Part:BBa_K4247020

Mfp151

This part codes for MFP151, a hybrid protein composed of mussel foot proteins 1 and 5. This is a composite part consisting of the following basic parts: BBa_K4247018 (mfp151_first-half) and BBa_K4247019 (mfp151_second-half).

This part is one of a collection of compatible mussel foot protein parts: BBa_K4247018 (mfp151_first-half), BBa_K4247019 (mfp151_second-half) and BBa_K4247021 (mfp151_snoopcacher).

Usage and Biology

Mussels have the ability to attach themselves to various surfaces underwater by permanent adhesion. This adhesion is facilitated by their byssus, which is secreted from their foot. The byssus comprises a bundle of threads and at the end of each thread, there is an adhesion plaque containing a water-resistant adhesive that enables the mussel to anchor itself to surfaces.

Several types of foot proteins have been characterised and each of them have a different function as per their location in the byssus. Of these, MFP3 and MFP5 are found in the distal end of the byssus. Post-translational modification of tyrosines yields L-3,4-dihydroxyphenylalanine (DOPA) and these DOPA groups are associated with the adhesion strength of MFPs. MFP3 and MFP5 are known to have the highest DOPA content among MFPs and hence, these intrinsically disordered proteins enable the adhesion mechanisms of the byssus. MFP1 forms the outer coating of the byssus and it has a lower DOPA content compared to MFP3 and MFP5.

Recombinant production of MFP5 wasn’t very successful and there were several bottlenecks in terms of cell growth and protein purification since the sticky nature of the protein makes it difficult to purify. In order to overcome these limitations, a hybrid protein called MFP151 was constructed and produced. This hybrid protein consists of six M. galloprovincialis MFP1 decapeptide repeats added to the N- and C-terminus of M. galloprovincialis MFP5. So, the protein consists of 6 MFP1 repeats followed by a MFP5 sequence and 6 MFP1 repeats again. MFP151 was found to have comparable adhesion characteristics to recombinant MFP5, could be produced with greater yields and could be purified easily.