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A novel defensin‐like peptide from salivary glands of the hard tick, Haemaphysalis longicornis
A novel defensin‐like antimicrobial peptide named longicornsin was isolated from the salivary glands of the hard tick, Haemaphysalis longicornis, using a 10‐kDa cut‐off Centriprep filter and reversed‐phase high‐performance liquid chromatography (RP‐HPLC). Its amino acid sequence was determined as DF...
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| Published in: | Protein science 2010-03, Vol.19 (3), p.392-397 |
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| Main Authors: | , , , , , , , |
| Format: | Article |
| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c5317-f0fb01cbc2a734bbfd5722579d34824ad19c3c4d9764add223d3c48c69f95dac3 |
| container_end_page | 397 |
| container_issue | 3 |
| container_start_page | 392 |
| container_title | Protein science |
| container_volume | 19 |
| creator | Lu, Xiangyun Che, Qiaolin Lv, Yi Wang, Meijuan Lu, Zekuan Feng, Feifei Liu, Jingze Yu, Haining |
| description | A novel defensin‐like antimicrobial peptide named longicornsin was isolated from the salivary glands of the hard tick, Haemaphysalis longicornis, using a 10‐kDa cut‐off Centriprep filter and reversed‐phase high‐performance liquid chromatography (RP‐HPLC). Its amino acid sequence was determined as DFGCGQGMIFMCQRRCMRLYPGSTGFCRGFRCMCDTHIPLRPPFMVG by Edman degradation. The cDNA encoding longicornsin was cloned by cDNA library screening. The predicted protein from the cDNA sequence was composed of 78 amino acids including a mature longicornsin. It showed similarity with defensin‐like peptides from other ticks by BLAST search. Different from most other tick defensin‐like peptides, longicornsin had a C‐terminal extension. Purified longicornsin exerted potent antimicrobial activities against bacteria and fungi. Interestingly, it even showed strong antimicrobial ability against drug‐resistant microorganisms and Helicobacter pylori. The results of this study indicated that longicornsin is a potential candidate for novel antimicrobial drug design. |
| doi_str_mv | 10.1002/pro.317 |
| format | article |
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Its amino acid sequence was determined as DFGCGQGMIFMCQRRCMRLYPGSTGFCRGFRCMCDTHIPLRPPFMVG by Edman degradation. The cDNA encoding longicornsin was cloned by cDNA library screening. The predicted protein from the cDNA sequence was composed of 78 amino acids including a mature longicornsin. It showed similarity with defensin‐like peptides from other ticks by BLAST search. Different from most other tick defensin‐like peptides, longicornsin had a C‐terminal extension. Purified longicornsin exerted potent antimicrobial activities against bacteria and fungi. Interestingly, it even showed strong antimicrobial ability against drug‐resistant microorganisms and Helicobacter pylori. The results of this study indicated that longicornsin is a potential candidate for novel antimicrobial drug design.</description><identifier>ISSN: 0961-8368</identifier><identifier>EISSN: 1469-896X</identifier><identifier>DOI: 10.1002/pro.317</identifier><identifier>PMID: 20027626</identifier><identifier>CODEN: PRCIEI</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Amino Acid Sequence ; Amino acids ; Animals ; Anti-Infective Agents - chemistry ; Anti-Infective Agents - isolation & purification ; Anti-Infective Agents - pharmacology ; antimicrobial peptide ; Bacteria - drug effects ; Chromatography ; Chromatography, High Pressure Liquid ; defensin ; Defensins - chemistry ; Defensins - genetics ; Defensins - pharmacology ; Drug Resistance, Bacterial ; Fungi - drug effects ; Haemaphysalis longicornis ; Helicobacter pylori ; Helicobacter pylori - drug effects ; Ixodidae ; Ixodidae - chemistry ; Ixodidae - metabolism ; Molecular Sequence Data ; salivary gland ; Salivary Glands - chemistry ; Salivary Glands - metabolism ; tick</subject><ispartof>Protein science, 2010-03, Vol.19 (3), p.392-397</ispartof><rights>Copyright © 2009 The Protein Society</rights><rights>Copyright © 2010 The Protein