Abstract

For many years, the potential of immunoglobulin M (IgM) antibodies was not fully understood because of characteristics different to the well-known immunoglobulin G type like low target affinity, cross reactivity and complex protein structure. In the meanwhile IgMs have been positively evaluated for their use as therapeutic agent in the mucosal environment but also in serum to eradicate upcoming tumor cells and invading antigens. Therefore IgM class of antibodies will play a significant role in clinical applications but also diagnosis in the future. To evaluate the full potential of this kind of antibody molecules large amounts of high quality product will be needed. In this review the focus is set on the biotechnological aspect of producing IgM class antibodies recombinantly in mammalian cells. Current achievements in expression and purification of this molecule are highlighted and compared.

Highlights

  • The immunoglobulin M (IgM) class of antibodies is known to be the first defense against various antigens

  • In consistence with the literature we found different oligomerization states of individual IgM molecules that have been expressed in the same host cell line with the same expression constructs

  • After reviewing the available literature it is clear that the improvements gained with immunoglobulin G (IgG) type molecules have not been achieved with IgMs so far

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Summary

INTRODUCTION

The immunoglobulin M (IgM) class of antibodies is known to be the first defense against various antigens. IgMs are produced by the immune system and play an important role in primary and adaptive humoral immune responses [1] This class of antibodies tends to be less specific but recognizes a large variety of pathogenic antigens and has been proposed to be highly active in cytotoxic and cytolytic reactions due to superior activation of the complement system [2,3]. Despite the therapeutic benefits of IgM antibodies a major technological drawback has been identified in comparison to the classical IgG molecule. Recombinant production of this immunoglobulin class is not straight forward and has not been routinely accomplished so far. We will highlight current achievements and shortcomings of recombinant expression in the mammalian cell system as well as purification of such molecules and discuss our findings with available literature

THE STRUCTURE OF IgM
Antibody Productivity
Product Quality and Biological Function
PURIFICATION OF IgMs
Findings
CONCLUDING REMARKS

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