Molecular structural analysis of antibacterial factor proteins from Ascaris suum

College

College of Science

Department/Unit

Biology

Document Type

Conference Proceeding

Source Title

Proceedings of the Thirteenth OU-DLSU Academic Research Workshop

First Page

24

Last Page

26

Publication Date

2010

Abstract

A large number of invertebrates has recently been used as models in the study of innate immunity. Kato (1995) previously reported antibacterial property exhibited in the pseudocoelom of the nematode Ascaris suum. The antibacterial activity was due to a heat-stable and trypsin-sensitive protein designated as ASABF (Ascaris suum Antibacterial Factor). Several studies have been carried out in the purification, determination of primary structure and cDNA cloning of ASBF. Transcription induction studies reported that ASBF occurs as a type form a, followed by five recently identified novel members namely β, y, δ, ε and ζ. Amino acid sequence alignment revealed several amino acid changes except the presence of six highly conserved cysteine residues previously identified in insect/arthropod defensins. Until recently, there are only few studies which investigate the three-dimensional structure ASABF proteins. This paper presents molecular comparison between ASABF proteins by computer modeling. Analyzing molecular changes through structure molecular graphics and model building analysis further help in the understanding of mechanisms involved in antibacterial property and subsequent drug design.

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Disciplines

Biochemistry, Biophysics, and Structural Biology

Note

Undated; publication/creation date supplied

Keywords

Nematodes; Antibacterial agents

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