A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
The Nipah virus fusion (F) protein is proteolytically processed to F1 + F2 subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced i...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2006-03, Vol.346 (2), p.251-257 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Pager, Cara Theresia Craft, Willie Warren Patch, Jared Dutch, Rebecca Ellis |
| description | The Nipah virus fusion (F) protein is proteolytically processed to F1 + F2 subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form. |
| doi_str_mv | 10.1016/j.virol.2006.01.007 |
| format | Article |
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We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2006.01.007</identifier><identifier>PMID: 16460775</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cathepsin B - metabolism ; Cathepsin L ; cathepsins ; Cathepsins - antagonists & inhibitors ; Cathepsins - metabolism ; Cell Fusion ; Chlorocebus aethiops ; Cricetinae ; Cysteine Endopeptidases - metabolism ; endosomes ; Enzyme Inhibitors - pharmacology ; Fusion protein ; Gene Silencing ; human health ; Nipah ; Nipah virus ; Nipah Virus - physiology ; Paramyxoviridae ; Protein Processing, Post-Translational ; proteolysis ; Proteolytic processing ; swine diseases ; Vero Cells ; viral fusion proteins ; Viral Fusion Proteins - metabolism</subject><ispartof>Virology (New York, N.Y.), 2006-03, Vol.346 (2), p.251-257</ispartof><rights>2006 Elsevier Inc.</rights><rights>Copyright © 2006 Elsevier Inc. All rights reserved. 2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4277-8da76cf43a2c807272fa107faf32d4610224c6a972456ecd0652665d288b49393</citedby><cites>FETCH-LOGICAL-c4277-8da76cf43a2c807272fa107faf32d4610224c6a972456ecd0652665d288b49393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0042682206000122$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16460775$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pager, Cara Theresia</creatorcontrib><creatorcontrib>Craft, Willie Warren</creatorcontrib><creatorcontrib>Patch, Jared</creatorcontrib><creatorcontrib>Dutch, Rebecca Ellis</creatorcontrib><title>A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>The Nipah virus fusion (F) protein is proteolytically processed to F1 + F2 subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form.</description><subject>Animals</subject><subject>Cathepsin B - metabolism</subject><subject>Cathepsin L</subject><subject>cathepsins</subject><subject>Cathepsins - antagonists & inhibitors</subject><subject>Cathepsins - metabolism</subject><subject>Cell Fusion</subject><subject>Chlorocebus aethiops</subject><subject>Cricetinae</subject><subject>Cysteine Endopeptidases - metabolism</subject><subject>endosomes</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Fusion protein</subject><subject>Gene Silencing</subject><subject>human health</subject><subject>Nipah</subject><subject>Nipah virus</subject><subject>Nipah Virus - physiology</subject><subject>Paramyxoviridae</subject><subject>Protein Processing, Post-Translational</subject><subject>proteolysis</subject><subject>Proteolytic processing</subject><subject>swine diseases</subject><subject>Vero Cells</subject><subject>viral fusion proteins</subject><subject>Viral Fusion Proteins - metabolism</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUuP0zAUhS0EYsrAL0ACr2aXcO04drIAaTTiJVWwgFlbrnPdukrijp1U6r_HJRWPDazsa3_n3GsfQl4yKBkw-WZfHn0MfckBZAmsBFCPyIpBKwuoBHtMVgCCF7Lh_Io8S2kPuVYKnpIrJoUEpeoV6W_pYKY5IjVjR92cwhZHb6kLcaDB0WmH9Is_mB3NzeZ0JnwY6SGGCf1IIz7MPmJaDkJ_mrI27y2m5Mct3ZyoNdnjkCu6fk6eONMnfHFZr8n9h_ff7z4V668fP9_drgsruFJF0xklrROV4bYBxRV3hoFyxlW8E5IB58JK0youaom2A1lzKeuON81GtFVbXZN3i-9h3gzYWRynaHp9iH4w8aSD8frvm9Hv9DYctWKMKVFlg5uLQQwPM6ZJDz5Z7HszYpiTlkqJuhX8vyBTDGROI4PVAtoYUorofk3DQJ_j1Hv9M059jlMD0znOrHr150N-ay75ZeD1AjgTtNlGn_T9Nw6syuqGccUy8XYhMH_40WPUyXocLXY5NzvpLvh_jvAD4i687A</recordid><startdate>20060315</startdate><enddate>20060315</enddate><creator>Pager, Cara Theresia</creator><creator>Craft, Willie Warren</creator><creator>Patch, Jared</creator><creator>Dutch, Rebecca Ellis</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20060315</creationdate><title>A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L</title><author>Pager, Cara Theresia ; Craft, Willie Warren ; Patch, Jared ; Dutch, Rebecca Ellis</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4277-8da76cf43a2c807272fa107faf32d4610224c6a972456ecd0652665d288b49393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Cathepsin B - metabolism</topic><topic>Cathepsin L</topic><topic>cathepsins</topic><topic>Cathepsins - antagonists & inhibitors</topic><topic>Cathepsins - metabolism</topic><topic>Cell Fusion</topic><topic>Chlorocebus aethiops</topic><topic>Cricetinae</topic><topic>Cysteine Endopeptidases - metabolism</topic><topic>endosomes</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Fusion protein</topic><topic>Gene Silencing</topic><topic>human health</topic><topic>Nipah</topic><topic>Nipah virus</topic><topic>Nipah Virus - physiology</topic><topic>Paramyxoviridae</topic><topic>Protein Processing, Post-Translational</topic><topic>proteolysis</topic><topic>Proteolytic processing</topic><topic>swine diseases</topic><topic>Vero Cells</topic><topic>viral fusion proteins</topic><topic>Viral Fusion Proteins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pager, Cara Theresia</creatorcontrib><creatorcontrib>Craft, Willie Warren</creatorcontrib><creatorcontrib>Patch, Jared</creatorcontrib><creatorcontrib>Dutch, Rebecca Ellis</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pager, Cara Theresia</au><au>Craft, Willie Warren</au><au>Patch, Jared</au><au>Dutch, Rebecca Ellis</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2006-03-15</date><risdate>2006</risdate><volume>346</volume><issue>2</issue><spage>251</spage><epage>257</epage><pages>251-257</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>The Nipah virus fusion (F) protein is proteolytically processed to F1 + F2 subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16460775</pmid><doi>10.1016/j.virol.2006.01.007</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 2006-03, Vol.346 (2), p.251-257 |
| issn | 0042-6822 1096-0341 |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present); Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Cathepsin B - metabolism Cathepsin L cathepsins Cathepsins - antagonists & inhibitors Cathepsins - metabolism Cell Fusion Chlorocebus aethiops Cricetinae Cysteine Endopeptidases - metabolism endosomes Enzyme Inhibitors - pharmacology Fusion protein Gene Silencing human health Nipah Nipah virus Nipah Virus - physiology Paramyxoviridae Protein Processing, Post-Translational proteolysis Proteolytic processing swine diseases Vero Cells viral fusion proteins Viral Fusion Proteins - metabolism |
| title | A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L |
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