Loading…
The C-terminal region of the Turnip mosaic virus P3 protein is essential for viral infection via targeting P3 to the viral replication complex
Like other positive-strand RNA viruses, plant potyviruses assemble viral replication complexes (VRCs) on modified cellular membranes. Potyviruses encode two membrane proteins, 6K2 and P3. The former is known to play pivotal roles in the formation of membrane-associated VRCs. However, P3 remains to b...
Saved in:
Published in: | Virology (New York, N.Y.) N.Y.), 2017-10, Vol.510, p.147-155 |
---|---|
Main Authors: | , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | cdi_FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023 |
---|---|
cites | cdi_FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023 |
container_end_page | 155 |
container_issue | |
container_start_page | 147 |
container_title | Virology (New York, N.Y.) |
container_volume | 510 |
creator | Cui, Xiaoyan Yaghmaiean, Hoda Wu, Guanwei Wu, Xiaoyun Chen, Xin Thorn, Greg Wang, Aiming |
description | Like other positive-strand RNA viruses, plant potyviruses assemble viral replication complexes (VRCs) on modified cellular membranes. Potyviruses encode two membrane proteins, 6K2 and P3. The former is known to play pivotal roles in the formation of membrane-associated VRCs. However, P3 remains to be one of the least characterized potyviral proteins. The P3 cistron codes for P3 as well as P3N-PIPO which results from RNA polymerase slippage. In this study, we show that the P3N-PIPO of Turnip mosaic virus (TuMV) is required for viral cell-to-cell movement but not for viral replication. We demonstrate that the C-terminal region of P3 (P3C) is indispensable for P3 to form cytoplasmic punctate inclusions and target VRCs. We reveal that TuMV mutants that lack P3C are replication-defective. Taken together, these data suggest that the P3 cistron has two distinct functions: P3N-PIPO as a dedicated movement protein and P3 as an essential component of the VRC.
•The potyviarl P3 coding region encodes P3 and P3N-PIPO.•P3N-PIPO is not required for viral replication and is a dedicated movement protein.•P3 forms punctate structures that colocalize with viral replication complexes (VRC).•The C-terminal region of P3 (P3C) is required for P3 to target the VRC.•P3 is a component of the VRC and is essential for viral genome replication. |
doi_str_mv | 10.1016/j.virol.2017.07.016 |
format | article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1923111689</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0042682217302350</els_id><sourcerecordid>1923111689</sourcerecordid><originalsourceid>FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023</originalsourceid><addsrcrecordid>eNp9kcuOEzEQRS0EYsLMfAES8pJNBz_64V6wQBGPkUaaWYS15TjlUFG33djuaPgJvhl3MrBEKsm2fO69qipC3nK25oy3H47rE8YwrAXj3ZqV4u0LsuKsbysma_6SrBirRdUqIa7Im5SOrLy7jr0mV0J1suG8WZHf2x9AN1WGOKI3A41wwOBpcDSXj-0cPU50DMmgpSVuTvRR0imGDOgpJgopgc9YlC7EhSg39A5sXmxOaGg28QAZ_WFR5nD2vXARpgGtOZM2jNMATzfklTNDgtvn85p8__J5u_lW3T98vdt8uq9sLZpcCSkE74WSzgnbmVoxB7LnrPS1E-1OCVfX0kEjQFnDnFNS7hvRSOWs6i0T8pq8v_iWVn7OkLIeMVkYBuMhzEkXc8k5b1VfUHlBbQwpRXB6ijia-EtzppdF6KM-L0Ivi9CsFG-L6t1zwLwbYf9P83fyBfh4AaC0eUKIOlkEb2GPsUxP7wP-N-APW0Cb3w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1923111689</pqid></control><display><type>article</type><title>The C-terminal region of the Turnip mosaic virus P3 protein is essential for viral infection via targeting P3 to the viral replication complex</title><source>Elsevier</source><creator>Cui, Xiaoyan ; Yaghmaiean, Hoda ; Wu, Guanwei ; Wu, Xiaoyun ; Chen, Xin ; Thorn, Greg ; Wang, Aiming</creator><creatorcontrib>Cui, Xiaoyan ; Yaghmaiean, Hoda ; Wu, Guanwei ; Wu, Xiaoyun ; Chen, Xin ; Thorn, Greg ; Wang, Aiming</creatorcontrib><description>Like