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Role of Salicylidene Acylhydrazide and Proteases in Biofilm Inhibition of Desulfovibrio spp.

Role of Salicylidene Acylhydrazide and Proteases in Biofilm Inhibition of Desulfovibrio spp.

Iram Liaqat1,*, Nazish Mazhar Ali2, Najma Arshad3, Riffat Iqbal1 and Zain-ul-Abideen1

1Department of Zoology, Govt. College University, Lahore-54000
2Department of Zoology, Govt. College for Women, Model town, Lahore-54000
3Department of Zoology, University of the Punjab, Lahore-54000

*      Corresponding author: iramliaq@hotmail.com

 

ABSTRACT

This study has highlighted that several compounds including salicylidene acylhydrazide, proteinase k, trypsin and chymotrypsin target bacterial virulence in Desulfovibrio spp. that causes bacteremia, periodontitis and abdominal infections. Ten soil samples were collected and screened by morphological and biochemical study. Only one strain DUV1 was confirmed by 16S rRNA gene sequencing as D. vulgaris (accession number: KY698020). It showed significantly reduced biofilm formation (52%; p<0.05) by test tube method compared to liquid interface coverslip assay (35%) and congo red assay. D. vulgaris was treated with various concentrations (5, 40, 80 and 100µM) of salicylidene acylhydrazide and 5-15 µM of proteases (proteinase K, trypsin, and chymotrypsin). Concentration dependent decrease was observed after 72 hours in biofilm formation of D. vulgaris on treatment with salicylidene acylhydrazide. Whereas 15 µM concentration of proteases produced significantly (p<0.05) reduced biofilm formation via test tube assay. Overall, while comparing all inhibitory compounds trypsin was most effective in decreasing biofilm formation followed by chymotrypsin > proteinase k > salicylidene acylhydrazides. Our study indicated that inhibitory compounds may disrupt the protein filament of flagellar apparatus producing significantly controlled biofilm formation which might also be helpful to control clinical infections associated with Desulfovibrio spp.

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Pakistan Journal of Zoology

April

Pakistan J. Zool., Vol. 56, Iss. 2, pp. 503-1000

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