Selection and characterisation of a phage-displayed human antibody (Fab) reactive to the lung resistance-related major vault protein
2002

Human Antibody Fragment Against Major Vault Protein

Sample size: 750 publication Evidence: moderate

Author Information

Author(s): Scheffer G L, Reurs A W, Jutten B, Beiboer S H W, van Amerongen R, Schoester M, Wiemer E A C, Hoogenboom H R, Scheper R J

Primary Institution: Free University Medical Center, Amsterdam, The Netherlands

Hypothesis

The study aims to isolate a human antibody fragment that reacts with the major vault protein, which is associated with multidrug resistance in tumor cells.

Conclusion

A human Fab fragment reactive to the major vault protein was successfully isolated and may serve as a valuable tool for studying its role in normal physiology and drug resistance.

Supporting Evidence

  • The isolated Fab fragment showed binding affinity comparable to that of murine monoclonal antibodies.
  • The study utilized a phage display method, which is a powerful tool for identifying human antibodies.
  • Immunohistochemical analysis confirmed the presence of the major vault protein in various tumor cell lines.
  • The selected Fab fragment may be used for functional knock-out studies of the major vault protein.

Takeaway

Researchers found a special human antibody that can stick to a protein involved in making cancer cells resistant to drugs, which could help in understanding and treating cancer better.

Methodology

The study used a large non-immunized human Fab fragment phage library to select and characterize a human antibody fragment that binds to the major vault protein.

Limitations

The study's findings may be limited by the selection process, which could have favored higher affinity phages and resulted in the loss of lower affinity ones.

Digital Object Identifier (DOI)

10.1038/sj.bjc.6600159

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