A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection
Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection. Other endogenous or exogenous factors present during sexual intercourse have also been reported to promote the formation of...
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| creator | Chen, Jinquan Ren, Ruxia Tan, Suiyi Zhang, Wanyue Zhang, Xuanxuan Yu, Fei Xun, Tianrong Jiang, Shibo Liu, Shuwen Li, Lin |
| description | Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection. Other endogenous or exogenous factors present during sexual intercourse have also been reported to promote the formation of seminal amyloid fibrils.
Here, we demonstrated that a synthetic 15-residue peptide derived from the HIV-1 gp120 coreceptor-binding region, designated enhancing peptide 2 (EP2), can rapidly self-assemble into nanofibers. These EP2-derivated nanofibers promptly accelerated the formation of semen amyloid fibrils by PAP248-286, as shown by Thioflavin T (ThT) and Congo red assays. The amyloid fibrils presented similar morphology, assessed via transmission electron microscopy (TEM), in the presence or absence of EP2. Circular dichroism (CD) spectroscopy revealed that EP2 accelerates PAP248-286 amyloid fibril formation by promoting the structural transition of PAP248-286 from a random coil into a cross-β-sheet. Newly formed semen amyloid fibrils effectively enhanced HIV-1 infection in TZM-bl cells and U87 cells by promoting the binding of HIV-1 virions to target cells.
Nanofibers composed of EP2 promote the formation of PAP248-286 amyloid fibrils and enhance HIV-1 infection. |
| doi_str_mv | 10.1371/journal.pone.0144522 |
| format | Article |
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Here, we demonstrated that a synthetic 15-residue peptide derived from the HIV-1 gp120 coreceptor-binding region, designated enhancing peptide 2 (EP2), can rapidly self-assemble into nanofibers. These EP2-derivated nanofibers promptly accelerated the formation of semen amyloid fibrils by PAP248-286, as shown by Thioflavin T (ThT) and Congo red assays. The amyloid fibrils presented similar morphology, assessed via transmission electron microscopy (TEM), in the presence or absence of EP2. Circular dichroism (CD) spectroscopy revealed that EP2 accelerates PAP248-286 amyloid fibril formation by promoting the structural transition of PAP248-286 from a random coil into a cross-β-sheet. Newly formed semen amyloid fibrils effectively enhanced HIV-1 infection in TZM-bl cells and U87 cells by promoting the binding of HIV-1 virions to target cells.
Nanofibers composed of EP2 promote the formation of PAP248-286 amyloid fibrils and enhance HIV-1 infection.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0144522</identifier><identifier>PMID: 26656730</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Acid phosphatase ; Acid Phosphatase - metabolism ; Acquired immune deficiency syndrome ; AIDS ; Amyloid - metabolism ; Binding ; Binding sites (Biochemistry) ; Cell Line ; Circular dichroism ; Development and progression ; Dichroism ; Disease transmission ; Electron microscopy ; Fibrillogenesis ; Glycoprotein gp120 ; Glycoproteins ; Health aspects ; HIV ; HIV Envelope Protein gp120 - metabolism ; HIV infections ; HIV Infections - pathology ; HIV-1 - metabolism ; Human immunodeficiency virus ; Humans ; Infections ; Molecular structure ; Nanofibers ; Peptides ; Peptides - metabolism ; Plasmids ; Protein Aggregation, Pathological - physiopathology ; Protein Structure, Tertiary ; Random coil ; Semen ; Sexual behavior ; Sexual intercourse ; Sexually transmitted diseases ; Spectroscopy ; STD ; Transmission electron microscopy ; Virions</subject><ispartof>PloS one, 2015-12, Vol.10 (12), p.e0144522-e0144522</ispartof><rights>COPYRIGHT 2015 Public Library of Science</rights><rights>2015 Chen et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2015 Chen et al 2015 Chen et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c762t-656824545d72ec7014cd0116f4c5169431235c1af6fe7037a471b47ba8860b4f3</citedby><cites>FETCH-LOGICAL-c762t-656824545d72ec7014cd0116f4c5169431235c1af6fe7037a471b47ba8860b4f3</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/PMC4687630/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4687630/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23864,27922,27923,53789,53791,79370,79371</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26656730$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Baskakov, Ilia V</contributor><creatorcontrib>Chen, Jinquan</creatorcontrib><creatorcontrib>Ren, Ruxia</creatorcontrib><creatorcontrib>Tan, Suiyi</creatorcontrib><creatorcontrib>Zhang, Wanyue</creatorcontrib><creatorcontrib>Zhang, Xuanxuan</creatorcontrib><creatorcontrib>Yu, Fei</creatorcontrib><creatorcontrib>Xun, Tianrong</creatorcontrib><creatorcontrib>Jiang, Shibo</creatorcontrib><creatorcontrib>Liu, Shuwen</creatorcontrib><creatorcontrib>Li, Lin</creatorcontrib><title>A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection. Other endogenous or exogenous factors present during sexual intercourse have also been reported to promote the formation of seminal amyloid fibrils.