other positive-strand RNA viruses, plant potyviruses assemble viral replication complexes (VRCs) on modified cellular membranes. Potyviruses encode two membrane proteins, 6K2 and P3. The former is known to play pivotal roles in the formation of membrane-associated VRCs. However, P3 remains to be one of the least characterized potyviral proteins. The P3 cistron codes for P3 as well as P3N-PIPO which results from RNA polymerase slippage. In this study, we show that the P3N-PIPO of Turnip mosaic virus (TuMV) is required for viral cell-to-cell movement but not for viral replication. We demonstrate that the C-terminal region of P3 (P3C) is indispensable for P3 to form cytoplasmic punctate inclusions and target VRCs. We reveal that TuMV mutants that lack P3C are replication-defective. Taken together, these data suggest that the P3 cistron has two distinct functions: P3N-PIPO as a dedicated movement protein and P3 as an essential component of the VRC.
•The potyviarl P3 coding region encodes P3 and P3N-PIPO.•P3N-PIPO is not required for viral replication and is a dedicated movement protein.•P3 forms punctate structures that colocalize with viral replication complexes (VRC).•The C-terminal region of P3 (P3C) is required for P3 to target the VRC.•P3 is a component of the VRC and is essential for viral genome replication.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2017.07.016</identifier><identifier>PMID: 28735115</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cell-to-cell movement ; DNA Mutational Analysis ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Movement protein ; Nicotiana ; P3N-PIPO ; Plant RNA virus ; Plant Viral Movement Proteins - genetics ; Plant Viral Movement Proteins - metabolism ; Potyvirus ; Potyvirus - physiology ; Punctate inclusion ; Turnip mosaic virus ; Viral Proteins - genetics ; Viral Proteins - metabolism ; Virus Release ; Virus Replication ; Virus replication complex</subject><ispartof>Virology (New York, N.Y.), 2017-10, Vol.510, p.147-155</ispartof><rights>2017</rights><rights>Crown Copyright © 2017. Published by Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023</citedby><cites>FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28735115$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cui, Xiaoyan</creatorcontrib><creatorcontrib>Yaghmaiean, Hoda</creatorcontrib><creatorcontrib>Wu, Guanwei</creatorcontrib><creatorcontrib>Wu, Xiaoyun</creatorcontrib><creatorcontrib>Chen, Xin</creatorcontrib><creatorcontrib>Thorn, Greg</creatorcontrib><creatorcontrib>Wang, Aiming</creatorcontrib><title>The C-terminal region of the Turnip mosaic virus P3 protein is essential for viral infection via targeting P3 to the viral replication complex</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Like other positive-strand RNA viruses, plant potyviruses assemble viral replication complexes (VRCs) on modified cellular membranes. Potyviruses encode two membrane proteins, 6K2 and P3. The former is known to play pivotal roles in the formation of membrane-associated VRCs. However, P3 remains to be one of the least characterized potyviral proteins. The P3 cistron codes for P3 as well as P3N-PIPO which results from RNA polymerase slippage. In this study, we show that the P3N-PIPO of Turnip mosaic virus (TuMV) is required for viral cell-to-cell movement but not for viral replication. We demonstrate that the C-terminal region of P3 (P3C) is indispensable for P3 to form cytoplasmic punctate inclusions and target VRCs. We reveal that TuMV mutants that lack P3C are replication-defective. Taken together, these data suggest that the P3 cistron has two distinct functions: P3N-PIPO as a dedicated movement protein and P3 as an essential component of the VRC.
