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中国生物工程杂志

China Biotechnology
China Biotechnology
China Biotechnology  2020, Vol. 40 Issue (11): 82-89    DOI: 10.13523/j.cb.2007046
    
Advances and Applications of Recombinant Mussel Foot Proteins
XUE Rui,YAO Lin,WANG Rui,LUO Zheng-shan,XU Hong,LI Sha()
State Key Laboratory of Materials-Oriented Chemical Engineering, College of Food Science and Light Industry, Nanjing Tech University, Nanjing 211800, China
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Abstract  

Mussel foot proteins are a kind of protein complex secreted by mussel foot gland, which have strong adhesion to the surface of substrates due to reactions. Because of its strong adhesion, biodegradability and excellent biocompatibility in the marine environments, it is often used as bio-medical adhesives. However, the extraction of natural proteins is limited by the source of raw materials, and the complex process leads to high price, which hinders the further application and development of mussel foot proteins. The latest development of microbial synthesis provides a new way of thinking for mussel foot protein production and has the significance of expanding the scale of production. The production methods of mussel foot protein by genetic engineering were reviewed, and the applications of recombinant proteins in adhesion antifouling coatings and tissue engineering materials were summarized. At the same time, the research direction is prospected, and it is pointed out that the key technology for the further development of recombinant mussel foot proteins is to analyze the structure activity and hierarchical structure of the protein, on the basis of which the expression level of the protein is improved, so as to obtain more derivatives with biological efficacy.

Key words： Mussel proteins      Recombinant expression      Biological adhesives     
Received: 26 July 2020      Published: 11 December 2020
ZTFLH:  Q78  
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Corresponding Authors: Sha LI     E-mail: lisha@njtech.edu.cn
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Rui XUE
Lin YAO
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Sha LI
Cite this article:

XUE Rui,YAO Lin,WANG Rui,LUO Zheng-shan,XU Hong,LI Sha. Advances and Applications of Recombinant Mussel Foot Proteins. China Biotechnology, 2020, 40(11): 82-89.

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https://manu60.magtech.com.cn/biotech/10.13523/j.cb.2007046     OR     https://manu60.magtech.com.cn/biotech/Y2020/V40/I11/82

Fig.1 Distribution of different mussel proteins in the byssus
Protein type Molecular weight(kDa) Isoelectric point(pI) DOPA(mol%) Distribution
Mfp-1 ≈110 10.5 10-15 The cuticle layer of the byssus
Mfp-2 42-47 9-10 2-3 Plaque foam
Mfp-3 5-7 >10.5 20-25 Primer layer
Mfp-4 93 9 2 Thread collagen anchor
Mfp-5 9.5 9.5 25-30 Primer layer
Mfp-6 11.6 9.5 <5 Primer layer
Table 1 Comparisons of properties of different types of mussel foot proteins
Host Origin Protein
type		 Expressed fragment Molecular
weight
(kDa)		 Expression Reference
Escherichia
coli		 Mytilus
edulis		 Mefp-1 6 decapeptide repeats 7 Inclusion body [8]
7 decapeptide repeats; fused with OmpA signal peptide at N-terminus 8 The soluble expression was twice higher than without OmpA [18]
Mytilus
galloprovinciali		 Mgfp-5 Full-length 13.5 ≈ 40% of total cell proteins; mainly soluble [16]
Mgfp-3A Full-length 7 ≈56% of total cell proteins; half soluble [17]
In vivo DOPA incorporation by TyrRS 7 — [23]
fp-151 6 Mfp-1 decapeptide repeats at each Mfp-5 terminus 24.5 ≈40% of total cell proteins; inclusion body [20]
Co-expression with tyrosinase 24.5 Mainly soluble [22]
fp-353 Mfp-3A at each Mfp-5 terminus 22 ≈21% of total cell proteins; inclusion body [21]
Mytilus
coruscus		 Mcofp-1 12 decapeptide repeats 40.5 Soluble [11]
Mcofp-3 Full-length 9.18 Inclusion body [12]
Perna viridis Pvfp-1
(R-240)		 8 decapeptide repeats 26.78 Soluble [13]
Pvfp-1
(C-237)		 C-terminus non repetitive area 25.58 Soluble [13]
Yeast Mytilus
californianus		 Mcfp-3 Fused with first 9 amino acids of HA0 at N-terminus 7 Soluble [26]
Insect Sf9
cells		 Mytilus
galloprovinciali		 fp-151 6 Mfp-1 decapeptide repeats at each Mfp-5 terminus 24.5 ≈50% of total cell proteins; soluble [27]
Chicory Mytilus
galloprovinciali		 Mgfp-5 Full-length — The expression rate in T1 generation was 58.70% [29]
Table 2 Advances in the production of mussel foot proteins by genetic engineering
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