Antigenicity of the region encoded by exon8 of the human serine protease, HtrA2/Omi, is associated with its protein solubility

Hyo Jin Park; Ju Youn Choi; Young Mo Seong; Chul Han; Sung Joo Kim Yoon; Seongman Kang; Hyangshuk Rhim

doi:10.1023/A:1025630013679

Antigenicity of the region encoded by exon8 of the human serine protease, HtrA2/Omi, is associated with its protein solubility

Hyo Jin Park, Ju Youn Choi, Young Mo Seong, Chul Han, Sung Joo Kim Yoon, Seongman Kang, Hyangshuk Rhim

Department of Life Sciences

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

Abstract

HtrA2/Omi, a mitochondrial serine protease, is pivotal in regulating apoptotic cell death. To determine the location of antigenic determinants in HtrA2/Omi, we expressed a series of the N-terminally truncated HtrA2/Omi as GST fusion proteins in E. coli. We assessed protein solubility and antigenic reactivity of various N-terminally truncated HtrA2/Omi proteins by binding to glutathione beads and immunoblot analyses, respectively. We identified that the region encoded by exon8 of HtrA2/Omi was expressed as a highly soluble form and contains an antigenic determinant specifically recognized by a polyclonal serum against HtrA2/Omi. Our data provide evidence that protein solubility of the specific region in target proteins may contribute to the antigenicity.

Original language	English
Pages (from-to)	1597-1603
Number of pages	7
Journal	Biotechnology letters
Volume	25
Issue number	19
DOIs	https://doi.org/10.1023/A:1025630013679
Publication status	Published - 2003 Oct

Bibliographical note

Funding Information:
This work was supported by the Korean Health 21 R&D Project, Ministry of Health & Welfare, Republic of Korea (HMP-02-PJ1-PG3-20908-0020).

Keywords

Antigenic determinant
Exon8
Protein solubility
pGEX expression

ASJC Scopus subject areas

Biotechnology
Bioengineering
Applied Microbiology and Biotechnology

Access to Document

10.1023/A:1025630013679

Cite this

@article{1b31397e1ec443b7b682733a7d267bbe,

title = "Antigenicity of the region encoded by exon8 of the human serine protease, HtrA2/Omi, is associated with its protein solubility",

abstract = "HtrA2/Omi, a mitochondrial serine protease, is pivotal in regulating apoptotic cell death. To determine the location of antigenic determinants in HtrA2/Omi, we expressed a series of the N-terminally truncated HtrA2/Omi as GST fusion proteins in E. coli. We assessed protein solubility and antigenic reactivity of various N-terminally truncated HtrA2/Omi proteins by binding to glutathione beads and immunoblot analyses, respectively. We identified that the region encoded by exon8 of HtrA2/Omi was expressed as a highly soluble form and contains an antigenic determinant specifically recognized by a polyclonal serum against HtrA2/Omi. Our data provide evidence that protein solubility of the specific region in target proteins may contribute to the antigenicity.",

keywords = "Antigenic determinant, Exon8, Protein solubility, pGEX expression",

author = "Park, {Hyo Jin} and Choi, {Ju Youn} and Seong, {Young Mo} and Chul Han and Yoon, {Sung Joo Kim} and Seongman Kang and Hyangshuk Rhim",

note = "Funding Information: This work was supported by the Korean Health 21 R&D Project, Ministry of Health & Welfare, Republic of Korea (HMP-02-PJ1-PG3-20908-0020).",

year = "2003",

month = oct,

doi = "10.1023/A:1025630013679",

language = "English",

volume = "25",

pages = "1597--1603",

journal = "Biotechnology letters",

issn = "0141-5492",

publisher = "Springer Science and Business Media B.V.",

number = "19",

}

TY - JOUR

T1 - Antigenicity of the region encoded by exon8 of the human serine protease, HtrA2/Omi, is associated with its protein solubility

AU - Park, Hyo Jin

AU - Choi, Ju Youn

AU - Seong, Young Mo

AU - Han, Chul

AU - Yoon, Sung Joo Kim

AU - Kang, Seongman

AU - Rhim, Hyangshuk

N1 - Funding Information: This work was supported by the Korean Health 21 R&D Project, Ministry of Health & Welfare, Republic of Korea (HMP-02-PJ1-PG3-20908-0020).

PY - 2003/10

Y1 - 2003/10

N2 - HtrA2/Omi, a mitochondrial serine protease, is pivotal in regulating apoptotic cell death. To determine the location of antigenic determinants in HtrA2/Omi, we expressed a series of the N-terminally truncated HtrA2/Omi as GST fusion proteins in E. coli. We assessed protein solubility and antigenic reactivity of various N-terminally truncated HtrA2/Omi proteins by binding to glutathione beads and immunoblot analyses, respectively. We identified that the region encoded by exon8 of HtrA2/Omi was expressed as a highly soluble form and contains an antigenic determinant specifically recognized by a polyclonal serum against HtrA2/Omi. Our data provide evidence that protein solubility of the specific region in target proteins may contribute to the antigenicity.

AB - HtrA2/Omi, a mitochondrial serine protease, is pivotal in regulating apoptotic cell death. To determine the location of antigenic determinants in HtrA2/Omi, we expressed a series of the N-terminally truncated HtrA2/Omi as GST fusion proteins in E. coli. We assessed protein solubility and antigenic reactivity of various N-terminally truncated HtrA2/Omi proteins by binding to glutathione beads and immunoblot analyses, respectively. We identified that the region encoded by exon8 of HtrA2/Omi was expressed as a highly soluble form and contains an antigenic determinant specifically recognized by a polyclonal serum against HtrA2/Omi. Our data provide evidence that protein solubility of the specific region in target proteins may contribute to the antigenicity.

KW - Antigenic determinant

KW - Exon8

KW - Protein solubility

KW - pGEX expression

UR - http://www.scopus.com/inward/record.url?scp=0141638591&partnerID=8YFLogxK

U2 - 10.1023/A:1025630013679

DO - 10.1023/A:1025630013679

M3 - Article

C2 - 14584913

AN - SCOPUS:0141638591

SN - 0141-5492

VL - 25

SP - 1597

EP - 1603

JO - Biotechnology letters

JF - Biotechnology letters

IS - 19

ER -

Antigenicity of the region encoded by exon8 of the human serine protease, HtrA2/Omi, is associated with its protein solubility

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this