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ISSN: 2168-9547

Molecular Biology: Open Access
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Research Article

Conservation of Properties of Outer Membranes Protein across Host Genera of Pasteurella multocida Suggests Common Mechanism of Action

Neetesh Pandey, Monendra Grover* and Anil Rai

Centre for Agricultural Bio-Informatics, ICAR-Indian Agricultural Statistics Research Institute, Library Avenue, PUSA, New Delhi, India

*Corresponding Author:
Monendra Grover
Centre for Agricultural Bio-Informatics
ICAR-Indian Agricultural Statistics Research Institute
Library Avenue, PUSA, New Delhi, India
E-mail: [email protected]

Received date: April 07, 2016 Accepted date: April 18, 2016 Published date: April 11, 2016

Citation: Pandey N, Grover M, Rai A (2016) Conservation of Properties of Outer Membranes Protein across Host Genera of Pasteurella multocida Suggest Common Mechanism of Action. Mol Biol 5:162. doi: 10.4172/2168-9547.1000162

Copyright: © 2016 Pandey N, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.



Pasteurella multocida is a non-motile coccobacillus pathogenic Gram-negative bacterium and belongs to Pasteurellaceae family. Pasteurella multocida causes diseases in economically important animals and birds in developing and developed countries. Haemorrhagic septicaemia in cattle and buffaloes and other diseases like fowl cholera (turkey, chicken, and duck), Septicaemic pasteurellosis (sheep, pig, and goat) and Snuffles (rabbit) are caused by Pasteurella multocida. In this analysis we have taken three outer membrane proteins (vacJ, ompW and skp) from P. multocida which are involved in infectious diseases of animals and birds. The literature shows that all three outer membrane proteins are infectious in nature. This is supported by multiple sequence alignment and analysis of physicochemical properties of protein sequences encoded by vacJ, ompW and skp outer membrane protein families. The studied proteins are similar with respect to number of positively and negatively charged amino acids, molecular weight, Theoretical pI, instability index and grand average of hydropathicity (Gravy) in the proteins from P. multocida strains infecting different genera. The domains, transmembrane helices, twin arginine signal peptides and ß-barrels are also broadly similar. This suggests common mechanism of action of these proteins across host genera.


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