Isolation and Characterization of Gomesin, an 18-Residue Cysteine-rich Defense Peptide from the Spider Acanthoscurria gomesiana Hemocytes with Sequence Similarities to Horseshoe Crab Antimicrobial Peptides of the Tachyplesin Family
We have purified a small size antimicrobial peptide, named gomesin, from the hemocytes of the unchallenged tarantula spider Acanthoscurria gomesiana. Gomesin has a molecular mass of 2270.4 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine α-amide, and fo...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-10, Vol.275 (43), p.33464-33470 |
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| creator | Silva, Pedro I. Daffre, Sirlei Bulet, Philippe |
| description | We have purified a small size antimicrobial peptide, named gomesin, from the hemocytes of the unchallenged tarantula spider Acanthoscurria gomesiana. Gomesin has a molecular mass of 2270.4 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine α-amide, and four cysteine residues forming two disulfide bridges. This peptide shows marked sequence similarities to antimicrobial peptides from other arthropods such as tachyplesin and polyphemusin from horseshoe crabs and androctonin from scorpions. Interestingly, it also shows sequence similarities to protegrins, antimicrobial peptides from porcine leukocytes. Gomesin strongly affects bacterial growth, as well as the development of filamentous fungi and yeast. In addition, we showed that gomesin affects the viability of the parasite Leishmania amazonensis. |
| doi_str_mv | 10.1074/jbc.M001491200 |
| format | Article |
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Gomesin has a molecular mass of 2270.4 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine α-amide, and four cysteine residues forming two disulfide bridges. This peptide shows marked sequence similarities to antimicrobial peptides from other arthropods such as tachyplesin and polyphemusin from horseshoe crabs and androctonin from scorpions. Interestingly, it also shows sequence similarities to protegrins, antimicrobial peptides from porcine leukocytes. Gomesin strongly affects bacterial growth, as well as the development of filamentous fungi and yeast. In addition, we showed that gomesin affects the viability of the parasite Leishmania amazonensis.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M001491200</identifier><identifier>PMID: 10942757</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acanthoscurria gomesiana ; Amino Acid Sequence ; Animals ; Anti-Bacterial Agents ; Anti-Infective Agents - chemistry ; Anti-Infective Agents - isolation & purification ; Anti-Infective Agents - pharmacology ; Antimicrobial Cationic Peptides ; Bacteria - drug effects ; Blood Proteins - chemistry ; Blood Proteins - isolation & purification ; Blood Proteins - pharmacology ; DNA-Binding Proteins - chemistry ; Fungi - drug effects ; gomesin ; Hemocytes - chemistry ; Life Sciences ; Molecular Sequence Data ; Peptides - chemistry ; Peptides - isolation & purification ; Peptides - pharmacology ; Peptides, Cyclic - chemistry ; Spiders - chemistry</subject><ispartof>The Journal of biological chemistry, 2000-10, Vol.275 (43), p.33464-33470</ispartof><rights>2000 © 2000 ASBMB. 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Gomesin has a molecular mass of 2270.4 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine α-amide, and four cysteine residues forming two disulfide bridges. This peptide shows marked sequence similarities to antimicrobial peptides from other arthropods such as tachyplesin and polyphemusin from horseshoe crabs and androctonin from scorpions. Interestingly, it also shows sequence similarities to protegrins, antimicrobial peptides from porcine leukocytes. Gomesin strongly affects bacterial growth, as well as the development of filamentous fungi and yeast. In addition, we showed that gomesin affects the viability of the parasite Leishmania amazonensis.