Here, we demonstrated that a synthetic 15-residue peptide derived from the HIV-1 gp120 coreceptor-binding region, designated enhancing peptide 2 (EP2), can rapidly self-assemble into nanofibers. These EP2-derivated nanofibers promptly accelerated the formation of semen amyloid fibrils by PAP248-286, as shown by Thioflavin T (ThT) and Congo red assays. The amyloid fibrils presented similar morphology, assessed via transmission electron microscopy (TEM), in the presence or absence of EP2. Circular dichroism (CD) spectroscopy revealed that EP2 accelerates PAP248-286 amyloid fibril formation by promoting the structural transition of PAP248-286 from a random coil into a cross-β-sheet. Newly formed semen amyloid fibrils effectively enhanced HIV-1 infection in TZM-bl cells and U87 cells by promoting the binding of HIV-1 virions to target cells.
Nanofibers composed of EP2 promote the formation of PAP248-286 amyloid fibrils and enhance HIV-1 infection.</description><subject>Acid phosphatase</subject><subject>Acid Phosphatase - metabolism</subject><subject>Acquired immune deficiency syndrome</subject><subject>AIDS</subject><subject>Amyloid - metabolism</subject><subject>Binding</subject><subject>Binding sites (Biochemistry)</subject><subject>Cell Line</subject><subject>Circular dichroism</subject><subject>Development and progression</subject><subject>Dichroism</subject><subject>Disease transmission</subject><subject>Electron microscopy</subject><subject>Fibrillogenesis</subject><subject>Glycoprotein gp120</subject><subject>Glycoproteins</subject><subject>Health aspects</subject><subject>HIV</subject><subject>HIV Envelope Protein gp120 - metabolism</subject><subject>HIV infections</subject><subject>HIV Infections - pathology</subject><subject>HIV-1 - metabolism</subject><subject>Human immunodeficiency virus</subject><subject>Humans</subject><subject>Infections</subject><subject>Molecular structure</subject><subject>Nanofibers</subject><subject>Peptides</subject><subject>Peptides - metabolism</subject><subject>Plasmids</subject><subject>Protein Aggregation, Pathological - physiopathology</subject><subject>Protein Structure, Tertiary</subject><subject>Random coil</subject><subject>Semen</subject><subject>Sexual behavior</subject><subject>Sexual intercourse</subject><subject>Sexually transmitted diseases</subject><subject>Spectroscopy</subject><subject>STD</subject><subject>Transmission electron microscopy</subject><subject>Virions</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>DOA</sourceid><recordid>eNqNk99u0zAUxiMEYmPwBggsISG4SPG_OOkNUikrqzRp1YDdWo7jpK4Su7Odib0DD41D06lFuyC5SHT8-77jc-yTJK8RnCCSo08b2zsj2snWGjWBiNIM4yfJKZoSnDIMydOD_5PkhfcbCDNSMPY8OcGMZSwn8DT5PQMrtQ26UuCrcvpOVaB2tgNhrcDF8iZFoNkiDMHcOiUjaF36RZtKmwZcq0ZbA1YRt0F5sLCuE2EI2RqsZitMixQXDMy6-9bqCix06XTrQbDg3KyFkfsMS1MrOQhfJs9q0Xr1avyeJT8X5z_mF-nl1bflfHaZypzhkMa9F5hmNKtyrGQea5cVRIjVVGaITSlBmGQSiZrVKockFzRHJc1LURQMlrQmZ8nbne-2tZ6PjfQc5bQosgJPSSSWO6KyYsO3TnfC3XMrNP8bsK7hwgUtW8WxQHTKZCkZhZRCXEosJStoJRmqajGNXp_HbH3ZqUoqE5xoj0yPV4xe88beccqKnBEYDT6MBs7e9soH3mkvVdsKo2w_7DuD8SFwQN_9gz5e3Ug1IhagTW1jXjmY8hklOWUM4sFr8ggV30p1WsZbV-sYPxJ8PBJEJqhfoRG993z5_fr_2aubY_b9AbtWog1rb9t-uDL-GKQ7UDrrvVP1Q5MR5MPQ7LvBh6Hh49BE2ZvDA3oQ7aeE_AGZIw1Z</recordid><startdate>20151214</startdate><enddate>20151214</enddate><creator>Chen, Jinquan</creator><creator>Ren, Ruxia</creator><creator>Tan, Suiyi</creator><creator>Zhang, Wanyue</creator><creator>Zhang, Xuanxuan</creator><creator>Yu, Fei</creator><creator>Xun, Tianrong</creator><creator>Jiang, Shibo</creator><creator>Liu, Shuwen</creator><creator>Li, Lin</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20151214</creationdate><title>A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection</title><author>Chen, Jinquan ; Ren, Ruxia ; Tan, Suiyi ; Zhang, Wanyue ; Zhang, Xuanxuan ; Yu, Fei ; Xun, Tianrong ; Jiang, Shibo ; Liu, Shuwen ; Li, Lin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c762t-656824545d72ec7014cd0116f4c5169431235c1af6fe7037a471b47ba8860b4f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Acid phosphatase</topic><topic>Acid Phosphatase - metabolism</topic><topic>Acquired immune deficiency syndrome</topic><topic>AIDS</topic><topic>Amyloid - metabolism</topic><topic>Binding</topic><topic>Binding sites (Biochemistry)</topic><topic>Cell Line</topic><topic>Circular dichroism</topic><topic>Development and progression</topic><topic>Dichroism</topic><topic>Disease transmission</topic><topic>Electron microscopy</topic><topic>Fibrillogenesis</topic><topic>Glycoprotein gp120</topic><topic>Glycoproteins</topic><topic>Health aspects</topic><topic>HIV</topic><topic>HIV Envelope Protein gp120 - metabolism</topic><topic>HIV infections</topic><topic>HIV Infections - pathology</topic><topic>HIV-1 - metabolism</topic><topic>Human immunodeficiency virus</topic><topic>Humans</topic><topic>Infections</topic><topic>Molecular structure</topic><topic>Nanofibers</topic><topic>Peptides</topic><topic>Peptides - metabolism</topic><topic>Plasmids</topic><topic>Protein Aggregation, Pathological - physiopathology</topic><topic>Protein Structure, Tertiary</topic><topic>Random coil</topic><topic>Semen</topic><topic>Sexual behavior</topic><topic>Sexual intercourse</topic><topic>Sexually transmitted diseases</topic><topic>Spectroscopy</topic><topic>STD</topic><topic>Transmission electron microscopy</topic><topic>Virions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Jinquan</creatorcontrib><creatorcontrib>Ren, Ruxia</creatorcontrib><creatorcontrib>Tan, Suiyi</creatorcontrib><creatorcontrib>Zhang, Wanyue</creatorcontrib><creatorcontrib>Zhang, Xuanxuan</creatorcontrib><creatorcontrib>Yu, Fei</creatorcontrib><creatorcontrib>Xun, Tianrong</creatorcontrib><creatorcontrib>Jiang, Shibo</creatorcontrib><creatorcontrib>Liu, Shuwen</creatorcontrib><creatorcontrib>Li, Lin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Jinquan</au><au>Ren, Ruxia</au><au>Tan, Suiyi</au><au>Zhang, Wanyue</au><au>Zhang, Xuanxuan</au><au>Yu, Fei</au><au>Xun, Tianrong</au><au>Jiang, Shibo</au><au>Liu, Shuwen</au><au>Li, Lin</au><au>Baskakov, Ilia V</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2015-12-14</date><risdate>2015</risdate><volume>10</volume><issue>12</issue><spage>e0144522</spage><epage>e0144522</epage><pages>e0144522-e0144522</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Semen is a major vehicle for HIV transmission. Prostatic acid phosphatase (PAP) fragments, such as PAP248-286, in human semen can form amyloid fibrils to enhance HIV infection. Other endogenous or exogenous factors present during sexual intercourse have also been reported to promote the formation of seminal amyloid fibrils.
