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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

  • Jensen, Kim Bak
  • Martin Larsen
  • Jesper Søndergaard Pedersen
  • Peter Astrup Christensen
  • Luis Alvarez-Vallina
  • Steffen Goletz
  • Brian F C Clark
  • Peter Kristensen

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.

OriginalsprogEngelsk
TidsskriftMolecular Cell Biology Research Communications
Vol/bind298
Udgave nummer4
Sider (fra-til)566-73
Antal sider8
ISSN0006-291X
StatusUdgivet - 8 nov. 2002
Eksternt udgivetJa

ID: 200572782