MAIN


©1996-2019. All Rights Reserved. Online Journal of Bioinformatics . You may not store these pages in any form except for your own personal use. All other usage or distribute on is illegal under international copyright treaties. Permission to use any of these pages in any other way besides the  before mentioned must be gained in writing from the publisher. This article is exclusively copyrighted in its entirety to OJB publications. This article may be copied once but may not be, reproduced or  re-transmitted without the express permission of the editors. This journal satisfies the refereeing requirements (DEST) for the Higher Education Research Data Collection (Australia). Linking:To link to this page or any pages linking to this page you must link directly to this page only here rather than put up your own page.


OJBTM

 Online Journal of Bioinformatics © 

 Volume 12(1):18-33, 2011


Comparative evolutionary analysis of metallo-β-lactamases with reference to NDM1

 

Odedra D1 (M.Sc), Mallick M1 (M.Sc), Vidyarthi AS1 (Ph.D), Shankaracharya1* (M.Sc)

 

Department of Biotechnology, Birla Institute of Technology, Mesra, Ranchi

 

ABSTRACT

Odedra D, Mallick M, Vidyarthi AS, Shankaracharya D, Comparative evolutionary analysis of metallo-β-lactamases with reference to NDM1, Onl J Bioinform., 12(1):18-33, 2011. The amino acid sequences of Metallo-β-lactamases in fast evolving carbapenem resistant E. coli and K. pneumoniae were used for addressing demographic relationships on an evolutionary scale. The study was undertaken to establish the relation of New Delhi metallo-β-lactamase (NDM1) with various other types of metallo-β-lactamases. Results demonstrated well resolved topologies of trees indicating separate line of evolution of NDM1 from other types of metallo-β-lactamases. This was the first systematic study to establish a substitution rate as high as 0.0005 substitutions per site per year for NDM1. Structural alignment of Metallo-β-lactamases from various bacterial strains revealed a highly conserved zinc binding motif His116-X-His118-X-Asp120. This estimate fairly mirrored the quick and regular emergence of new variant forms of metallo-β-lactamases. However, none of the trees could demonstrate geographical separation suggesting the spread of bacterial isolates due to geographical migration of patients for seeking medical services.

 

Keywords: metallo-β-lactamases, NDM1, carbapenem resistance, evolution


MAIN

 

FULL-TEXT(SUBSCRIPTION OR PURCHASE TITLE $25USD)