Molecular structural analysis of antibacterial factor proteins from Ascaris suum
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 desig...
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| Format: | text |
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Animo Repository
2010
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| Online Access: | https://animorepository.dlsu.edu.ph/faculty_research/8597 |
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| Institution: | De La Salle University |
| Summary: | 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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