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Article: Structural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)

TitleStructural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)
Authors
KeywordsAnti-HIV-1
Luffin P1
Nuclear magnetic resonance
Ribosome-inactivating peptide
Issue Date2011
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yjsbi
Citation
Journal Of Structural Biology, 2011, v. 174 n. 1, p. 164-172 How to Cite?
AbstractLuffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a helix-loop-helix motif, with the two alpha helices tightly associated by two disulfide bonds. Based on our findings, we conclude that unlike the well-studied ribosome-inactivating proteins, which exert their action through N-glycosidase activities, Luffin P1 demonstrates a novel inactivation mechanism probably through the charge complementation with viral or cellular proteins. Our work also provides a new scaffold for the design of novel inhibitors from a simple helical motif. © 2010 Elsevier Inc.
Persistent Identifierhttp://hdl.handle.net/10722/133607
ISSN
2015 Impact Factor: 2.57
2015 SCImago Journal Rankings: 3.561
ISI Accession Number ID
Funding AgencyGrant Number
Research Grants CouncilHKU 7533/06M
7755/08M
CUHK 4606/06M
Chinese University of Hong Kong
University Grants Council of Hong Kong SARSEG CUHKO8
CUHKO9
National Basic Research Program of China2009CB5223006
Eleventh Five-Year Key Scientific and Technological Program of China2009ZX09501-029
2008ZX10001-002
2008ZX10001-015
Chinese Academy of SciencesKSCX2-YW-R-185
Funding Information:

The work in Hong Kong was supported by grants from the Research Grants Council General Research Grant (HKU 7533/06M and 7755/08M for KH Sze and CUHK 4606/06M for PC Shaw). Yinghua Yang was supported in part by a postdoctoral fellowship from the Chinese University of Hong Kong. The purchase of the 700 MHz nuclear magnetic spectrometer was by a One-Off Special Equipment Grant (SEG CUHKO8 and CUHKO9) of the University Grants Council of Hong Kong SAR. The work in China was supported in part by grants from the National Basic Research Program of China (2009CB5223006), Eleventh Five-Year Key Scientific and Technological Program of China (2009ZX09501-029; 2008ZX10001-002, 2008ZX10001-015), Chinese Academy of Sciences (KSCX2-YW-R-185).

References
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DC FieldValueLanguage
dc.contributor.authorNg, YMen_HK
dc.contributor.authorYang, Yen_HK
dc.contributor.authorSze, KHen_HK
dc.contributor.authorZhang, Xen_HK
dc.contributor.authorZheng, YTen_HK
dc.contributor.authorShaw, PCen_HK
dc.date.accessioned2011-05-24T02:11:41Z-
dc.date.available2011-05-24T02:11:41Z-
dc.date.issued2011en_HK
dc.identifier.citationJournal Of Structural Biology, 2011, v. 174 n. 1, p. 164-172en_HK
dc.identifier.issn1047-8477en_HK
dc.identifier.urihttp://hdl.handle.net/10722/133607-
dc.description.abstractLuffin P1, the smallest ribosome-inactivating peptide from the seeds of Luffa cylindrica was found to have anti-HIV-1 activity in HIV-1 infected C8166 T-cell lines and be able to bind with HIV Rev Response Element. Nuclear magnetic resonance spectroscopy revealed that the Luffin P1 comprises a helix-loop-helix motif, with the two alpha helices tightly associated by two disulfide bonds. Based on our findings, we conclude that unlike the well-studied ribosome-inactivating proteins, which exert their action through N-glycosidase activities, Luffin P1 demonstrates a novel inactivation mechanism probably through the charge complementation with viral or cellular proteins. Our work also provides a new scaffold for the design of novel inhibitors from a simple helical motif. © 2010 Elsevier Inc.en_HK
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yjsbien_HK
dc.relation.ispartofJournal of Structural Biologyen_HK
dc.rightsAppropriate Bibliographic Citation:Authors posting Accepted Author Manuscript online should later add a citation for the Published Journal Article indicating that the Article was subsequently published, and may mention the journal title provided that they add the following text at the beginning of the document: “NOTICE: this is the author’s version of a work that was accepted for publication in <Journal title>. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in PUBLICATION, [VOL#, ISSUE#, (DATE)] DOI#”-
dc.subjectAnti-HIV-1en_HK
dc.subjectLuffin P1en_HK
dc.subjectNuclear magnetic resonanceen_HK
dc.subjectRibosome-inactivating peptideen_HK
dc.subject.meshAnti-HIV Agents - chemistry - pharmacology-
dc.subject.meshCircular Dichroism-
dc.subject.meshLuffa - chemistry-
dc.subject.meshPeptides - chemistry - pharmacology-
dc.subject.meshSeeds - chemistry-
dc.titleStructural characterization and anti-HIV-1 activities of arginine/glutamate-rich polypeptide Luffin P1 from the seeds of sponge gourd (Luffa cylindrica)en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1047-8477&volume=174&issue=1&spage=164&epage=172&date=2011&atitle=Structural+characterization+and+anti-HIV-1+activities+of+arginine/glutamate-rich+polypeptide+Luffin+P1+from+the+seeds+of+sponge+gourd+(Luffa+cylindrica)-
dc.identifier.emailSze, KH:khsze@hku.hken_HK
dc.identifier.authoritySze, KH=rp00785en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jsb.2010.12.007en_HK
dc.identifier.pmid21195767-
dc.identifier.scopuseid_2-s2.0-79952450056en_HK
dc.identifier.hkuros185371en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79952450056&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume174en_HK
dc.identifier.issue1en_HK
dc.identifier.spage164en_HK
dc.identifier.epage172en_HK
dc.identifier.isiWOS:000288640100019-
dc.publisher.placeUnited Statesen_HK
dc.relation.projectStructural and functional studies of the SWIRM domain in Lysine-specific Demethylase 1 (LSD1)-
dc.identifier.scopusauthoridNg, YM=42462197300en_HK
dc.identifier.scopusauthoridYang, Y=35750932800en_HK
dc.identifier.scopusauthoridSze, KH=7006735061en_HK
dc.identifier.scopusauthoridZhang, X=36062136800en_HK
dc.identifier.scopusauthoridZheng, YT=35228297300en_HK
dc.identifier.scopusauthoridShaw, PC=35599523600en_HK
dc.identifier.citeulike8625089-

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