Functional and immunological characterization of an elicitin-like protein of the pathogenic oomycete Pythium insidiosum
11
Issued Date
2014
Resource Type
Language
eng
Call No.
Q179.9 A816s 2014 [LICL,LIEN,LIPT]
Rights
Mahidol University
Rights Holder(s)
Faculty of Graduate Studies Mahidol University
Physical Location
Central Library
Environment and Resource Studies Library
Faculty of Physical Therapy, Surasak Srisuk Library
Environment and Resource Studies Library
Faculty of Physical Therapy, Surasak Srisuk Library
Suggested Citation
Tassanee Lerksuthirat, Tassanee Lowhnoo, Wanta Yingyong, Theerapong Krajaejun (2014). Functional and immunological characterization of an elicitin-like protein of the pathogenic oomycete Pythium insidiosum. Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/61247
Title
Functional and immunological characterization of an elicitin-like protein of the pathogenic oomycete Pythium insidiosum
Abstract
Pythiosis is a life-threatening infectious disease of humans and animal living in tropical and subtropical countries, and caused by the pathogenic oomycete Pythium insidiosum. Pythiosis in humans has been reported mostly from Thailand. Most patients usually come with clinical symptoms resulting from arterial (vascular pythiosis) or corneal (ocular pythiosis) infection. Morbidity and mortality of pythiosis are markedly high. Unfortunately, there is no effective medical treatment for pythiosis, leaving extensive surgical removal the only options. Most patients with vascular pythiosis had their infected leg amputated, and those with ocular infection had their eye removed. Many patients died from the advanced stage of the disease. Basic information on pathogenesis of this disease, which could lead to a new method of infection control, is very limited. Recently, we have generated an expressed sequence tag database (ESTdb) of P. insidiosum. Bioinformatics analysis of the ESTdb revealed a number putative virulence factors. Among them, elicitins are an interesting group of protein, due to they are unique (not present in other human pathogens), and sterol binding molecules. A recombinant elicitin-like protein#025 (rELI025) was successfully expressed in Escherichia coli, and purified using an affinity column. Biological and immunological properties of ELIs have been explored. Molecular techniques using rabbit anti-ELI antibody showed that ELI was a secreted protein. Different strains of P. insidiosum produced different amount of ELI025. Serum samples from different patients with pythiosis showed various immunoreactivity against rELI025. Based on the rDNA sequence, P. insidiosum can be grouped into three phylogenetic clades: Clade I-III. The ELI025-encoding gene from the strains in Clade III cannot be detected by PCR. In conclusion, we report here rELI025 as the first recombinant protein of P. insidiosum to be molecularly investigated, which could be a virulence factor necessary for pathogenesis, a phylogenetic marker, and a potential therapeutic target.
Description
Proceeding of the 2nd ASEAN plus three graduate research congress, Bangkok. February 5-7, 2014.