Hydrophobicity and surface electrostatic charge of conidia of the mycoparasitic <Emphasis Type="Italic">Trichoderma</Emphasis> species |
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Authors: | Tanuja?Singh Ratul?Saikia Tarakanta?Jana Email author" target="_blank">Dilip?K?AroraEmail author |
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Institution: | (1) Glyco-Immunochemistry Research Lab., Institute of Molecular and Cellular Biology, College of Medicine, Chang-Gung University, Kwei-San, Tao-Yuan, 333, Taiwan;(2) National Bureau of Agriculturally Important Microorganisms, NBPGR Old Bldg., Pusa Campus, New Delhi, 110012, India;(3) National Research Centre on Plant Biotechnology, Indian Agricultural Research Institute, Pusa, New Delhi, 110012, India |
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Abstract: | The present investigation was done to understand the fungal-fungal interactions mechanisms based on level of nonspecific adhesion
of a potential fungal mycoparasite (Trichoderma) to their fungal host (Macrophomina phaseolina). The relative cell surface hydrophobicity (CSH) and cell surface electrostatic charge (CSEC) of 29 isolates of Trichoderma species, analyzed by bacterial adhesion to hydrocarbon (BATH), hydrophobic interaction chromatography (HIC), microelectrophoresis
and contact angle, revealed a large degree of variability. CSH and CSEC of conidia depended on culture age, pH and temperature.
Maximum CSH and CSEC were recorded in 25–28 °C range, and both declined significantly with increasing temperature. Isolate
Trichoderma hazianum (Th)-23/98 expressed surface hydrophobicity at 25–28 °C and hydrophilicity at 40 °C. Surface hydrophobicity of the isolate was
susceptible to various proteases (trypsin, pepsin, proteinase k and a-chymotrypsin) and inhibitors (SDS, mercaptoethanol and
Triton X-100) and a significant reduction in CSH was recorded in hydrophobic conidia. Hydrophilic conidia remained more or
less unaffected by such treatments. SDS-PAGE analysis of the hydrophobic and hydrophilic conidia exhibited several protein
bands in the 25 to 61 kDa range. However, each protein population contained one protein that was not observed in the other
population. For hydrophobic conidia, the unique protein had an apparent molecular mass of 49 kDa, while the unique protein
associated with hydrophilic conidia had a molecular mass of 61 kDa. Our findings suggest that CSH and CSEC of mycoparasitic
Trichoderma may contribute to non-specific adhesion on to the sclerotial surfaces of Macrophomina phaseolina that may be influenced by growth and environmental conditions. |
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