Effective expression of human proteins on bacterial magnetic particles in an anchor gene deletion mutant of Magnetospirillum magneticum AMB-1

Yuka Kanetsuki, Masayoshi Tanaka, Tsuyoshi Tanaka, Tadashi Matsunaga, Tomoko Yoshino

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Biologically synthesized magnetic particles by magnetotactic bacteria (BacMPs) have promising potential in the area of functional protein display technology for various biotechnological and biomedical applications. Functional proteins fused with an anchor protein, Mms13, have been demonstrated to be an effective and stable method for the display of functional proteins on BacMPs. However, the expression of some human proteins is relatively low. Useful host strains of Escherichia coli have been developed for the enhanced expression of recombinant proteins using a genetic engineering approach. To improve human protein expression level on BacMPs in Magnetospirillum magneticum AMB-1, a mutant strain with a deleted native mms13 gene (Δmms13 strain) was established and evaluated for effective functional protein display technology. As a result, the Δmms13 strain synthesized BacMPs with significantly improved expression of two human proteins, thyroid-stimulating hormone receptor (TSHR) and the class II major histocompatibility complex (MHC II) molecules. The Δmms13 strain could therefore be an effective strain for the display of other important human proteins on BacMPs and may be useful for further applications.

Original languageEnglish
Pages (from-to)7-11
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume426
Issue number1
DOIs
Publication statusPublished - 2012 Sep 14
Externally publishedYes

Fingerprint

Magnetospirillum
Bacterial Proteins
Gene Deletion
Anchors
Genes
Proteins
Display devices
Technology
Genetic engineering
Thyrotropin Receptors
Genetic Engineering
Major Histocompatibility Complex
Recombinant Proteins
Escherichia coli
Bacteria

Keywords

  • Bacterial magnetic particles
  • Human protein expression
  • Magnetotactic bacteria
  • Mms13
  • Protein display technology

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

Effective expression of human proteins on bacterial magnetic particles in an anchor gene deletion mutant of Magnetospirillum magneticum AMB-1. / Kanetsuki, Yuka; Tanaka, Masayoshi; Tanaka, Tsuyoshi; Matsunaga, Tadashi; Yoshino, Tomoko.

In: Biochemical and Biophysical Research Communications, Vol. 426, No. 1, 14.09.2012, p. 7-11.

Research output: Contribution to journalArticle

Kanetsuki, Yuka ; Tanaka, Masayoshi ; Tanaka, Tsuyoshi ; Matsunaga, Tadashi ; Yoshino, Tomoko. / Effective expression of human proteins on bacterial magnetic particles in an anchor gene deletion mutant of Magnetospirillum magneticum AMB-1. In: Biochemical and Biophysical Research Communications. 2012 ; Vol. 426, No. 1. pp. 7-11.
@article{eecbb96647cb41b0a13e37d2cf18b838,
title = "Effective expression of human proteins on bacterial magnetic particles in an anchor gene deletion mutant of Magnetospirillum magneticum AMB-1",
abstract = "Biologically synthesized magnetic particles by magnetotactic bacteria (BacMPs) have promising potential in the area of functional protein display technology for various biotechnological and biomedical applications. Functional proteins fused with an anchor protein, Mms13, have been demonstrated to be an effective and stable method for the display of functional proteins on BacMPs. However, the expression of some human proteins is relatively low. Useful host strains of Escherichia coli have been developed for the enhanced expression of recombinant proteins using a genetic engineering approach. To improve human protein expression level on BacMPs in Magnetospirillum magneticum AMB-1, a mutant strain with a deleted native mms13 gene (Δmms13 strain) was established and evaluated for effective functional protein display technology. As a result, the Δmms13 strain synthesized BacMPs with significantly improved expression of two human proteins, thyroid-stimulating hormone receptor (TSHR) and the class II major histocompatibility complex (MHC II) molecules. The Δmms13 strain could therefore be an effective strain for the display of other important human proteins on BacMPs and may be useful for further applications.",
keywords = "Bacterial magnetic particles, Human protein expression, Magnetotactic bacteria, Mms13, Protein display technology",
author = "Yuka Kanetsuki and Masayoshi Tanaka and Tsuyoshi Tanaka and Tadashi Matsunaga and Tomoko Yoshino",
year = "2012",
month = "9",
day = "14",
doi = "10.1016/j.bbrc.2012.07.116",
language = "English",
volume = "426",
pages = "7--11",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Effective expression of human proteins on bacterial magnetic particles in an anchor gene deletion mutant of Magnetospirillum magneticum AMB-1

AU - Kanetsuki, Yuka

AU - Tanaka, Masayoshi

AU - Tanaka, Tsuyoshi

AU - Matsunaga, Tadashi

AU - Yoshino, Tomoko

PY - 2012/9/14

Y1 - 2012/9/14

N2 - Biologically synthesized magnetic particles by magnetotactic bacteria (BacMPs) have promising potential in the area of functional protein display technology for various biotechnological and biomedical applications. Functional proteins fused with an anchor protein, Mms13, have been demonstrated to be an effective and stable method for the display of functional proteins on BacMPs. However, the expression of some human proteins is relatively low. Useful host strains of Escherichia coli have been developed for the enhanced expression of recombinant proteins using a genetic engineering approach. To improve human protein expression level on BacMPs in Magnetospirillum magneticum AMB-1, a mutant strain with a deleted native mms13 gene (Δmms13 strain) was established and evaluated for effective functional protein display technology. As a result, the Δmms13 strain synthesized BacMPs with significantly improved expression of two human proteins, thyroid-stimulating hormone receptor (TSHR) and the class II major histocompatibility complex (MHC II) molecules. The Δmms13 strain could therefore be an effective strain for the display of other important human proteins on BacMPs and may be useful for further applications.

AB - Biologically synthesized magnetic particles by magnetotactic bacteria (BacMPs) have promising potential in the area of functional protein display technology for various biotechnological and biomedical applications. Functional proteins fused with an anchor protein, Mms13, have been demonstrated to be an effective and stable method for the display of functional proteins on BacMPs. However, the expression of some human proteins is relatively low. Useful host strains of Escherichia coli have been developed for the enhanced expression of recombinant proteins using a genetic engineering approach. To improve human protein expression level on BacMPs in Magnetospirillum magneticum AMB-1, a mutant strain with a deleted native mms13 gene (Δmms13 strain) was established and evaluated for effective functional protein display technology. As a result, the Δmms13 strain synthesized BacMPs with significantly improved expression of two human proteins, thyroid-stimulating hormone receptor (TSHR) and the class II major histocompatibility complex (MHC II) molecules. The Δmms13 strain could therefore be an effective strain for the display of other important human proteins on BacMPs and may be useful for further applications.

KW - Bacterial magnetic particles

KW - Human protein expression

KW - Magnetotactic bacteria

KW - Mms13

KW - Protein display technology

UR - http://www.scopus.com/inward/record.url?scp=84866337901&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84866337901&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2012.07.116

DO - 10.1016/j.bbrc.2012.07.116

M3 - Article

C2 - 22846572

AN - SCOPUS:84866337901

VL - 426

SP - 7

EP - 11

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -