Loading…
The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth
Toxoplasma gondii is an obligate intracellular apicomplexan parasite that infects almost all warm-blooded vertebrates. Heat shock proteins (HSP) regulate key signal transduction events in many organisms, and heat shock protein 90 (Hsp90) plays an important role in growth, development, and virulence...
Saved in:
Published in: | Parasite (Paris) 2017, Vol.24, p.22-22 |
---|---|
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-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3 |
---|---|
cites | cdi_FETCH-LOGICAL-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3 |
container_end_page | 22 |
container_issue | |
container_start_page | 22 |
container_title | Parasite (Paris) |
container_volume | 24 |
creator | Sun, Hongchao Zhuo, Xunhui Zhao, Xianfeng Yang, Yi Chen, Xueqiu Yao, Chaoqun Du, Aifang |
description | Toxoplasma gondii is an obligate intracellular apicomplexan parasite that infects almost all warm-blooded vertebrates. Heat shock proteins (HSP) regulate key signal transduction events in many organisms, and heat shock protein 90 (Hsp90) plays an important role in growth, development, and virulence in several parasitic protozoa. Here, we discovered increased transcription of the Hsp90 gene under conditions for bradyzoite differentiation, i.e. alkaline and heat shock conditions in vitro, suggesting that Hsp90 may be connected with bradyzoite development in T. gondii. A knockout of the TgHsp90 strain (ΔHsp90) and a complementation strain were constructed. The TgHsp90 knockout cells were found to be defective in host-cell invasion, were not able to proliferate in vitro in Vero cells, and did not show long-time survival in mice in vivo. These inabilities of the knockout parasites were restored upon complementation of TgHsp90. These data unequivocally show that TgHsp90 contributes to bradyzoite development, and to invasion and replication of T. gondii in host cells. |
doi_str_mv | 10.1051/parasite/2017023 |
format | article |
fullrecord | <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_78e343d40cce47439deda55929556037</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_78e343d40cce47439deda55929556037</doaj_id><sourcerecordid>1911207469</sourcerecordid><originalsourceid>FETCH-LOGICAL-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3</originalsourceid><addsrcrecordid>eNpdks1vEzEQxVcIREvhzglZ4sIl1J9r-4KEKj4qVeISztbUns06bNbBdgrlr8chadXii63xm5_ejF7XvWb0PaOKnW8hQ4kVzzllmnLxpDtlWvcLRiV_-uB90r0oZU1pL3ojnncn3PRcC6VPu2k5IhkRKilj8j_INqeKcSaWkjSQZfqdthOUDZBVmkOMJBaCpeBcI0xkSJnE-aZZSPNePqZSicdpKgTmQCr48fZPav7IKqdfdXzZPRtgKvjqeJ913z9_Wl58XVx9-3J58fFq4ZXq6-JaCEYHrtFSyYxsB4UExYcQzMCVCeg11SFI7OVgQFijtfFCCNvTIDSIs-7ywA0J1m6b4wbyrUsQ3b9CyisHuUY_odOmsUWQ1HuUWgobMIBSlttmhQrdWB8OrO3ueoPBt9EzTI-gj3_mOLpVunFKaispa4B3R0BOP3dYqtvEsl8SzJh2xTHLGKda9rZJ3_4nXaddntuqHG9eaG8kU01FDyqfUykZh3szjLp9LNxdLNwxFq3lzcMh7hvuciD-AqxUtQ4</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2037068415</pqid></control><display><type>article</type><title>The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth</title><source>Publicly Available Content Database</source><source>PubMed Central</source><creator>Sun, Hongchao ; Zhuo, Xunhui ; Zhao, Xianfeng ; Yang, Yi ; Chen, Xueqiu ; Yao, Chaoqun ; Du, Aifang</creator><creatorcontrib>Sun, Hongchao ; Zhuo, Xunhui ; Zhao, Xianfeng ; Yang, Yi ; Chen, Xueqiu ; Yao, Chaoqun ; Du, Aifang</creatorcontrib><description>Toxoplasma gondii is an obligate intracellular apicomplexan parasite that infects almost all warm-blooded vertebrates. Heat shock proteins (HSP) regulate key signal transduction events in many organisms, and heat shock protein 90 (Hsp90) plays an important role in growth, development, and virulence in several parasitic protozoa. Here, we discovered increased transcription of the Hsp90 gene under conditions for bradyzoite differentiation, i.e. alkaline and heat shock conditions in vitro, suggesting that Hsp90 may be connected with bradyzoite development in T. gondii. A knockout of the TgHsp90 strain (ΔHsp90) and a complementation strain were constructed. The TgHsp90 knockout cells were found to be defective in host-cell invasion, were not able to proliferate in vitro in Vero cells, and did not show long-time survival in mice in vivo. These inabilities of the knockout parasites were restored upon complementation of TgHsp90. These data unequivocally show that TgHsp90 contributes to bradyzoite development, and to invasion and replication of T. gondii in host cells.