Functional roles of mannose-binding protein in the adhesion, cytotoxicity and phagocytosis of Acanthamoeba castellanii

Jong Hyun Kim, Abdul Matin, Ho Joon Shin, Hyun Park, Kyung Tae Yoo, Xi Zhe Yuan, Kwang Sik Kim, Suk Yul Jung

Research output: Contribution to journalArticle

Abstract

Acanthamoeba castellanii is a single-celled protozoan that is widely distributed in the environment and is a well-known of causing human keratitis, a vision-threatening infection. In this study, an ethyl methane sulfonate (EMS) and a selection of saccharide were applied to A. castellanii by chemical mutagenesis. To understand the functional roles of a mannose-binding protein (MBP). A. castellanii were treated with methyl-alpha- d-mannopyranoside abbreviated Man, with and without the EMS pre-treatment, and their adhesion and cytotoxicity were analyzed, using a human brain microvascular endothelial cell (HBMEC) as the target cell. Both EMS and Man mutants exhibited significantly decreased levels of MBP expression and cytotoxicity to HBMEC, but showed similar levels of binding to HBMEC, as compared with the wild type. Of interest was that the exogenous mannose inhibited amoebae (i.e., Man mutant) binding to the HBMEC by <20%. Only the mutant Man exhibited a significant decrease in bacterial uptake, as compared to the wild type, 0.020 vs 0.032 (p<0.05) and proteolytic activity. The results showed that MBP should be clearly provided as the pathogenic target candidate, to further target-based therapy, but EMS mutation should not be associated with initial adhesion and phagocytosis of A. castellanii.

Original languageEnglish (US)
Pages (from-to)287-292
Number of pages6
JournalExperimental Parasitology
Volume132
Issue number2
DOIs
StatePublished - Oct 1 2012

    Fingerprint

Keywords

  • Acanthamoeba castellanii
  • Ethyl methane sulfonate
  • Mannose binding protein

ASJC Scopus subject areas

  • Parasitology
  • Immunology
  • Infectious Diseases

Cite this