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The involvement of an integrin-like protein and protein kinase C in amoebic adhesion to fibronectin and amoebic cytotoxicity

Authors
 Kyu-Lee Han  ;  Hyun-Ju Lee  ;  Soon-Jung Park  ;  Kyung-Il Im  ;  Ho-Joon Shin  ;  Myeong Heon Shin 
Citation
 PARASITOLOGY RESEARCH, Vol.94(1) : 53-60, 2004 
Journal Title
PARASITOLOGY RESEARCH
ISSN
 0932-0113 
Issue Date
2004
MeSH
Animals ; CHO Cells ; Cell Adhesion ; Cricetinae ; Fibronectins/metabolism* ; Gene Expression Regulation ; Integrins/metabolism* ; Naegleria fowleri/pathogenicity* ; Naegleria fowleri/physiology* ; Protein Kinase C/metabolism* ; Signal Transduction
Keywords
Integrin ; Chinese Hamster Ovary Cell ; Integrin Antibody ; Primary Amoebic Meningoencephalitis ; Immobilize Bovine Serum Albumin
Abstract
Adherence of a pathogen to the host cell is one of the critical steps in microbial infections. Naegleria fowleri, a causative agent of primary amoebic meningoencephalitis in humans, is expected to interact with extracellular components of the host, such as fibronectin, in a receptor-mediated mode. In this study, we investigated the interaction between N. fowleri and fibronectin to understand its cytopathology. In binding assays using immobilized fibronectin, the number of amoebae bound to fibronectin was increased compared to the controls, and was dependent on the amount of coated fibronectin present. A fibronectin binding protein of 60 kDa was found in extracts of N. fowleri. Western blot and immunolocalization assays using integrin α5/FnR antibodies showed that a 60 kDa protein reacted with the antibodies in extracts of N. fowleri, which was localized on the surface of N. fowleri. Preincubation of N. fowleri with the integrin antibodies significantly inhibited amoebic binding to fibronectin and cytotoxicity to the CHO cells. Additionally, protein kinase C activity was detected in the extract of N. fowleri. When N. fowleri was pretreated with protein kinase C activator or inhibitor, the abilities of amoebic adhesion to fibronectin and cytotoxicity to the host cells were markedly affected compared to untreated amoebae. These results suggest that an amoebic integrin-like receptor and protein kinase C play important roles in amoebic cellular processes in response to fibronectin.
Full Text
http://link.springer.com/article/10.1007%2Fs00436-004-1158-9
DOI
10.1007/s00436-004-1158-9
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Park, Soon Jung(박순정) ORCID logo https://orcid.org/0000-0002-0423-1944
Shin, Myeong Heon(신명헌) ORCID logo https://orcid.org/0000-0001-8207-6110
Im, Kyung Il(임경일)
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/111266
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