•The potyviarl P3 coding region encodes P3 and P3N-PIPO.•P3N-PIPO is not required for viral replication and is a dedicated movement protein.•P3 forms punctate structures that colocalize with viral replication complexes (VRC).•The C-terminal region of P3 (P3C) is required for P3 to target the VRC.•P3 is a component of the VRC and is essential for viral genome replication.</description><subject>Cell-to-cell movement</subject><subject>DNA Mutational Analysis</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Movement protein</subject><subject>Nicotiana</subject><subject>P3N-PIPO</subject><subject>Plant RNA virus</subject><subject>Plant Viral Movement Proteins - genetics</subject><subject>Plant Viral Movement Proteins - metabolism</subject><subject>Potyvirus</subject><subject>Potyvirus - physiology</subject><subject>Punctate inclusion</subject><subject>Turnip mosaic virus</subject><subject>Viral Proteins - genetics</subject><subject>Viral Proteins - metabolism</subject><subject>Virus Release</subject><subject>Virus Replication</subject><subject>Virus replication complex</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNp9kcuOEzEQRS0EYsLMfAES8pJNBz_64V6wQBGPkUaaWYS15TjlUFG33djuaPgJvhl3MrBEKsm2fO69qipC3nK25oy3H47rE8YwrAXj3ZqV4u0LsuKsbysma_6SrBirRdUqIa7Im5SOrLy7jr0mV0J1suG8WZHf2x9AN1WGOKI3A41wwOBpcDSXj-0cPU50DMmgpSVuTvRR0imGDOgpJgopgc9YlC7EhSg39A5sXmxOaGg28QAZ_WFR5nD2vXARpgGtOZM2jNMATzfklTNDgtvn85p8__J5u_lW3T98vdt8uq9sLZpcCSkE74WSzgnbmVoxB7LnrPS1E-1OCVfX0kEjQFnDnFNS7hvRSOWs6i0T8pq8v_iWVn7OkLIeMVkYBuMhzEkXc8k5b1VfUHlBbQwpRXB6ijia-EtzppdF6KM-L0Ivi9CsFG-L6t1zwLwbYf9P83fyBfh4AaC0eUKIOlkEb2GPsUxP7wP-N-APW0Cb3w</recordid><startdate>201710</startdate><enddate>201710</enddate><creator>Cui, Xiaoyan</creator><creator>Yaghmaiean, Hoda</creator><creator>Wu, Guanwei</creator><creator>Wu, Xiaoyun</creator><creator>Chen, Xin</creator><creator>Thorn, Greg</creator><creator>Wang, Aiming</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>201710</creationdate><title>The C-terminal region of the Turnip mosaic virus P3 protein is essential for viral infection via targeting P3 to the viral replication complex</title><author>Cui, Xiaoyan ; Yaghmaiean, Hoda ; Wu, Guanwei ; Wu, Xiaoyun ; Chen, Xin ; Thorn, Greg ; Wang, Aiming</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Cell-to-cell movement</topic><topic>DNA Mutational Analysis</topic><topic>Membrane Proteins - genetics</topic><topic>Membrane Proteins - metabolism</topic><topic>Movement protein</topic><topic>Nicotiana</topic><topic>P3N-PIPO</topic><topic>Plant RNA virus</topic><topic>Plant Viral Movement Proteins - genetics</topic><topic>Plant Viral Movement Proteins - metabolism</topic><topic>Potyvirus</topic><topic>Potyvirus - physiology</topic><topic>Punctate inclusion</topic><topic>Turnip mosaic virus</topic><topic>Viral Proteins - genetics</topic><topic>Viral Proteins - metabolism</topic><topic>Virus Release</topic><topic>Virus Replication</topic><topic>Virus replication complex</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cui, Xiaoyan</creatorcontrib><creatorcontrib>Yaghmaiean, Hoda</creatorcontrib><creatorcontrib>Wu, Guanwei</creatorcontrib><creatorcontrib>Wu, Xiaoyun</creatorcontrib><creatorcontrib>Chen, Xin</creatorcontrib><creatorcontrib>Thorn, Greg</creatorcontrib><creatorcontrib>Wang, Aiming</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cui, Xiaoyan</au><au>Yaghmaiean, Hoda</au><au>Wu, Guanwei</au><au>Wu, Xiaoyun</au><au>Chen, Xin</au><au>Thorn, Greg</au><au>Wang, Aiming</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The