Structure Based Functional Annotation of Putative Conserved Proteins from Treponema Pallidum: Search for a Potential Drug Target

ISSN: 1875-628X (Online)
ISSN: 1570-1808 (Print)


Volume 11, 10 Issues, 2014


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Structure Based Functional Annotation of Putative Conserved Proteins from Treponema Pallidum: Search for a Potential Drug Target

Author(s): Avni Sinha, Faizan Ahmad and Md. Imtaiyaz Hassan

Affiliation: Center for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi – 110025, India.

Abstract

Treponema pallidum, a Gram negative bacterium, causes chronic disease, syphilis, a sexually transmitted disease. T. pallidum penetrates dermal microabrasions or intact mucous membranes resulting in varieties of symptoms. The complete genome for T. pallidum was sequenced, which contains approximately 1,090 genes encoding approximately 1,041 proteins [1]. These open reading frames account for a large number of hypothetical proteins (HPs), for which no experimental evidences are available. Being a virulent and not very well characterized organism, it is essential to analyze these HPs whose structure and function are not known. Here, our aim is to predict structure and ultimately function of HPs using combination of modern bioinformatics tools. We successfully modeled the structures of six HPs with high accuracy, which possess endonuclease, NTP transferase, transcription regulator and DNA-binding activities. We further performed virulence search to check their potential role in pathogenicity. The unique sequence of a given HP is often key determinants for its structure and hence function. The structure analysis will provide better insight into the function of a particular protein. We believe that these analyses expand our knowledge regarding the functional roles of HPs of T. pallidum and provide an opportunity to validate novel potential drug targets.

Keywords: Homology modeling, Sequence analysis, Structural genomics, Treponema pallidum, Virulence factor and Function prediction

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Article Details

Volume: 11
First Page: 1
Last Page: 14
Page Count: 14
DOI: 10.2174/1570180811666140806005822
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