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Current Trends in Biotechnology and Pharmacy Vol. 5 (3) 1309-1317 July 2011, ISSN 0973-8916 (Print), 2230-7303 (Online) 1317 21. James, C.C., Joseph, G. J., Hugh, A.G., Loren, D.S., William, M.H., Kathrin, U. J., Robert, W. H., Charlotte, I.P., Robert, S. L., Paul M. K. and E Dale, L. (1999). Purification of Virus-like Particles of Recombinant Human papillomavirus Type 11 Major Capsid Protein L1fr‘om Saccharomyces cerevisiae. Prot. Expr. Pur. 17: 477–484 22. Hindmarsh, P.L. and Laimins, L.A. (2007). Mechanisms regulating expression of the HPV 31L1 and L2 capsid proteins and pseudovirion entry. Virol. J., 4:19 23. Reading, D.S., Hallberg, R.L. and Myers, A.M. (1989). Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature, 337(6208): 655- 659 24. Martina, B.M., Nina, M., Mia L., Lawrence B. and Helena, S.G. (2010). Modification of Human Papillomavirus Minor Capsid Protein L2 by Sumoylation. J. Virol., 84: 11585-11589 25. Roden, R. and T. C. Wu. (2006). How will HPV vaccines affect cervical cancer Nat. Rev. Cancer. 6: 753–763 26. B Karanam, S Jagu, Huh WK and Roden R (2009). Developing vaccines against minor capsid antigen L2 to prevent papillomavirus infection. Immunol Cell Biol., 87(4): 287–299. Expression of recombinant minor capsid protein of HPV in Pichia pastoris
Current Trends in Biotechnology and Pharmacy Vol. 5 (3) 1318 -1324 July 2011, ISSN 0973-8916 (Print), 2230-7303 (Online) Docking and Molecular Modelling of the Target - Penicillin Binding Protein -1A of Haemophilus influenzae B.N. Ramya Jyothi, K. Siva Prasad and S. Krupanidhi* Centre for Bioinformatics, Department of Zoology, Sri Venkateswara University, Tirupati – 517 502. A.P. India. *Department of Biosciences, Sri Satya Sai Institute of Higher Learning, Prasanthi Nilayam - 515 134, India *For Correspondence - krupanidhi_srirama@rediffmail.com 1318 Abstract Penicillin binding protein-1A (PBP-1A; IPR011816) plays a pivotal role in the biogenesis of cell-wall and biosynthesis of peptidoglycan in bacteria. It is considered to be a novel target for pneumonia. The present study is to deduce the structure of the PBP-1A using ICM Molsoft and to validate the same with Ramachandran plot. These bioinformatics tools have been used to identify a lead molecule against PBP-1A of Haemophilus influenza. The proposed model structure is further explored for in silico docking studies with suitable inhibitors. The docking scores indicated that the ampicillin could be a better inhibitor among the seven antibiotics chosen in the present investigation. Key words: Haemophilus influenzae strain 86- 028NP, PBP protein, ICM Molsoft, Argus lab 4.0.1, Gold. Introduction Pneumonia is an inflammation of lungs, usually caused by a pathogen. Three common causative groups of pathogens that cause pneumonia are bacteria, viruses and fungi (1). The people at risk are older than 65 or younger than 2 years of age, or those with impaired immunity. Some of the gram-negative bacteria that cause pneumonia include Haemophilus influenzae (HI), Klebsiella pneumoniae, Escherichia coli, Pseudomonas aeruginosa and Moraxella catarrhalis. HI is a non-motile gram-negative bacterium belonging to the family Pasteurellaceae. Pneumonia caused by HI seems to occur exclusively among humans. HI was first isolated by Pfeiffer during the influenza pandemic of 1890. This pathogen is present in the nasopharynx of approximately 75 percent of healthy children and adults. It is rarely encountered in the oral cavity and has not been detected in any other animal species (2). HI was the first pathogenic organism to have its entire genome sequenced during the year 1995 (3). Bacterial cell wall and PBPs are the targets for drugs of selective toxicity because the related metabolic pathways and enzymes are unique to prokaryotes (4). Whereas, mitogen-activated protein kinase and trypanothione reductase are considered as targets in a eukaryotic protozoan parasite viz., Leishmania infantum (5, 6). However, in bacterial system, PBPs have been shown to catalyse a variety of reactions involved in the process of synthesizing cross-linked peptidoglycan from lipid intermediates and mediate the removal of D-alanine from the precursor of peptidoglycan (7). PBP-1A in HI strain 86-028np is coded by mrcA gene. This possesses two domains viz., penicillin-insensitive transglycosylase EC=2.4.2.- and penicillin- Docking of the penicillin binding protein of Haemophilus influenzae
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(December 7-9, 2011) Venue: Karunya
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