</description><subject>Acanthoscurria gomesiana</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Anti-Bacterial Agents</subject><subject>Anti-Infective Agents - chemistry</subject><subject>Anti-Infective Agents - isolation & purification</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>Antimicrobial Cationic Peptides</subject><subject>Bacteria - drug effects</subject><subject>Blood Proteins - chemistry</subject><subject>Blood Proteins - isolation & purification</subject><subject>Blood Proteins - pharmacology</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>Fungi - drug effects</subject><subject>gomesin</subject><subject>Hemocytes - chemistry</subject><subject>Life Sciences</subject><subject>Molecular Sequence Data</subject><subject>Peptides - chemistry</subject><subject>Peptides - isolation & purification</subject><subject>Peptides - pharmacology</subject><subject>Peptides, Cyclic - chemistry</subject><subject>Spiders - chemistry</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkk1v1DAQhiMEokvhyhH5gJCQyGLH-fAeVwvtVloEokXiZjnOpJkqibe2t9Xyh_kbTNjl44LwxfLMMzPvjCdJngs-F7zK397Udv6Bc5EvRMb5g2QmuJKpLMTXh8mM80yki6xQJ8mTEG44HeIeJyeCL_KsKqpZ8v0iuN5EdCMzY8NWnfHGRvD47WB0LTt3AwQc3xDAhEo_06PZAVvtQwQcIfVoO_YOWhgDsE-wjdgAa70bWOyAXW7p6dnSmjF2Ltid92jY9c-cZjRsDYOz-wiB3WPs2CXc7mC0FIcD9sZjRHJFx9bOBwido8Le1Gw5RgKsdzWa_lfVMMmdil4Z2-23_SSbnRlKtH-aPGpNH-DZ8T5Nvpy9v1qt083H84vVcpPavMpjWkJpCsgKmUPdWK6UrVuoCyNzGlxTWxBCKSHKtlJZqaoMRAuirlRb0DELIU-T14e8nen11uNg_F47g3q93OjJxqXKlCrLu4l9dWC33lHXIeoBg4W-NyO4XdBVJpWQpfwvKKoqE6SHwPkBpMGE4KH9LUFwPe2Lpn3Rf_aFAl4cM-_qAZq_8MOCEPDy2A9ed_foQdfobAeDJrfOpZYyL3PC1AEDmu0dgtfB4vSPDYXYqBuH_5LwAyZS3mo</recordid><startdate>20001027</startdate><enddate>20001027</enddate><creator>Silva, Pedro I.</creator><creator>Daffre, Sirlei</creator><creator>Bulet, Philippe</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7X8</scope><scope>1XC</scope></search><sort><creationdate>20001027</creationdate><title>Isolation and Characterization of Gomesin, an 18-Residue Cysteine-rich Defense Peptide from the Spider Acanthoscurria gomesiana Hemocytes with Sequence Similarities to Horseshoe Crab Antimicrobial Peptides of the Tachyplesin Family</title><author>Silva, Pedro I. ; 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Gomesin has a molecular mass of 2270.4 Da, with 18 amino acids, including a pyroglutamic acid as the N terminus, a C-terminal arginine α-amide, and four cysteine residues forming two disulfide bridges. This peptide shows marked sequence similarities to antimicrobial peptides from other arthropods such as tachyplesin and polyphemusin from horseshoe crabs and androctonin from scorpions. Interestingly, it also shows sequence similarities to protegrins, antimicrobial peptides from porcine leukocytes. Gomesin strongly affects bacterial growth, as well as the development of filamentous fungi and yeast. In addition, we showed that gomesin affects the viability of the parasite Leishmania amazonensis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10942757</pmid><doi>10.1074/jbc.M001491200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acanthoscurria gomesiana Amino Acid Sequence Animals Anti-Bacterial Agents Anti-Infective Agents - chemistry Anti-Infective Agents - isolation & purification Anti-Infective Agents - pharmacology Antimicrobial Cationic Peptides Bacteria - drug effects Blood Proteins - chemistry Blood Proteins - isolation & purification Blood Proteins - pharmacology DNA-Binding Proteins - chemistry Fungi - drug effects gomesin Hemocytes - chemistry Life Sciences Molecular Sequence Data Peptides - chemistry Peptides - isolation & purification Peptides - pharmacology Peptides, Cyclic - chemistry Spiders - chemistry |
| title | Isolation and Characterization of Gomesin, an 18-Residue Cysteine-rich Defense Peptide from the Spider Acanthoscurria gomesiana Hemocytes with Sequence Similarities to Horseshoe Crab Antimicrobial Peptides of the Tachyplesin Family |
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