sequence Analysis</subject><subject>two-dimensional SDS–PAGE</subject><issn>0965-1748</issn><issn>1879-0240</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EglL4AwyQiQUlnB0ntiUWhPiSKjHQzpadXIirpC5xi8S_x1UqscF0wz3vq7uHkAsKGQVa3i4zZ3ubMYAigzwDYAdkQqVQKTAOh2QCqixSKrg8IachLAGA80IckxNaKM5ByAm5mbeYtNj77rtft8l68Bv0PSa-Se5Xft1ihyH5ML11Bs_IUWO6gOf7OSWLp8f5w0s6e3t-fbifpVUB5Sa1QlJmUAIqATQvocobKyWvGyEbyVUlLLKyFjwXVtBa0sYWwoi4URIsx3xKrsfeeM3nFsNG9y5U2HVmhX4bdClUfEDl_4IMBC1YCf-CVBSQl1RFkI1gNfgQBmz0enC9Gb41Bb2Trpd6J13vpGvIdZQeQ5f79q3tsf6N7C1H4GoEGuO1-Rhc0It3Ft1ArAQFu0_uRgKj1y-Hgw6Vw1WFtRuw2ujau78u-AGzI5lf</recordid><startdate>20050801</startdate><enddate>20050801</enddate><creator>Paskewitz, Susan M.</creator><creator>Shi, Lei</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>7SS</scope><scope>7QL</scope><scope>7T5</scope><scope>C1K</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>20050801</creationdate><title>The hemolymph proteome of Anopheles gambiae</title><author>Paskewitz, Susan M. ; Shi, Lei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c506t-b7812ae80e9701360c3fb884df78f849c7be26d7437b71d81fb57a7849980b4e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>amino acid sequences</topic><topic>animal injuries</topic><topic>Animals</topic><topic>Anopheles - genetics</topic><topic>Anopheles - immunology</topic><topic>Anopheles gambiae</topic><topic>Bacteria - pathogenicity</topic><topic>bacterial infections</topic><topic>Culicidae</topic><topic>DNA Fingerprinting</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>hemolymph</topic><topic>Hemolymph - chemistry</topic><topic>hemolymph proteins</topic><topic>Immunity</topic><topic>injection</topic><topic>Injury</topic><topic>insect immunity</topic><topic>insect proteins</topic><topic>Iron</topic><topic>Lipid</topic><topic>protein synthesis</topic><topic>Proteome</topic><topic>proteomics</topic><topic>Sequence Analysis</topic><topic>two-dimensional SDS–PAGE</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Paskewitz, Susan M.</creatorcontrib><creatorcontrib>Shi, Lei</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>Entomology Abstracts (Full archive)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</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>Paskewitz, Susan M.</au><au>Shi, Lei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The hemolymph proteome of Anopheles gambiae</atitle><jtitle>Insect biochemistry and molecular biology</jtitle><addtitle>Insect Biochem Mol Biol</addtitle><date>2005-08-01</date><risdate>2005</risdate><volume>35</volume><issue>8</issue><spage>815</spage><epage>824</epage><pages>815-824</pages><issn>0965-1748</issn><eissn>1879-0240</eissn><abstract>We used two-dimensional SDS–PAGE and microsequencing or peptide mass fingerprinting to identify major proteins in the hemolymph of
Anopheles gambiae. We found approximately 280 protein spots in hemolymph and identified 28 spots, representing 26 individual proteins. Most of these proteins have known or predicted functions in immunity, iron transport, or lipid biology. Many of the proteins have been found in hemolymph in other insects but one protein is novel: a new member of the ML family (involved in lipid recognition). Three of the identified proteins increased in spot intensity or appeared de novo following bacterial injection: a phenoloxidase, and two chitinase-like proteins. A subset of proteins decreased following bacterial injections: these included the light and heavy chains of ferritin. Several proteins appeared in hemolymph following any wound or injection. Most of these are metabolic enzymes lacking signal peptides that are likely to be released as a result of damage to muscles and other tissues by injury. The map will provide a useful tool for examining changes in hemolymph proteins following blood feeding and infection by parasites.</abstract><cop>England</cop><pub>Elsevier Ltd</pub><pmid>15944078</pmid><doi>10.1016/j.ibmb.2005.03.002</doi><tpages>10</tpages></addata></record> |
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| ispartof | Insect biochemistry and molecular biology, 2005-08, Vol.35 (8), p.815-824 |
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| subjects | amino acid sequences animal injuries Animals Anopheles - genetics Anopheles - immunology Anopheles gambiae Bacteria - pathogenicity bacterial infections Culicidae DNA Fingerprinting Electrophoresis, Polyacrylamide Gel hemolymph Hemolymph - chemistry hemolymph proteins Immunity injection Injury insect immunity insect proteins Iron Lipid protein synthesis Proteome proteomics Sequence Analysis two-dimensional SDS–PAGE |
| title | The hemolymph proteome of Anopheles gambiae |
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