Abstract
We previously isolated and characterized a 40-kDa cytotoxic outer-membrane protein (ComP) produced by Plesiomonas shigelloides strain P-1 (P-1). Sequence analysis of the comP gene revealed a coding region of 1068 bp, with a predicted mature protein composed of 335 amino acids and a molecular mass of 38.597 kDa. Three-dimensional structural modeling of ComP suggests that it has a β-barrel structure with 16 transmembrane strands, eight short periplasmic turns and eight external loops. blast search results and protein modeling suggest that ComP may be a novel porin protein of P. shigelloides. In order to understand the role of ComP during P. shigelloides infection, we constructed a deletion mutant strain (P. shigelloides ΔcomP; P-1201), and compared the pathogenicity of P-1201 vs. the wild-type strain P-1 in Caco-2 cells. Unlike P-1, the deletion strain P-1201 was not cytotoxic to Caco-2 cells and did not lead to apoptosis. These data indicate that ComP may be the predominant virulence factor that triggers cell death in the host cells following infection.
| Original language | English |
|---|---|
| Pages (from-to) | 10-16 |
| Number of pages | 7 |
| Journal | FEMS Microbiology Letters |
| Volume | 281 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2008 Apr |
| Externally published | Yes |
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Keywords
- Apoptosis
- Cytotoxic outer-membrane protein (ComP)
- Molecular cloning
- Plesiomonas shigelloides
- Structure
ASJC Scopus subject areas
- Genetics
- Molecular Biology
- Applied Microbiology and Biotechnology
- Microbiology
Cite this
Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides. / Tsugawa, Hitoshi; Ogawa, Asako; Takehara, Satomi; Kimura, Mayumi; Okawa, Yoshio.
In: FEMS Microbiology Letters, Vol. 281, No. 1, 04.2008, p. 10-16.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides
AU - Tsugawa, Hitoshi
AU - Ogawa, Asako
AU - Takehara, Satomi
AU - Kimura, Mayumi
AU - Okawa, Yoshio
PY - 2008/4
Y1 - 2008/4
N2 - We previously isolated and characterized a 40-kDa cytotoxic outer-membrane protein (ComP) produced by Plesiomonas shigelloides strain P-1 (P-1). Sequence analysis of the comP gene revealed a coding region of 1068 bp, with a predicted mature protein composed of 335 amino acids and a molecular mass of 38.597 kDa. Three-dimensional structural modeling of ComP suggests that it has a β-barrel structure with 16 transmembrane strands, eight short periplasmic turns and eight external loops. blast search results and protein modeling suggest that ComP may be a novel porin protein of P. shigelloides. In order to understand the role of ComP during P. shigelloides infection, we constructed a deletion mutant strain (P. shigelloides ΔcomP; P-1201), and compared the pathogenicity of P-1201 vs. the wild-type strain P-1 in Caco-2 cells. Unlike P-1, the deletion strain P-1201 was not cytotoxic to Caco-2 cells and did not lead to apoptosis. These data indicate that ComP may be the predominant virulence factor that triggers cell death in the host cells following infection.
AB - We previously isolated and characterized a 40-kDa cytotoxic outer-membrane protein (ComP) produced by Plesiomonas shigelloides strain P-1 (P-1). Sequence analysis of the comP gene revealed a coding region of 1068 bp, with a predicted mature protein composed of 335 amino acids and a molecular mass of 38.597 kDa. Three-dimensional structural modeling of ComP suggests that it has a β-barrel structure with 16 transmembrane strands, eight short periplasmic turns and eight external loops. blast search results and protein modeling suggest that ComP may be a novel porin protein of P. shigelloides. In order to understand the role of ComP during P. shigelloides infection, we constructed a deletion mutant strain (P. shigelloides ΔcomP; P-1201), and compared the pathogenicity of P-1201 vs. the wild-type strain P-1 in Caco-2 cells. Unlike P-1, the deletion strain P-1201 was not cytotoxic to Caco-2 cells and did not lead to apoptosis. These data indicate that ComP may be the predominant virulence factor that triggers cell death in the host cells following infection.
KW - Apoptosis
KW - Cytotoxic outer-membrane protein (ComP)
KW - Molecular cloning
KW - Plesiomonas shigelloides
KW - Structure
UR - http://www.scopus.com/inward/record.url?scp=40349106440&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=40349106440&partnerID=8YFLogxK
U2 - 10.1111/j.1574-6968.2007.01041.x
DO - 10.1111/j.1574-6968.2007.01041.x
M3 - Article
VL - 281
SP - 10
EP - 16
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1
ER -