C-terminal region of the Turnip mosaic virus P3 protein is essential for viral infection via targeting P3 to the viral replication complex</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2017-10</date><risdate>2017</risdate><volume>510</volume><spage>147</spage><epage>155</epage><pages>147-155</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Like other positive-strand RNA viruses, plant potyviruses assemble viral replication complexes (VRCs) on modified cellular membranes. Potyviruses encode two membrane proteins, 6K2 and P3. The former is known to play pivotal roles in the formation of membrane-associated VRCs. However, P3 remains to be one of the least characterized potyviral proteins. The P3 cistron codes for P3 as well as P3N-PIPO which results from RNA polymerase slippage. In this study, we show that the P3N-PIPO of Turnip mosaic virus (TuMV) is required for viral cell-to-cell movement but not for viral replication. We demonstrate that the C-terminal region of P3 (P3C) is indispensable for P3 to form cytoplasmic punctate inclusions and target VRCs. We reveal that TuMV mutants that lack P3C are replication-defective. Taken together, these data suggest that the P3 cistron has two distinct functions: P3N-PIPO as a dedicated movement protein and P3 as an essential component of the VRC.
•The potyviarl P3 coding region encodes P3 and P3N-PIPO.•P3N-PIPO is not required for viral replication and is a dedicated movement protein.•P3 forms punctate structures that colocalize with viral replication complexes (VRC).•The C-terminal region of P3 (P3C) is required for P3 to target the VRC.•P3 is a component of the VRC and is essential for viral genome replication.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>28735115</pmid><doi>10.1016/j.virol.2017.07.016</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0042-6822 |
ispartof | Virology (New York, N.Y.), 2017-10, Vol.510, p.147-155 |
issn | 0042-6822 1096-0341 |
language | eng |
recordid | cdi_proquest_miscellaneous_1923111689 |
source | Elsevier |
subjects | Cell-to-cell movement DNA Mutational Analysis Membrane Proteins - genetics Membrane Proteins - metabolism Movement protein Nicotiana P3N-PIPO Plant RNA virus Plant Viral Movement Proteins - genetics Plant Viral Movement Proteins - metabolism Potyvirus Potyvirus - physiology Punctate inclusion Turnip mosaic virus Viral Proteins - genetics Viral Proteins - metabolism Virus Release Virus Replication Virus replication complex |
title | The C-terminal region of the Turnip mosaic virus P3 protein is essential for viral infection via targeting P3 to the viral replication complex |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T17%3A13%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20C-terminal%20region%20of%20the%20Turnip%20mosaic%20virus%20P3%20protein%20is%20essential%20for%20viral%20infection%20via%20targeting%20P3%20to%20the%20viral%20replication%20complex&rft.jtitle=Virology%20(New%20York,%20N.Y.)&rft.au=Cui,%20Xiaoyan&rft.date=2017-10&rft.volume=510&rft.spage=147&rft.epage=155&rft.pages=147-155&rft.issn=0042-6822&rft.eissn=1096-0341&rft_id=info:doi/10.1016/j.virol.2017.07.016&rft_dat=%3Cproquest_cross%3E1923111689%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c425t-232219283ff2c7a480fe3910287b26b82f443fe52e8ca0ff833d52538fc89c023%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1923111689&rft_id=info:pmid/28735115&rfr_iscdi=true |