</description><identifier>ISSN: 1776-1042</identifier><identifier>ISSN: 1252-607X</identifier><identifier>EISSN: 1776-1042</identifier><identifier>DOI: 10.1051/parasite/2017023</identifier><identifier>PMID: 28627357</identifier><language>eng</language><publisher>France: EDP Sciences</publisher><subject>Animals ; Antibodies, Protozoan - analysis ; Antibodies, Protozoan - biosynthesis ; Blotting, Western ; Cercopithecus aethiops ; Complementation ; Differentiation ; Enzyme-Linked Immunosorbent Assay ; Female ; Fluorescent Antibody Technique ; Gene Knockout Techniques ; Genetic Complementation Test ; Heat shock protein 90 ; Heat shock proteins ; Hot Temperature ; HSP90 Heat-Shock Proteins - genetics ; HSP90 Heat-Shock Proteins - immunology ; HSP90 Heat-Shock Proteins - physiology ; Hsp90 protein ; Hydrogen-Ion Concentration ; Invasion ; Mice ; Mice, Inbred BALB C ; Parasites ; Protozoa ; Rabbits ; Radioimmunoprecipitation Assay ; Real-Time Polymerase Chain Reaction ; Recombinant Proteins - genetics ; Recombinant Proteins - immunology ; Recombinant Proteins - isolation & purification ; Replication ; Signal transduction ; Toxoplasma - chemistry ; Toxoplasma - growth & development ; Toxoplasma - pathogenicity ; Toxoplasma - physiology ; Toxoplasma gondii ; Vero Cells ; Vertebrates ; Virulence</subject><ispartof>Parasite (Paris), 2017, Vol.24, p.22-22</ispartof><rights>H. Sun et al., published by EDP Sciences, 2017.</rights><rights>2017. This work is licensed under http://creativecommons.org/licenses/by/4.0 (the “License”). Notwithstanding the ProQuest Terms and conditions, you may use this content in accordance with the terms of the License.</rights><rights>H. Sun et al., published by EDP Sciences, 2017 2017 H. Sun et al.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3</citedby><cites>FETCH-LOGICAL-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3</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/PMC5479401/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2037068415?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,4024,25753,27923,27924,27925,37012,37013,44590,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28627357$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sun, Hongchao</creatorcontrib><creatorcontrib>Zhuo, Xunhui</creatorcontrib><creatorcontrib>Zhao, Xianfeng</creatorcontrib><creatorcontrib>Yang, Yi</creatorcontrib><creatorcontrib>Chen, Xueqiu</creatorcontrib><creatorcontrib>Yao, Chaoqun</creatorcontrib><creatorcontrib>Du, Aifang</creatorcontrib><title>The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth</title><title>Parasite (Paris)</title><addtitle>Parasite</addtitle><description>Toxoplasma gondii is an obligate intracellular apicomplexan parasite that infects almost all warm-blooded vertebrates. Heat shock proteins (HSP) regulate key signal transduction events in many organisms, and heat shock protein 90 (Hsp90) plays an important role in growth, development, and virulence in several parasitic protozoa. Here, we discovered increased transcription of the Hsp90 gene under conditions for bradyzoite differentiation, i.e. alkaline and heat shock conditions in vitro, suggesting that Hsp90 may be connected with bradyzoite development in T. gondii. A knockout of the TgHsp90 strain (ΔHsp90) and a complementation strain were constructed. The TgHsp90 knockout cells were found to be defective in host-cell invasion, were not able to proliferate in vitro in Vero cells, and did not show long-time survival in mice in vivo. These inabilities of the knockout parasites were restored upon complementation of TgHsp90. These data unequivocally show that TgHsp90 contributes to bradyzoite development, and to invasion and replication of T. gondii in host cells.