The Native Gene of Anti-Lps Factor from Tachypleus tridentatus: Cloning, Expression and its Bacteriostatic Activity in Vitro

Authors: Wang D-N.; Chen L.; Liu J-W.; He Z-Y.; Zhang W-J.; Wu X-F.

Source: Protein and Peptide Letters, Volume 8, Number 4, August 2001 , pp. 273-280(8)

Publisher: Bentham Science Publishers

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Abstract:

The native gene information of anti-LPS factor from Tachypleus tridentatus was first reported in this study. The total RNA was extracted from amebocytes of Tachypleus tridentatus and the first-strand cDNA was synthesized by RT-PCR. Then the amplified cDNA of TALF was cloned and expressed in Pichia pastoris. The biological activity of the recombinant proteins obtained have been confirmed by LPS neutralization assay and bacteriostatic assay in vitro.

Keywords: ANTI-LPS FACTOR; TACHYPLEUS TRIDENTATUS; CLONING, EXPRESSION; BACTERIOSTATIC ACTIVITY; Lipopolysaccharide (LPS); Endotoxin; Limulus polyphemus; Degenerate Oligonucleotides; Degenerate Oligonucleotides; LPS neutralization assay; Bacteriostatic assay

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929866013409337

Publication date: 2001-08-01

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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.