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...

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Main Authors:	Mohamed Suffian, Izzat Fahimuddin, Nishimura, Yuya, Morita, Kenta, Nakamura-Tsuruta, Sachiko, Al-Jamal, Khuloud, Ishii, Jun, Ogino, Chiaki, Kondo, Akihiko
Format:	Article
Language:	English
Published:	Biomed Central 2015
Subjects:	QH301 Biology QR355 Virology RM Therapeutics. Pharmacology
Online Access:	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

id	iium-57364
recordtype	eprints
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
repository_type	Digital Repository
institution_category	Local University
institution	International Islamic University Malaysia
building	IIUM Repository
collection	Online Access
language	English
topic	QH301 Biology QR355 Virology RM Therapeutics. Pharmacology
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
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.
format	Article
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
title	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_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_sort	mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis b virus core particles
publisher	Biomed Central
publishDate	2015
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
first_indexed	2023-09-18T21:21:05Z
last_indexed	2023-09-18T21:21:05Z
_version_	1777411886523875328

Mutation of arginine residues to avoid non-specific cellular uptakes for hepatitis B virus core particles

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