Functional improvement of antibody fragments using a novel phage coat protein III fusion system

TY - JOUR

T1 - Functional improvement of antibody fragments using a novel phage coat protein III fusion system

AU - Jensen, Kim Bak

AU - Larsen, Martin

AU - Pedersen, Jesper Søndergaard

AU - Christensen, Peter Astrup

AU - Alvarez-Vallina, Luis

AU - Goletz, Steffen

AU - Clark, Brian F C

AU - Kristensen, Peter

PY - 2002/11/8

Y1 - 2002/11/8

N2 - Functional expressions of proteins often depend on the presence of host specific factors. Frequently recombinant expression strategies of proteins in foreign hosts, such as bacteria, have been associated with poor yields or significant loss of functionality. Improvements in the performance of heterologous expression systems will benefit present-day quests in structural and functional genomics where high amounts of active protein are required. One example, which has been the subject of considerable interest, is recombinant antibodies or fragments thereof as expressions of these in bacteria constitute an easy and inexpensive method compared to hybridoma cultures. Such approaches have, however, often suffered from low yields and poor functionality. A general method is described here which enables expressions of functional antibody fragments when fused to the amino-terminal domain(s) of the filamentous phage coat protein III. Furthermore, it will be shown that the observed effect is neither due to improved stability nor increased avidity.

AB - Functional expressions of proteins often depend on the presence of host specific factors. Frequently recombinant expression strategies of proteins in foreign hosts, such as bacteria, have been associated with poor yields or significant loss of functionality. Improvements in the performance of heterologous expression systems will benefit present-day quests in structural and functional genomics where high amounts of active protein are required. One example, which has been the subject of considerable interest, is recombinant antibodies or fragments thereof as expressions of these in bacteria constitute an easy and inexpensive method compared to hybridoma cultures. Such approaches have, however, often suffered from low yields and poor functionality. A general method is described here which enables expressions of functional antibody fragments when fused to the amino-terminal domain(s) of the filamentous phage coat protein III. Furthermore, it will be shown that the observed effect is neither due to improved stability nor increased avidity.

KW - Base Sequence

KW - Capsid Proteins/chemistry

KW - Chromatography, Gel

KW - DNA Primers

KW - Enzyme-Linked Immunosorbent Assay

KW - Immunoglobulin Fragments/immunology

KW - Inovirus/immunology

KW - Recombinant Fusion Proteins/chemistry

M3 - Journal article

C2 - 12408989

SN - 1522-4724

VL - 298

SP - 566

EP - 573

JO - Molecular Cell Biology Research Communications

JF - Molecular Cell Biology Research Communications

IS - 4

ER -