</description><subject>Animals</subject><subject>Antibodies, Protozoan - analysis</subject><subject>Antibodies, Protozoan - biosynthesis</subject><subject>Blotting, Western</subject><subject>Cercopithecus aethiops</subject><subject>Complementation</subject><subject>Differentiation</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Female</subject><subject>Fluorescent Antibody Technique</subject><subject>Gene Knockout Techniques</subject><subject>Genetic Complementation Test</subject><subject>Heat shock protein 90</subject><subject>Heat shock proteins</subject><subject>Hot Temperature</subject><subject>HSP90 Heat-Shock Proteins - genetics</subject><subject>HSP90 Heat-Shock Proteins - immunology</subject><subject>HSP90 Heat-Shock Proteins - physiology</subject><subject>Hsp90 protein</subject><subject>Hydrogen-Ion Concentration</subject><subject>Invasion</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Parasites</subject><subject>Protozoa</subject><subject>Rabbits</subject><subject>Radioimmunoprecipitation Assay</subject><subject>Real-Time Polymerase Chain Reaction</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - immunology</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Replication</subject><subject>Signal transduction</subject><subject>Toxoplasma - chemistry</subject><subject>Toxoplasma - growth & development</subject><subject>Toxoplasma - pathogenicity</subject><subject>Toxoplasma - physiology</subject><subject>Toxoplasma gondii</subject><subject>Vero Cells</subject><subject>Vertebrates</subject><subject>Virulence</subject><issn>1776-1042</issn><issn>1252-607X</issn><issn>1776-1042</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNpdks1vEzEQxVcIREvhzglZ4sIl1J9r-4KEKj4qVeISztbUns06bNbBdgrlr8chadXii63xm5_ejF7XvWb0PaOKnW8hQ4kVzzllmnLxpDtlWvcLRiV_-uB90r0oZU1pL3ojnncn3PRcC6VPu2k5IhkRKilj8j_INqeKcSaWkjSQZfqdthOUDZBVmkOMJBaCpeBcI0xkSJnE-aZZSPNePqZSicdpKgTmQCr48fZPav7IKqdfdXzZPRtgKvjqeJ913z9_Wl58XVx9-3J58fFq4ZXq6-JaCEYHrtFSyYxsB4UExYcQzMCVCeg11SFI7OVgQFijtfFCCNvTIDSIs-7ywA0J1m6b4wbyrUsQ3b9CyisHuUY_odOmsUWQ1HuUWgobMIBSlttmhQrdWB8OrO3ueoPBt9EzTI-gj3_mOLpVunFKaispa4B3R0BOP3dYqtvEsl8SzJh2xTHLGKda9rZJ3_4nXaddntuqHG9eaG8kU01FDyqfUykZh3szjLp9LNxdLNwxFq3lzcMh7hvuciD-AqxUtQ4</recordid><startdate>2017</startdate><enddate>2017</enddate><creator>Sun, Hongchao</creator><creator>Zhuo, Xunhui</creator><creator>Zhao, Xianfeng</creator><creator>Yang, Yi</creator><creator>Chen, Xueqiu</creator><creator>Yao, Chaoqun</creator><creator>Du, Aifang</creator><general>EDP Sciences</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>3V.</scope><scope>7QG</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>2017</creationdate><title>The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth</title><author>Sun, Hongchao ; Zhuo, Xunhui ; Zhao, Xianfeng ; Yang, Yi ; Chen, Xueqiu ; Yao, Chaoqun ; Du, Aifang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Antibodies, Protozoan - analysis</topic><topic>Antibodies, Protozoan - biosynthesis</topic><topic>Blotting, Western</topic><topic>Cercopithecus aethiops</topic><topic>Complementation</topic><topic>Differentiation</topic><topic>Enzyme-Linked Immunosorbent Assay</topic><topic>Female</topic><topic>Fluorescent Antibody Technique</topic><topic>Gene Knockout Techniques</topic><topic>Genetic Complementation Test</topic><topic>Heat shock protein 90</topic><topic>Heat shock proteins</topic><topic>Hot Temperature</topic><topic>HSP90 Heat-Shock Proteins - genetics</topic><topic>HSP90 Heat-Shock Proteins - immunology</topic><topic>HSP90 Heat-Shock Proteins - physiology</topic><topic>Hsp90 protein</topic><topic>Hydrogen-Ion Concentration</topic><topic>Invasion</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Parasites</topic><topic>Protozoa</topic><topic>Rabbits</topic><topic>Radioimmunoprecipitation Assay</topic><topic>Real-Time Polymerase Chain Reaction</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - immunology</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Replication</topic><topic>Signal transduction</topic><topic>Toxoplasma - chemistry</topic><topic>Toxoplasma - growth & development</topic><topic>Toxoplasma - pathogenicity</topic><topic>Toxoplasma - physiology</topic><topic>Toxoplasma gondii</topic><topic>Vero Cells</topic><topic>Vertebrates</topic><topic>Virulence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sun, Hongchao</creatorcontrib><creatorcontrib>Zhuo, Xunhui</creatorcontrib><creatorcontrib>Zhao, Xianfeng</creatorcontrib><creatorcontrib>Yang, Yi</creatorcontrib><creatorcontrib>Chen, Xueqiu</creatorcontrib><creatorcontrib>Yao, Chaoqun</creatorcontrib><creatorcontrib>Du, Aifang</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>ProQuest