Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides

Hitoshi Tsugawa, Asako Ogawa, Satomi Takehara, Mayumi Kimura, Yoshio Okawa

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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 languageEnglish
Pages (from-to)10-16
Number of pages7
JournalFEMS microbiology letters
Issue number1
Publication statusPublished - 2008 Apr
Externally publishedYes


  • Apoptosis
  • Cytotoxic outer-membrane protein (ComP)
  • Molecular cloning
  • Plesiomonas shigelloides
  • Structure

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics


Dive into the research topics of 'Primary structure and function of a cytotoxic outer-membrane protein (ComP) of Plesiomonas shigelloides'. Together they form a unique fingerprint.

Cite this