Cloning and expression of recombinant adhesive protein mefp-2 of the blue mussel, mytilus edulis

a technology of blue mussels and recombinant proteins, applied in the field of cloning and expression of recombinant adhesive proteins of blue mussels, mytilus edulis, can solve the problems of many mussels sacrificed, no conventional glues that can be applied in aqueous environment, no commercial product incorporates any of the other proteins known to be involved in underwater adhesion

Inactive Publication Date: 2006-02-09
THE UNITED STATES AS REPRESENTED BY THE DEPARTMENT OF ENERGY
View PDF3 Cites 3 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

There are no conventional glues that can be applied in an aqueous environment and are impervious to water and turbulent forces.
However, no commercial product incorporates any of the other proteins known to be involved in underwater adhesion by the M. edulis mussel.
Thus, subsequent purification and microscopic analysis require(d) the sacrifice of many mussels.
This is neither environmentally friendly nor economically practical.
In spite of the extensive research in this area, and relative success in patenting and commercializing aspects of these adhesive proteins, a complete understanding of how the byssus is assembled from its component proteins, and the role each protein plays in successful assembly and attachment has not been achieved.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Cloning and expression of recombinant adhesive protein mefp-2 of the blue mussel, mytilus edulis

Examples

Experimental program
Comparison scheme
Effect test

Embodiment Construction

[0025] In practicing the present invention several conventional techniques in microbiology and molecular biology (recombinant DNA) are used. Such techniques are well known and are explained in, for example, Sambrook, 1999, Molecular Cloning: A Laboratory Manual, Second Edition, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.; DNA Cloning: A practical Approach, 1985 (D. N. Glover ed); Current Protocols in Molecular Biology, John Wiley & Sons, Inc. (1994) and all more recent editions of these publications.

Definitions

[0026] Before proceeding further with a description of the specific embodiments of the present invention, a number of terms will be defined.

[0027] As used herein, a compound or molecule is an organic or inorganic assembly of atoms of any size, and can include macromolecules, peptides, polypeptides, whole proteins, and polynucleotides.

[0028] As used herein, a polynucleotide is a nucleic acid of more than one nucleotide. A polynucleotide can be made up of ...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

PUM

PropertyMeasurementUnit
diameteraaaaaaaaaa
diameteraaaaaaaaaa
diameteraaaaaaaaaa
Login to view more

Abstract

The present invention includes a Mytilus edulis cDNA having a nucleotide sequence that encodes for the Mytilus edulis foot protein-2 (Mefp-2), an example of a mollusk foot protein. Mefp-2 is an integral component of the blue mussels' adhesive protein complex, which allows the mussel to attach to objects underwater. The isolation, purification and sequencing of the Mefp-2 gene will allow researchers to produce Mefp-2 protein using genetic engineering techniques. The discovery of Mefp-2 gene sequences will also allow scientists to better understand how the blue mussel creates its waterproof adhesive protein complex.

Description

CROSS REFERENCED APPLICATIONS [0001] This patent application was filed by Applicants on the same day as another patent application filed by Applicants entitled “CLONING AND EXPRESSION OF RECOMBINANT ADHESIVE PROTEIN MEFP-10F THE BLUE MUSSEL, MYTILUS EDULIS”, having Serial No. ______.U.S. GOVERNMENT RIGHTS [0002] The United States Government may have rights in this invention pursuant to Contract No. DE-AC07-99ID13727 between the U.S. Department of Energy and Bechtel BWXT Idaho, LLC, representing the Idaho National Engineering & Environmental Laboratory (INEEL).TECHNICAL FIELD [0003] The invention relates to isolated or purified nucleic acid molecules encoding an adhesive protein, for example, Mefp-2 of the blue mussel, Mytilus edulis. Adhesives that can be derived from the present invention can be used in a variety of fields including but not limited to: military applications, construction products, plastics, electronics, automobile and aviation products as well as several biomedical...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to view more

Application Information

Patent Timeline
no application Login to view more
Patent Type & Authority Applications(United States)
IPC IPC(8): C07K14/435C07H21/04C12P21/06C12N5/06
CPCC07K14/43504C07H21/04
Inventor SILVERMAN, HEATHERROBERTO, FRANCISCO
Owner THE UNITED STATES AS REPRESENTED BY THE DEPARTMENT OF ENERGY
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Try Eureka
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap