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Online Journal of Bioinformatics©
 

Volume 6 (2):74-90, 2005.


In silico identification and modelling of a putative iron-regulated TonB-dependant outer membrane

receptor protein from the genome of Leptospira interrogans serovar Lai.

 

Sritharan M, Ramadevi S, Pasupala N, Asuthkar S, Tajne S.

 

Department of Animal Sciences, University of Hyderabad and Informatics Division, GVK Biosciences Pvt Ltd, Hyderabad, India

 

ABSTRACT

 

Sritharan M, Ramadevi S, Pasupala N, Asuthkar S, Tajne S., In silico identification and modelling of a putative iron-regulated TonB-dependant outer membrane receptor protein from the genome of Leptospira interrogans Serovar Lai, Onl J Bioinform., 6 (2):74-90, 2005. Identification and modelling of a leptospiral TonB-dependant outer membrane protein homologous to Fe3+-enterobactin receptor FepA of Escherichia coli is described.  This protein LEP_IRMP (leptospiral iron-regulated membrane protein), has a fold of 3 domains: the β-barrel, plug domain and N-terminal TonB box, characteristic of bacterial outer membrane receptors involved in the transport of iron. The Fur box was identified upstream of the lep_irmp gene encoding this protein, implying the possible regulation of its expression by iron. Also, the genes for the Fur regulator and heme oxygenase are found as neighbourhood genes. The FRAP-NPNL motif involved in heme binding is present in LEP_IRMP. Using sequence-specific primers, the full-length lep irmp gene in several pathogenic Leptospira sp. and absence in non-pathogenic leptospires has been identified. The possible role of the protein in heme binding by pathogenic leptospires is discussed in the light of the above observations as well as the failure to detect siderophores under conditions of iron deprivation.

 

KEY WORDS: iron, TonB-dependant outer membrane protein, LEP_IRMP, Leptospira, plug domain, β-barrel domain, N-terminal TonB box, heme binding.


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