Paragonimus westermani: Identification and characterization of the fasciclin I domain-containing protein

• Published in: Experimental parasitology 2010-06, Vol.125 (2), p.76-83
• Main Authors: Song, Su-Min, Shin, Jong-Won, de Guzman, Jefferson V., Kim, Jin, Yu, Hak-Sun, Jha, Bijay Kumar, Kong, Hyun-Hee, Hong, Yeonchul, Chung, Dong-Il
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal - immunology; Astacoidea; Base Sequence; Cell Adhesion; Cell Adhesion Molecules, Neuronal - chemistry; Cell Adhesion Molecules, Neuronal - genetics; Cell Adhesion Molecules, Neuronal - immunology; Cell Adhesion Molecules, Neuronal - isolation & purification; Cloning, Molecular; DNA, Complementary - chemistry; Dogs; Extracellular matrix; Fasciclin-I/βig-h3 domain; Fibroblasts - cytology; Fibroblasts - drug effects; Helminth Proteins - chemistry; Helminth Proteins - genetics; Helminth Proteins - immunology; Helminth Proteins - isolation & purification; Immune Sera - immunology; Immunohistochemistry; Integrin; Male; Marine; Paragonimus; Paragonimus westermani; Paragonimus westermani - chemistry; Paragonimus westermani - genetics; Paragonimus westermani - metabolism; Rats; Rats, Sprague-Dawley; Recombinant Proteins - chemistry; Trematode
• ISSN: 0014-4894; 1090-2449
• DOI: 10.1016/j.exppara.2009.12.022

Paragonimus westermani is a trematode parasite that causes inflammatory lung disease as well as systemic infections in carnivorous mammals. The interaction of the parasite with host cells and paired worms is initiated by adhesion and plays an important role in parasite proliferation and differentiation. In this study, we isolated a cDNA encoding a P. westermani fasciclin I domain-containing protein (Pwfas-I). The fasiclin-I domain is suggested to be involved in cell adhesion, migration, and differentiation. Immunohistochemical analysis of P. westermani adult worms with polyclonal anti-Pwfas-I serum revealed immunoreactivity in the egg shells and the cells lining the sub-tegumental layer of adult worm throughout the contact regions of the cyst wall and paired worms. Using cell adhesion and spreading assays, we showed that Pwfas-I supports cell adhesion and spreading. Furthermore, we determined that the ανβ5 integrin was a functional receptor for the Pwfas-I. Taken together, these results suggest that Pwfas-I may be functional for the modulation of cell adhesion via binding with ανβ5 integrin in the extracellular matrix of Paragonimus.