Society</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5317-f0fb01cbc2a734bbfd5722579d34824ad19c3c4d9764add223d3c48c69f95dac3</citedby><cites>FETCH-LOGICAL-c5317-f0fb01cbc2a734bbfd5722579d34824ad19c3c4d9764add223d3c48c69f95dac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2866266/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2866266/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20027626$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lu, Xiangyun</creatorcontrib><creatorcontrib>Che, Qiaolin</creatorcontrib><creatorcontrib>Lv, Yi</creatorcontrib><creatorcontrib>Wang, Meijuan</creatorcontrib><creatorcontrib>Lu, Zekuan</creatorcontrib><creatorcontrib>Feng, Feifei</creatorcontrib><creatorcontrib>Liu, Jingze</creatorcontrib><creatorcontrib>Yu, Haining</creatorcontrib><title>A novel defensin‐like peptide from salivary glands of the hard tick, Haemaphysalis longicornis</title><title>Protein science</title><addtitle>Protein Sci</addtitle><description>A novel defensin‐like antimicrobial peptide named longicornsin was isolated from the salivary glands of the hard tick, Haemaphysalis longicornis, using a 10‐kDa cut‐off Centriprep filter and reversed‐phase high‐performance liquid chromatography (RP‐HPLC). Its amino acid sequence was determined as DFGCGQGMIFMCQRRCMRLYPGSTGFCRGFRCMCDTHIPLRPPFMVG by Edman degradation. The cDNA encoding longicornsin was cloned by cDNA library screening. The predicted protein from the cDNA sequence was composed of 78 amino acids including a mature longicornsin. It showed similarity with defensin‐like peptides from other ticks by BLAST search. Different from most other tick defensin‐like peptides, longicornsin had a C‐terminal extension. Purified longicornsin exerted potent antimicrobial activities against bacteria and fungi. Interestingly, it even showed strong antimicrobial ability against drug‐resistant microorganisms and Helicobacter pylori. The results of this study indicated that longicornsin is a potential candidate for novel antimicrobial drug design.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Anti-Infective Agents - chemistry</subject><subject>Anti-Infective Agents - isolation & purification</subject><subject>Anti-Infective Agents - pharmacology</subject><subject>antimicrobial peptide</subject><subject>Bacteria - drug effects</subject><subject>Chromatography</subject><subject>Chromatography, High Pressure Liquid</subject><subject>defensin</subject><subject>Defensins - chemistry</subject><subject>Defensins - genetics</subject><subject>Defensins - pharmacology</subject><subject>Drug Resistance, Bacterial</subject><subject>Fungi - drug effects</subject><subject>Haemaphysalis longicornis</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - drug effects</subject><subject>Ixodidae</subject><subject>Ixodidae - chemistry</subject><subject>Ixodidae - metabolism</subject><subject>Molecular Sequence Data</subject><subject>salivary gland</subject><subject>Salivary Glands - chemistry</subject><subject>Salivary Glands - metabolism</subject><subject>tick</subject><issn>0961-8368</issn><issn>1469-896X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><recordid>eNp9kdtqFTEYhYModlvFN5CAFwo6NYfJ6UYopVqhUBEF72Imh73Tzkymyexd9p2P4DP6JGbTWg-gV2GRLyv_vxYAjzE6wAiRV1NOBxSLO2CBW64aqfjnu2CBFMeNpFzugQelnCOEWkzofbBH6hvBCV-AL4dwTBvfQ-eDH0scv3_91scLDyc_zdF5GHIaYDF93Ji8hcvejK7AFOC88nBlsoNztBcv4Ynxg5lW2x1ZYJ_GZbQpj7E8BPeC6Yt_dHPug09vjj8enTSnZ2_fHR2eNpbVwZuAQoew7SwxgrZdFxwThDChHG0laY3DylLbOiV4FY4Q6qqUlqugmDOW7oPX177Tuhu8s36cs-n1lONQB9fJRP3nzRhXepk2mkhek-DV4NmNQU6Xa19mPcRifV839mldtKCUYaoIreTz_5JYSEaIZIxU9Olf6Hla57EGUSnOZe1DsF9f25xKyT7cjo2R3vVbddI1pko--X3LW-5noRV4cQ1cxd5v_-Wj338429n9ADRBsJo</recordid><startdate>201003</startdate><enddate>201003</enddate><creator>Lu, Xiangyun</creator><creator>Che, Qiaolin</creator><creator>Lv, Yi</creator><creator>Wang, Meijuan</creator><creator>Lu, Zekuan</creator><creator>Feng, Feifei</creator><creator>Liu, Jingze</creator><creator>Yu, Haining</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><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>7QO</scope><scope>7T5</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201003</creationdate><title>A novel defensin‐like peptide from salivary glands of the hard tick, Haemaphysalis longicornis</title><author>Lu, Xiangyun ; Che, Qiaolin ; Lv, Yi ; Wang, Meijuan ; Lu, Zekuan ; Feng, Feifei ; Liu, Jingze ; Yu, Haining</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5317-f0fb01cbc2a734bbfd5722579d34824ad19c3c4d9764add223d3c48c69f95dac3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Anti-Infective