Expression and purification of a new lectin from mussel Mytilus trossulus

The gene of mtl from the mussel Mytilus trossulus was cloned into pET-40b(+) expression vector. After expression in E. coli using designed MX-medium an instable soluble form of MTL was obtained. The developed isolation method of the recombinant protein in “semi-denatured” conditions allowed obtainin...

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Bibliographic Details
Published in:Protein expression and purification 2019-02, Vol.154, p.62-65
Main Authors: Golotin, V.A., Filshtein, A.P., Chikalovets, I.V., Yu, Kim N., Molchanova, V.I., Chernikov, O.V.
Format: Article
Language:English
Subjects:
Animals
Escherichia coli - chemistry
Escherichia coli - genetics
Gene Expression
Lectins - biosynthesis
Lectins - chemistry
Lectins - genetics
Lectins - isolation & purification
Mytilus - chemistry
Mytilus - genetics
Rabbits
Recombinant Proteins - biosynthesis
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
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Summary:The gene of mtl from the mussel Mytilus trossulus was cloned into pET-40b(+) expression vector. After expression in E. coli using designed MX-medium an instable soluble form of MTL was obtained. The developed isolation method of the recombinant protein in “semi-denatured” conditions allowed obtaining an active soluble form of the homogenous lectin from the mussel M. trossulus (r-MTL). Both of the lectins had similar antigenic and spatial structures. •The recombinant analog of Mytilus trossulus lectin, a member of new lectin family was obtained in soluble and active form.•A method of isolation of the recombinant protein in “semi-denatured” conditions was developed.•It has been shown that native MTL and recombinant MTL have similar spatial structures and biological activity.
ISSN:1046-5928
1096-0279
DOI:10.1016/j.pep.2018.10.003