Bacterial Surface Display using Outer Membrane Proteins as Anchoring Sites

نویسندگان

  • Sharadwata Pan
  • Michael K. Danquah
چکیده

Surface display of heterologous proteins or polypeptides on the surface of bacteria has gained momentum in recent years. Until recently, arrays of anchors or carriers have been identified for displaying diverse passenger proteins on the surface of Escherichia coli, majority of these involving the outer membrane proteins (OMPs). The reason for opting outer membrane proteins lies mainly i n its ability to withstand the incorporation of large libraries of novel polypeptides, without a significant loss in steadiness. In this context, a thorough understanding of the underlying genetic mechanism of the OMP-mediated surface display is necessary. In this mini-review, we attempt to do the same and also compare the OMPs from two commonly used and available bacteria. The far reaching consequence of this lies in efficient surface display of imaginative and innovative polypeptides with applications ranging from bioremediation, immunology to vaccine development.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Microbial Cell Surface Display: Its Medical and Environmental Applications

Cell-surface display is the expression of peptides and proteins on the surface of living cells by fusing them tofunctional components of cells which are exposed to the environment of cells. This strategy can be carriedout using different surface proteins of cells as anchoring motifs and different proteins from different sourcesas a passenger protein. It is a promising strategy...

متن کامل

An engineered autotransporter-based surface expression vector enables efficient display of Affibody molecules on OmpT-negative E. coli as well as protease-mediated secretion in OmpT-positive strains

BACKGROUND Cell display technologies (e.g. bacterial display) are attractive in directed evolution as they provide the option to use flow-cytometric cell sorting for selection from combinatorial libraries. The aim of this study was to engineer and investigate an expression vector system with dual functionalities: i) recombinant display of Affibody libraries on Escherichia coli for directed evol...

متن کامل

Surface display of recombinant proteins on Escherichia coli by BclA exosporium of Bacillus anthracis

BACKGROUND The anchoring motif is one of the most important aspects of cell surface display as well as efficient and stable display of target proteins. Thus, there is currently a need for the identification and isolation of novel anchoring motifs. RESULTS A system for the display of recombinant proteins on the surface of Escherichia coli was developed using the Bacillus anthracis exosporal pr...

متن کامل

Structural determinants of the eosinophil cationic protein antimicrobial activity.

Antimicrobial RNases are small cationic proteins belonging to the vertebrate RNase A superfamily and endowed with a wide range of antipathogen activities. Vertebrate RNases, while sharing the active site architecture, are found to display a variety of noncatalytical biological properties, providing an excellent example of multitask proteins. The antibacterial activity of distant related RNases ...

متن کامل

Cloning, protein expression and display of synthetic multi-epitope mycobacterial antigens on Salmonella typhi Ty21a cell surface.

Expressing proteins of interest as fusion to proteins of bacterial envelope is a powerful technique for biotechnological and medical applications. The synthetic gene (VacII) encoding for T-cell epitopes of selected genes of Mycobacterium tuberculosis namely, ESAT6, MTP40, 38 kDa, and MPT64 was fused with N- terminus of Pseudomonas syringae ice nucleation protein (INP) outer membrane protein. Th...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2012