Agents - chemistry</topic><topic>Anti-Infective Agents - isolation & purification</topic><topic>Anti-Infective Agents - pharmacology</topic><topic>antimicrobial peptide</topic><topic>Bacteria - drug effects</topic><topic>Chromatography</topic><topic>Chromatography, High Pressure Liquid</topic><topic>defensin</topic><topic>Defensins - chemistry</topic><topic>Defensins - genetics</topic><topic>Defensins - pharmacology</topic><topic>Drug Resistance, Bacterial</topic><topic>Fungi - drug effects</topic><topic>Haemaphysalis longicornis</topic><topic>Helicobacter pylori</topic><topic>Helicobacter pylori - drug effects</topic><topic>Ixodidae</topic><topic>Ixodidae - chemistry</topic><topic>Ixodidae - metabolism</topic><topic>Molecular Sequence Data</topic><topic>salivary gland</topic><topic>Salivary Glands - chemistry</topic><topic>Salivary Glands - metabolism</topic><topic>tick</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lu, Xiangyun</creatorcontrib><creatorcontrib>Che, Qiaolin</creatorcontrib><creatorcontrib>Lv, Yi</creatorcontrib><creatorcontrib>Wang, Meijuan</creatorcontrib><creatorcontrib>Lu, Zekuan</creatorcontrib><creatorcontrib>Feng, Feifei</creatorcontrib><creatorcontrib>Liu, Jingze</creatorcontrib><creatorcontrib>Yu, Haining</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</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>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Protein science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lu, Xiangyun</au><au>Che, Qiaolin</au><au>Lv, Yi</au><au>Wang, Meijuan</au><au>Lu, Zekuan</au><au>Feng, Feifei</au><au>Liu, Jingze</au><au>Yu, Haining</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel defensin‐like peptide from salivary glands of the hard tick, Haemaphysalis longicornis</atitle><jtitle>Protein science</jtitle><addtitle>Protein Sci</addtitle><date>2010-03</date><risdate>2010</risdate><volume>19</volume><issue>3</issue><spage>392</spage><epage>397</epage><pages>392-397</pages><issn>0961-8368</issn><eissn>1469-896X</eissn><coden>PRCIEI</coden><abstract>A novel defensin‐like antimicrobial peptide named longicornsin was isolated from the salivary glands of the hard tick, Haemaphysalis longicornis, using a 10‐kDa cut‐off Centriprep filter and reversed‐phase high‐performance liquid chromatography (RP‐HPLC). Its amino acid sequence was determined as DFGCGQGMIFMCQRRCMRLYPGSTGFCRGFRCMCDTHIPLRPPFMVG by Edman degradation. The cDNA encoding longicornsin was cloned by cDNA library screening. The predicted protein from the cDNA sequence was composed of 78 amino acids including a mature longicornsin. It showed similarity with defensin‐like peptides from other ticks by BLAST search. Different from most other tick defensin‐like peptides, longicornsin had a C‐terminal extension. Purified longicornsin exerted potent antimicrobial activities against bacteria and fungi. Interestingly, it even showed strong antimicrobial ability against drug‐resistant microorganisms and Helicobacter pylori. The results of this study indicated that longicornsin is a potential candidate for novel antimicrobial drug design.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>20027626</pmid><doi>10.1002/pro.317</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0961-8368 |
| ispartof | Protein science, 2010-03, Vol.19 (3), p.392-397 |
| issn | 0961-8368 1469-896X |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2866266 |
| source | Wiley-Blackwell Read & Publish Collection; PubMed Central |
| subjects | Amino Acid Sequence Amino acids Animals Anti-Infective Agents - chemistry Anti-Infective Agents - isolation & purification Anti-Infective Agents - pharmacology antimicrobial peptide Bacteria - drug effects Chromatography Chromatography, High Pressure Liquid defensin Defensins - chemistry Defensins - genetics Defensins - pharmacology Drug Resistance, Bacterial Fungi - drug effects Haemaphysalis longicornis Helicobacter pylori Helicobacter pylori - drug effects Ixodidae Ixodidae - chemistry Ixodidae - metabolism Molecular Sequence Data salivary gland Salivary Glands - chemistry Salivary Glands - metabolism tick |
| title | A novel defensin‐like peptide from salivary glands of the hard tick, Haemaphysalis longicornis |
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