Indian Journal of Animal Research

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Research Article

Indian Journal of Animal Research, volume 51 issue 1 (february 2017) : 44-51

Impact analysis of missense variants on heat shock protein of farmed carp rohu, Labeo rohita (Hamilton, 1822)

Prajna Pradhan, Kiran Dashrath Rasal*, Dibyashree Swain, Pranati Swain, Jitendra Kumar Sundaray, Pallipuram Jayasankar
1<p>ICAR - Central Institute of Freshwater Aquaculture,&nbsp;Bhubaneswar 751 002, Odisha, India.</p>
Cite article:- Pradhan Prajna, Rasal* Dashrath Kiran, Swain Dibyashree, Swain Pranati, Sundaray Kumar Jitendra, Jayasankar Pallipuram (2016). Impact analysis of missense variants on heat shock protein offarmed carp rohu, Labeo rohita (Hamilton, 1822) . Indian Journal of Animal Research. 51(1): 44-51. doi: 10.18805/ijar.9645.

ABSTRACT

The progress in the computational field is advantageous for investigating the impact of missense variants/mutation on the protein structure-function. The impact analyses of variants on the genes/proteins using in vivo laboratory methods are laborious and time consuming. Thus, the present study was performed for investigating the impact of missense mutations on the Heat-shock proteins (HSP70) of farmed carp, rohu, Labeo rohita. We have used several sequence-based computational tools/algorithms such as SIFT, PANTHER, PROVEAN and I-Mutant2.0. We have depicted that all mutations (p.G6V, p.A56I, and p.A159T) in the HSP70 were deleterious. The 3D model of HSP70 of rohu was generated using Modeller9.14 and subsequently validated using SAVEs server. The Ramachandran plot shown that shifting of residues in the mutant structure towards the disallowed region due to mutation as compared to native counterpart. The ERAT score and PROSA score, also given clues of deteriorating quality of mutant protein HSP70. Moreover, STRING9.1 shown that HSP70 protein interacting with several proteins and strong association was observed with two proteins, hsp90 and dnajb (Hsp40 homolog). The RMSD was obtained 0.04Å between native and mutant structure. The present study will helpful for understanding the impact of missense mutations on the HSP70 of rohu using in vivo methods. This study enriched for further exploring disturbances of protein-protein interaction mechanism as well as associated molecular pathways. 

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