Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/15241
Title: Probing the evolutionary conserved regions within functional site of drug-resistant target proteins of Staphylococcus aureus: In silico phylogenetic motif profiling approach
Authors: Kahlon, Amandeep Kaur
Darokar, Mahendra P
Sharma, Ashok
Keywords: Multi-drug resistance
Staphylococcus aureus
Domain
Co-target
Phylogenetic similarity threshold
Phylogenetic motifs
Interactome analysis
Drug-resistant genes
Conserved residues
Functional partners
Issue Date: Dec-2012
Publisher: NISCAIR-CSIR, India
Abstract: Staphylococcus aureus is one of the major causes of clinical infections and increasing mortality due to multi-drug resistance. In this study, eight drug-resistant genes, beta-lactamase, metallo-beta-lactamase, vanB, mecA, norA, qacA, qacB and qacC of S. aureus strain Mu50 (vancomycin resistant) were studied to predict the evolutionary conserved functional site residues in their protein sequences. It was found that in beta-lactamase, Tyr, Gly, Thr, Asn and in metallo-beta-lactamase, Thr, His, Gly, Leu, Arg and Asp residues were highly conserved. In vanB, Gly, His and Asp residues were highly conserved. Whereas in mecA, His, Val, Phe, Gln, Lys and in norA, Ser, Leu and Ala residues showed conservedness at moderate level. In the multi-drug efflux pump (corresponding to qacA, qacB and qacC), Gly residue was found to be highly conserved. The homology clustering of target proteins through SCI-PHY algorithm and homologues identified through PSI-BLAST were compared to identify the degree of conservation of functional residues. The phylogenetic motifs identified using homologues of target proteins were validated through domain search to locate their site and functionality in the protein sequences. Interactome analysis was performed to understand the possible mode of interaction of target proteins with their functional partners.
Description: 442-450
URI: http://hdl.handle.net/123456789/15241
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.49(6) [December 2012]

Files in This Item:
File Description SizeFormat 
IJBB 49(6) 442-450.pdf273.86 kBAdobe PDFView/Open


Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.