Engineered resistance to Nosema bombycis by in vitro expression of a single-chain antibody in Sf9-III cells
Nosema bombycis is a destructive, obligate intracellular parasite of the Bombyx mori. In this study, a single-chain variable fragment (scFv) dependent technology is developed for the purpose of inhibiting parasite proliferation in insect cells. The scFv-G4, which we prepared from a mouse G4 monoclon...
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| creator | Huang, Yukang Chen, Jie Sun, Bin Zheng, Rong Li, Boning Li, Zeng Tan, Yaoyao Wei, Junhong Pan, Guoqing Li, Chunfeng Zhou, Zeyang |
| description | Nosema bombycis is a destructive, obligate intracellular parasite of the Bombyx mori. In this study, a single-chain variable fragment (scFv) dependent technology is developed for the purpose of inhibiting parasite proliferation in insect cells. The scFv-G4, which we prepared from a mouse G4 monoclonal antibody, can target the N. bombycis spore wall protein 12 (NbSWP12). Indirect immunofluorescence assays showed that NbSWP12 located mainly on the outside of the N. bombycis cytoskeleton, although some of it co-localized with β-tubulin in the meront-stage of parasites. When meront division began, NbSWP12 became concentrated at both ends of each meront. Western blotting showed that scFv-G4 could express in Sf9-III cells and recognized native NbSWP12. The transgenic Sf9-III cell line showed better resistance than the controls when challenged with N. bombycis, indicating that NbSWP12 is a promising target in this parasite and this scFv dependent strategy could be a solution for construction of N. bombycis-resistant Bombyx mori. |
| doi_str_mv | 10.1371/journal.pone.0193065 |
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In this study, a single-chain variable fragment (scFv) dependent technology is developed for the purpose of inhibiting parasite proliferation in insect cells. The scFv-G4, which we prepared from a mouse G4 monoclonal antibody, can target the N. bombycis spore wall protein 12 (NbSWP12). Indirect immunofluorescence assays showed that NbSWP12 located mainly on the outside of the N. bombycis cytoskeleton, although some of it co-localized with β-tubulin in the meront-stage of parasites. When meront division began, NbSWP12 became concentrated at both ends of each meront. Western blotting showed that scFv-G4 could express in Sf9-III cells and recognized native NbSWP12. The transgenic Sf9-III cell line showed better resistance than the controls when challenged with N. bombycis, indicating that NbSWP12 is a promising target in this parasite and this scFv dependent strategy could be a solution for construction of N. bombycis-resistant Bombyx mori.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0193065</identifier><identifier>PMID: 29447266</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Anopheles stephensi ; Biology ; Biology and Life Sciences ; Biotechnology ; Bombyx mori ; Cell proliferation ; Chains ; Culicidae ; Cytoskeleton ; Genetic aspects ; Genomes ; Genomics ; Genotypes ; Health aspects ; Immunofluorescence ; Infections ; Insect cells ; Insects ; Laboratories ; Malaria ; Medicine and Health Sciences ; Methods ; Microsporidia ; Monoclonal antibodies ; Nosema bombi ; Parasites ; Physical Sciences ; Plasmodium falciparum ; Proteins ; Research and Analysis Methods ; Signal transduction ; Tubulin ; Virulence (Microbiology) ; Western blotting</subject><ispartof>PloS one, 2018-02, Vol.13 (2), p.e0193065-e0193065</ispartof><rights>COPYRIGHT 2018 Public Library of Science</rights><rights>2018 Huang 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>2018 Huang et al 2018 Huang et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c692t-6db784c8b490dd1afaeacb82fe635dab86f36d71069fa703f58ed1d78d1058df3</citedby><cites>FETCH-LOGICAL-c692t-6db784c8b490dd1afaeacb82fe635dab86f36d71069fa703f58ed1d78d1058df3</cites><orcidid>0000-0003-2296-0742</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5814085/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5814085/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,729,782,786,866,887,2104,2930,23873,27931,27932,53798,53800</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29447266$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Ling, Erjun</contributor><creatorcontrib>Huang, Yukang</creatorcontrib><creatorcontrib>Chen, Jie</creatorcontrib><creatorcontrib>Sun, Bin</creatorcontrib><creatorcontrib>Zheng, Rong</creatorcontrib><creatorcontrib>Li, Boning</creatorcontrib><creatorcontrib>Li, Zeng</creatorcontrib><creatorcontrib>Tan, Yaoyao</creatorcontrib><creatorcontrib>Wei, Junhong</creatorcontrib><creatorcontrib>Pan, Guoqing</creatorcontrib><creatorcontrib>Li, Chunfeng</creatorcontrib><creatorcontrib>Zhou, Zeyang</creatorcontrib><title>Engineered resistance to Nosema bombycis by in vitro expression of a single-chain antibody in Sf9-III cells</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Nosema bombycis is a destructive, obligate intracellular parasite of the Bombyx mori. In this study, a single-chain variable fragment (scFv) dependent technology is developed for the purpose of inhibiting parasite proliferation in insect cells. The scFv-G4, which we prepared from a mouse G4 monoclonal antibody, can target the N. bombycis spore wall protein 12 (NbSWP12). Indirect immunofluorescence assays showed that NbSWP12 located mainly on the outside of the N. bombycis cytoskeleton, although some of it co-localized with β-tubulin in the meront-stage of parasites. When meront division began, NbSWP12 became concentrated at both ends of each meront. Western blotting showed that scFv-G4 could express in Sf9-III cells and recognized native NbSWP12. The transgenic Sf9-III cell line showed better resistance than the controls when challenged with N. bombycis, indicating that NbSWP12 is a promising target in this parasite and this scFv dependent strategy could be a solution for construction of N. bombycis-resistant Bombyx mori.