Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles
BACKGROUND: The hepatitis B virus core (HBc) particle is known as a promising new carrier for the delivery of drugs and nucleic acids. However, since the arginine-rich domain that is located in the C-terminal region of the HBc monomer binds to the heparan sulphate proteoglycan on the cell surface du...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Biomed Central
2015
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| Online Access: | http://irep.iium.edu.my/57364/ http://irep.iium.edu.my/57364/1/Suffian%20et%20al.%20Journal%20of%20Nanobiotechnology.pdf |
| _version_ | 1848784920018681856 |
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| author | Mohamed Suffian, Izzat Fahimuddin Nishimura, Yuya Morita, Kenta Nakamura-Tsuruta, Sachiko Al-Jamal, Khuloud Ishii, Jun Ogino, Chiaki Kondo, Akihiko |
| author_facet | Mohamed Suffian, Izzat Fahimuddin Nishimura, Yuya Morita, Kenta Nakamura-Tsuruta, Sachiko Al-Jamal, Khuloud Ishii, Jun Ogino, Chiaki Kondo, Akihiko |
| author_sort | Mohamed Suffian, Izzat Fahimuddin |
| building | IIUM Repository |
| collection | Online Access |
| description | BACKGROUND: The hepatitis B virus core (HBc) particle is known as a promising new carrier for the delivery of drugs and nucleic acids. However, since the arginine-rich domain that is located in the C-terminal region of the HBc monomer binds to the heparan sulphate proteoglycan on the cell surface due to its positive charge, HBc particles are introduced non-specifically into a wide range of cells. To avoid non-specific cellular uptake with the intent to control the ability of cell targeting, we individually replaced the respective arginine (R) residues of the arginine-rich domain located in amino acid positions 150-159 in glycine (G) residues.
RESULTS: The mutated HBc particles in which R154 was replaced with glycine (G) residue (R154G) showed a drastic decrease in the ability to bind to the heparan sulphate proteoglycan and to avoid non-specific cellular uptake by several types of cancer cells.
CONCLUSIONS: Because this mutant particle retains most of its C-terminal arginine-rich residues, it would be useful in the targeting of specificity-altered HBc particles in the delivery of nucleic acids. |
| first_indexed | 2025-11-14T16:44:54Z |
| format | Article |
| id | iium-57364 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T16:44:54Z |
| publishDate | 2015 |
| publisher | Biomed Central |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | iium-573642017-06-23T00:04:31Z http://irep.iium.edu.my/57364/ Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles Mohamed Suffian, Izzat Fahimuddin Nishimura, Yuya Morita, Kenta Nakamura-Tsuruta, Sachiko Al-Jamal, Khuloud Ishii, Jun Ogino, Chiaki Kondo, Akihiko QH301 Biology QR355 Virology RM Therapeutics. Pharmacology BACKGROUND: The hepatitis B virus core (HBc) particle is known as a promising new carrier for the delivery of drugs and nucleic acids. However, since the arginine-rich domain that is located in the C-terminal region of the HBc monomer binds to the heparan sulphate proteoglycan on the cell surface due to its positive charge, HBc particles are introduced non-specifically into a wide range of cells. To avoid non-specific cellular uptake with the intent to control the ability of cell targeting, we individually replaced the respective arginine (R) residues of the arginine-rich domain located in amino acid positions 150-159 in glycine (G) residues. RESULTS: The mutated HBc particles in which R154 was replaced with glycine (G) residue (R154G) showed a drastic decrease in the ability to bind to the heparan sulphate proteoglycan and to avoid non-specific cellular uptake by several types of cancer cells. CONCLUSIONS: Because this mutant particle retains most of its C-terminal arginine-rich residues, it would be useful in the targeting of specificity-altered HBc particles in the delivery of nucleic acids. Biomed Central 2015-02-13 Article PeerReviewed application/pdf en http://irep.iium.edu.my/57364/1/Suffian%20et%20al.%20Journal%20of%20Nanobiotechnology.pdf Mohamed Suffian, Izzat Fahimuddin and Nishimura, Yuya and Morita, Kenta and Nakamura-Tsuruta, Sachiko and Al-Jamal, Khuloud and Ishii, Jun and Ogino, Chiaki and Kondo, Akihiko (2015) Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles. Nanobiotechnology, 13. ISSN 1477-3155 http://dx.doi.org/10.1186/s12951-015-0074-8 |
| spellingShingle | QH301 Biology QR355 Virology RM Therapeutics. Pharmacology Mohamed Suffian, Izzat Fahimuddin Nishimura, Yuya Morita, Kenta Nakamura-Tsuruta, Sachiko Al-Jamal, Khuloud Ishii, Jun Ogino, Chiaki Kondo, Akihiko Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles |
| title | Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles |
| title_full | Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles |
| title_fullStr | Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles |
| title_full_unstemmed | Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles |
| title_short | Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles |
| title_sort | mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis b virus core particles |
| topic | QH301 Biology QR355 Virology RM Therapeutics. Pharmacology |
| url | http://irep.iium.edu.my/57364/ http://irep.iium.edu.my/57364/ http://irep.iium.edu.my/57364/1/Suffian%20et%20al.%20Journal%20of%20Nanobiotechnology.pdf |