Frequent-subsequence-based prediction of outer membrane proteins

  • Authors:
  • Rong She;Fei Chen;Ke Wang;Martin Ester;Jennifer L. Gardy;Fiona S. L. Brinkman

  • Affiliations:
  • Simon Fraser University;Simon Fraser University;Simon Fraser University;Simon Fraser University;Simon Fraser University;Simon Fraser University

  • Venue:
  • Proceedings of the ninth ACM SIGKDD international conference on Knowledge discovery and data mining
  • Year:
  • 2003

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Abstract

A number of medically important disease-causing bacteria (collectively called Gram-negative bacteria) are noted for the extra "outer" membrane that surrounds their cell. Proteins resident in this membrane (outer membrane proteins, or OMPs) are of primary research interest for antibiotic and vaccine drug design as they are on the surface of the bacteria and so are the most accessible targets to develop new drugs against. With the development of genome sequencing technology and bioinformatics, biologists can now deduce all the proteins that are likely produced in a given bacteria and have attempted to classify where proteins are located in a bacterial cell. However such protein localization programs are currently least accurate when predicting OMPs, and so there is a current need for the development of a better OMP classifier. Data mining research suggests that the use of frequent patterns has good performance in aiding the development of accurate and efficient classification algorithms. In this paper, we present two methods to identify OMPs based on frequent subsequences and test them on all Gram-negative bacterial proteins whose localizations have been determined by biological experiments. One classifier follows an association rule approach, while the other is based on support vector machines (SVMs). We compare the proposed methods with the state-of-the-art methods in the biological domain. The results demonstrate that our methods are better both in terms of accurately identifying OMPs and providing biological insights that increase our understanding of the structures and functions of these important proteins.