</description><subject>Anopheles stephensi</subject><subject>Biology</subject><subject>Biology and Life Sciences</subject><subject>Biotechnology</subject><subject>Bombyx mori</subject><subject>Cell proliferation</subject><subject>Chains</subject><subject>Culicidae</subject><subject>Cytoskeleton</subject><subject>Genetic aspects</subject><subject>Genomes</subject><subject>Genomics</subject><subject>Genotypes</subject><subject>Health aspects</subject><subject>Immunofluorescence</subject><subject>Infections</subject><subject>Insect cells</subject><subject>Insects</subject><subject>Laboratories</subject><subject>Malaria</subject><subject>Medicine and Health Sciences</subject><subject>Methods</subject><subject>Microsporidia</subject><subject>Monoclonal antibodies</subject><subject>Nosema bombi</subject><subject>Parasites</subject><subject>Physical Sciences</subject><subject>Plasmodium falciparum</subject><subject>Proteins</subject><subject>Research and Analysis Methods</subject><subject>Signal transduction</subject><subject>Tubulin</subject><subject>Virulence (Microbiology)</subject><subject>Western 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resistance to Nosema bombycis by in vitro expression of a single-chain antibody in Sf9-III cells</title><author>Huang, Yukang ; Chen, Jie ; Sun, Bin ; Zheng, Rong ; Li, Boning ; Li, Zeng ; Tan, Yaoyao ; Wei, Junhong ; Pan, Guoqing ; Li, Chunfeng ; Zhou, Zeyang</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c692t-6db784c8b490dd1afaeacb82fe635dab86f36d71069fa703f58ed1d78d1058df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Anopheles stephensi</topic><topic>Biology</topic><topic>Biology and Life Sciences</topic><topic>Biotechnology</topic><topic>Bombyx mori</topic><topic>Cell proliferation</topic><topic>Chains</topic><topic>Culicidae</topic><topic>Cytoskeleton</topic><topic>Genetic aspects</topic><topic>Genomes</topic><topic>Genomics</topic><topic>Genotypes</topic><topic>Health aspects</topic><topic>Immunofluorescence</topic><topic>Infections</topic><topic>Insect cells</topic><topic>Insects</topic><topic>Laboratories</topic><topic>Malaria</topic><topic>Medicine and Health Sciences</topic><topic>Methods</topic><topic>Microsporidia</topic><topic>Monoclonal antibodies</topic><topic>Nosema bombi</topic><topic>Parasites</topic><topic>Physical Sciences</topic><topic>Plasmodium falciparum</topic><topic>Proteins</topic><topic>Research and Analysis Methods</topic><topic>Signal transduction</topic><topic>Tubulin</topic><topic>Virulence (Microbiology)</topic><topic>Western blotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huang, Yukang</creatorcontrib><creatorcontrib>Chen, Jie</creatorcontrib><creatorcontrib>Sun, Bin</creatorcontrib><creatorcontrib>Zheng, Rong</creatorcontrib><creatorcontrib>Li, Boning</creatorcontrib><creatorcontrib>Li, Zeng</creatorcontrib><creatorcontrib>Tan, Yaoyao</creatorcontrib><creatorcontrib>Wei, Junhong</creatorcontrib><creatorcontrib>Pan, 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Erjun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Engineered resistance to Nosema bombycis by in vitro expression of a single-chain antibody in Sf9-III cells</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2018-02-15</date><risdate>2018</risdate><volume>13</volume><issue>2</issue><spage>e0193065</spage><epage>e0193065</epage><pages>e0193065-e0193065</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>Nosema bombycis is a destructive, obligate intracellular parasite of the Bombyx mori. In this study, a single-chain variable fragment (scFv) dependent technology is developed for the purpose of inhibiting parasite proliferation in insect cells. The scFv-G4, which we prepared from a mouse G4 monoclonal antibody, can target the N. bombycis spore wall protein 12 (NbSWP12). Indirect immunofluorescence assays showed that NbSWP12 located mainly on the outside of the N. bombycis cytoskeleton, although some of it co-localized with β-tubulin in the meront-stage of parasites. When meront division began, NbSWP12 became concentrated at both ends of each meront. Western blotting showed that scFv-G4 could express in Sf9-III cells and recognized native NbSWP12. The transgenic Sf9-III cell line showed better resistance than the controls when challenged with N. bombycis, indicating that NbSWP12 is a promising target in this parasite and this scFv dependent strategy could be a solution for construction of N. bombycis-resistant Bombyx mori.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>29447266</pmid><doi>10.1371/journal.pone.0193065</doi><tpages>e0193065</tpages><orcidid>https://orcid.org/0000-0003-2296-0742</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Anopheles stephensi Biology Biology and Life Sciences Biotechnology Bombyx mori Cell proliferation Chains Culicidae Cytoskeleton Genetic aspects Genomes Genomics Genotypes Health aspects Immunofluorescence Infections Insect cells Insects Laboratories Malaria Medicine and Health Sciences Methods Microsporidia Monoclonal antibodies Nosema bombi Parasites Physical Sciences Plasmodium falciparum Proteins Research and Analysis Methods Signal transduction Tubulin Virulence (Microbiology) Western blotting |
| title | Engineered resistance to Nosema bombycis by in vitro expression of a single-chain antibody in Sf9-III cells |
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