Health and Medical</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</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>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>ProQuest Biological Science Journals</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Parasite (Paris)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sun, Hongchao</au><au>Zhuo, Xunhui</au><au>Zhao, Xianfeng</au><au>Yang, Yi</au><au>Chen, Xueqiu</au><au>Yao, Chaoqun</au><au>Du, Aifang</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth</atitle><jtitle>Parasite (Paris)</jtitle><addtitle>Parasite</addtitle><date>2017</date><risdate>2017</risdate><volume>24</volume><spage>22</spage><epage>22</epage><pages>22-22</pages><issn>1776-1042</issn><issn>1252-607X</issn><eissn>1776-1042</eissn><abstract>Toxoplasma gondii is an obligate intracellular apicomplexan parasite that infects almost all warm-blooded vertebrates. Heat shock proteins (HSP) regulate key signal transduction events in many organisms, and heat shock protein 90 (Hsp90) plays an important role in growth, development, and virulence in several parasitic protozoa. Here, we discovered increased transcription of the Hsp90 gene under conditions for bradyzoite differentiation, i.e. alkaline and heat shock conditions in vitro, suggesting that Hsp90 may be connected with bradyzoite development in T. gondii. A knockout of the TgHsp90 strain (ΔHsp90) and a complementation strain were constructed. The TgHsp90 knockout cells were found to be defective in host-cell invasion, were not able to proliferate in vitro in Vero cells, and did not show long-time survival in mice in vivo. These inabilities of the knockout parasites were restored upon complementation of TgHsp90. These data unequivocally show that TgHsp90 contributes to bradyzoite development, and to invasion and replication of T. gondii in host cells.</abstract><cop>France</cop><pub>EDP Sciences</pub><pmid>28627357</pmid><doi>10.1051/parasite/2017023</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1776-1042 |
ispartof | Parasite (Paris), 2017, Vol.24, p.22-22 |
issn | 1776-1042 1252-607X 1776-1042 |
language | eng |
recordid | cdi_doaj_primary_oai_doaj_org_article_78e343d40cce47439deda55929556037 |
source | Publicly Available Content Database; PubMed Central |
subjects | Animals Antibodies, Protozoan - analysis Antibodies, Protozoan - biosynthesis Blotting, Western Cercopithecus aethiops Complementation Differentiation Enzyme-Linked Immunosorbent Assay Female Fluorescent Antibody Technique Gene Knockout Techniques Genetic Complementation Test Heat shock protein 90 Heat shock proteins Hot Temperature HSP90 Heat-Shock Proteins - genetics HSP90 Heat-Shock Proteins - immunology HSP90 Heat-Shock Proteins - physiology Hsp90 protein Hydrogen-Ion Concentration Invasion Mice Mice, Inbred BALB C Parasites Protozoa Rabbits Radioimmunoprecipitation Assay Real-Time Polymerase Chain Reaction Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - isolation & purification Replication Signal transduction Toxoplasma - chemistry Toxoplasma - growth & development Toxoplasma - pathogenicity Toxoplasma - physiology Toxoplasma gondii Vero Cells Vertebrates Virulence |
title | The heat shock protein 90 of Toxoplasma gondii is essential for invasion of host cells and tachyzoite growth |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T10%3A19%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20heat%20shock%20protein%2090%20of%20Toxoplasma%20gondii%20is%20essential%20for%20invasion%20of%20host%20cells%20and%20tachyzoite%20growth&rft.jtitle=Parasite%20(Paris)&rft.au=Sun,%20Hongchao&rft.date=2017&rft.volume=24&rft.spage=22&rft.epage=22&rft.pages=22-22&rft.issn=1776-1042&rft.eissn=1776-1042&rft_id=info:doi/10.1051/parasite/2017023&rft_dat=%3Cproquest_doaj_%3E1911207469%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c556t-b3310f27e904184444e34a52fdd8f258dec707dd4e64f8a398778c333960d37a3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2037068415&rft_id=info:pmid/28627357&rfr_iscdi=true |