Here, we demonstrated that a synthetic 15-residue peptide derived from the HIV-1 gp120 coreceptor-binding region, designated enhancing peptide 2 (EP2), can rapidly self-assemble into nanofibers. These EP2-derivated nanofibers promptly accelerated the formation of semen amyloid fibrils by PAP248-286, as shown by Thioflavin T (ThT) and Congo red assays. The amyloid fibrils presented similar morphology, assessed via transmission electron microscopy (TEM), in the presence or absence of EP2. Circular dichroism (CD) spectroscopy revealed that EP2 accelerates PAP248-286 amyloid fibril formation by promoting the structural transition of PAP248-286 from a random coil into a cross-β-sheet. Newly formed semen amyloid fibrils effectively enhanced HIV-1 infection in TZM-bl cells and U87 cells by promoting the binding of HIV-1 virions to target cells.
Nanofibers composed of EP2 promote the formation of PAP248-286 amyloid fibrils and enhance HIV-1 infection.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>26656730</pmid><doi>10.1371/journal.pone.0144522</doi><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Public Library of Science (PLoS) Journals Open Access; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Acid phosphatase Acid Phosphatase - metabolism Acquired immune deficiency syndrome AIDS Amyloid - metabolism Binding Binding sites (Biochemistry) Cell Line Circular dichroism Development and progression Dichroism Disease transmission Electron microscopy Fibrillogenesis Glycoprotein gp120 Glycoproteins Health aspects HIV HIV Envelope Protein gp120 - metabolism HIV infections HIV Infections - pathology HIV-1 - metabolism Human immunodeficiency virus Humans Infections Molecular structure Nanofibers Peptides Peptides - metabolism Plasmids Protein Aggregation, Pathological - physiopathology Protein Structure, Tertiary Random coil Semen Sexual behavior Sexual intercourse Sexually transmitted diseases Spectroscopy STD Transmission electron microscopy Virions |
| title | A Peptide Derived from the HIV-1 gp120 Coreceptor-Binding Region Promotes Formation of PAP248-286 Amyloid Fibrils to Enhance HIV-1 Infection |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T09%3A14%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20Peptide%20Derived%20from%20the%20HIV-1%20gp120%20Coreceptor-Binding%20Region%20Promotes%20Formation%20of%20PAP248-286%20Amyloid%20Fibrils%20to%20Enhance%20HIV-1%20Infection&rft.jtitle=PloS%20one&rft.au=Chen,%20Jinquan&rft.date=2015-12-14&rft.volume=10&rft.issue=12&rft.spage=e0144522&rft.epage=e0144522&rft.pages=e0144522-e0144522&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0144522&rft_dat=%3Cgale_plos_%3EA437466020%3C/gale_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1748858293&rft_id=info:pmid/26656730&rft_galeid=A437466020&rft_doaj_id=oai_doaj_org_article_2a1496cbc6404402bc2cc684dc61dfa9&rfr_iscdi=true |