Prediction of mycoplasma hominis proteins targeting in mitochondria and cytoplasm of host cells and their implication in prostate cancer etiology
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Shahanavaj Khan1,2, Mohammed Zakariah3, Christian Rolfo4, Lembrechts Robrecht4 and Sellappan Palaniappan5
1Nanomedicine & Biotechnology Research Unit, Department of Pharmaceutics, College of Pharmacy, King Saud University, Riyadh, Saudi Arabia
2Department of Bioscience, Shri Ram Group of College (SRGC), Muzaffarnagar, India
3Research Center, College of Computer and Information Science, King Saud University, Riyadh, Saudi Arabia
4Phase I- Early Clinical Trials Unit, Oncology Department, Antwerp University Hospital, “Centre for Oncological Research (CORE)”, Edegem, Belgium
5School of Science and Engineeringing, Malaysia University of Science and Technology, Selangor, Malaysia
Shahanavaj Khan, e-mail: email@example.com
Christian Rolfo, e-mail: Christian.Rolfo@uza.be
Keywords: M. hominis, database, mitochondria, cytoplasm, prostate cancer
Received: February 09, 2016 Accepted: March 02, 2016 Published: March 23, 2016
Although the idea of bacteria causing different types of cancer has exploded about century ago, the potential mechanisms of carcinogenesis is still not well established. Many reports showed the involvement of M. hominis in the development of prostate cancer, however, mechanistic approach for growth and development of prostate cancer has been poorly understood. In the current study, we predicted M. hominis proteins targeting in the mitochondria and cytoplasm of host cells and their implication in prostate cancer. A total of 77 and 320 proteins from M. hominis proteome were predicted to target in the mitochondria and cytoplasm of host cells respectively. In particular, various targeted proteins may interfere with normal growth behaviour of host cells, thereby altering the decision of programmed cell death. Furthermore, we investigated possible mechanisms of the mitochondrial and cytoplasmic targeted proteins of M. hominis in etiology of prostate cancer by screening the whole proteome.
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