Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells
Abstract Recombinant MrNV capsid protein has been shown to effectively deliver plasmid DNA and dsRNA into Sf9 insect cells and shrimp tissues. To extend its application to cancer cell-targeting drug delivery, we created three different types of chimeric MrNV virus-like particles (VLPs) (R-MrNV, I-Mr...
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2021
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oai:doaj.org-article:0420e6e5d02143c4b628d97ea645139b2021-12-02T18:51:46ZChimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells10.1038/s41598-021-95891-x2045-2322https://doaj.org/article/0420e6e5d02143c4b628d97ea645139b2021-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-95891-xhttps://doaj.org/toc/2045-2322Abstract Recombinant MrNV capsid protein has been shown to effectively deliver plasmid DNA and dsRNA into Sf9 insect cells and shrimp tissues. To extend its application to cancer cell-targeting drug delivery, we created three different types of chimeric MrNV virus-like particles (VLPs) (R-MrNV, I-MrNV, and E-MrNV) that have specificity toward the epidermal growth factor receptor (EGFR), a cancer cell biomarker, by incorporating the EGFR-specific GE11 peptide at 3 different locations within the host cell recognition site of the capsid. All three chimeric MrNV-VLPs preserved the ability to form a mulberry-like VLP structure and to encapsulate EGFP DNA plasmid with an efficiency comparable to that previously reported for normal MrNV (N-MrNV). Compared to N-MrNV, the chimeric R-MrNV and E-MrNV carrying the exposed GE-11 peptide showed a significantly enhanced binding and internalization abilities that were specific towards EGFR expression in colorectal cancer cells (SW480). Specific targeting of chimeric MrNV to EGFR was proven by both EGFR silencing with siRNA vector and a competition with excess GE-11 peptide as well as the use of EGFR-negative colorectal cells (SW620) and breast cancer cells (MCF7). We demonstrated here that both chimeric R-MrNV and E-MrNV could be used to encapsulate cargo such as exogenous DNA and deliver it specifically to EGFR-positive cells. Our study presents the potential use of surface-modified VLPs of shrimp virus origin as nanocontainers for targeted cancer drug delivery.Khwanthana GrataitongSébastien HuaultCharoonroj ChotwiwatthanakunPitchanee JariyapongOrawan ThongsumChidchanok ChawiwithayaKrittalak ChakrabandhuAnne-Odile HueberWattana WeerachatyanukulNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021) |
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Medicine R Science Q Khwanthana Grataitong Sébastien Huault Charoonroj Chotwiwatthanakun Pitchanee Jariyapong Orawan Thongsum Chidchanok Chawiwithaya Krittalak Chakrabandhu Anne-Odile Hueber Wattana Weerachatyanukul Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells |
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Abstract Recombinant MrNV capsid protein has been shown to effectively deliver plasmid DNA and dsRNA into Sf9 insect cells and shrimp tissues. To extend its application to cancer cell-targeting drug delivery, we created three different types of chimeric MrNV virus-like particles (VLPs) (R-MrNV, I-MrNV, and E-MrNV) that have specificity toward the epidermal growth factor receptor (EGFR), a cancer cell biomarker, by incorporating the EGFR-specific GE11 peptide at 3 different locations within the host cell recognition site of the capsid. All three chimeric MrNV-VLPs preserved the ability to form a mulberry-like VLP structure and to encapsulate EGFP DNA plasmid with an efficiency comparable to that previously reported for normal MrNV (N-MrNV). Compared to N-MrNV, the chimeric R-MrNV and E-MrNV carrying the exposed GE-11 peptide showed a significantly enhanced binding and internalization abilities that were specific towards EGFR expression in colorectal cancer cells (SW480). Specific targeting of chimeric MrNV to EGFR was proven by both EGFR silencing with siRNA vector and a competition with excess GE-11 peptide as well as the use of EGFR-negative colorectal cells (SW620) and breast cancer cells (MCF7). We demonstrated here that both chimeric R-MrNV and E-MrNV could be used to encapsulate cargo such as exogenous DNA and deliver it specifically to EGFR-positive cells. Our study presents the potential use of surface-modified VLPs of shrimp virus origin as nanocontainers for targeted cancer drug delivery. |
format |
article |
author |
Khwanthana Grataitong Sébastien Huault Charoonroj Chotwiwatthanakun Pitchanee Jariyapong Orawan Thongsum Chidchanok Chawiwithaya Krittalak Chakrabandhu Anne-Odile Hueber Wattana Weerachatyanukul |
author_facet |
Khwanthana Grataitong Sébastien Huault Charoonroj Chotwiwatthanakun Pitchanee Jariyapong Orawan Thongsum Chidchanok Chawiwithaya Krittalak Chakrabandhu Anne-Odile Hueber Wattana Weerachatyanukul |
author_sort |
Khwanthana Grataitong |
title |
Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells |
title_short |
Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells |
title_full |
Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells |
title_fullStr |
Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells |
title_full_unstemmed |
Chimeric virus-like particles (VLPs) designed from shrimp nodavirus (MrNV) capsid protein specifically target EGFR-positive human colorectal cancer cells |
title_sort |
chimeric virus-like particles (vlps) designed from shrimp nodavirus (mrnv) capsid protein specifically target egfr-positive human colorectal cancer cells |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/0420e6e5d02143c4b628d97ea645139b |
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