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Macromolecular antimicrobial glycoprotein, achacin, expressed in a methylotrophic yeast Pichia pastoris
Author(s) -
Ogawa Masahiro,
Nakamura Soichiro,
Atsuchi Tetsumori,
Tamiya Toru,
Tsuchiya Takahide,
Nakai Shuryo
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00327-0
Subject(s) - microbiology and biotechnology , biology , pichia pastoris , antimicrobial , staphylococcus aureus , vibrio parahaemolyticus , biochemistry , recombinant dna , bacteria , genetics , gene
A cDNA encoding achacin, an antimicrobial glycoprotein from the body surface mucus of giant African snail Achacina fulica Férussac, was expressed in a methylotrophic yeast, Pichia pastoris , and recombinant achacin (rAch) was secreted in yeast minimal medium in a polyglycosylated form with 80 kDa. Carbohydrate analysis revealed that the glycosylated moiety of rAch was composed of 50 mol mannose and 2 mol N ‐acetylglucosamine residues. Antimicrobial activity using Escherichia coli and Staphylococcus aureus showed that the rAch had a behavior similar to its native counterpart. The rAch showed so wide an antimicrobial spectrum that 0.1 mg/ml rAch inhibited the growth of Pseudomonas fluorescens , Staphylococcus epidermidis , and Streptococcus faecalis in addition to E. coli and S. aureus , whereas it did not appreciably affect the growth of Proteus mirabilis , Bacillus cereus and Micrococcus luteus . The rAch was also effective in preventing growth of Vibrio anguillarum and Vibrio parahaemolyticus . The results suggested that the rAch had great potential of using as an antimicrobial agent.