Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Recombinant human IgA expressed in insect cells

L Carayannopoulos1, E E Max, J D Capra

  • 1Program in Molecular Biophysics, University of Texas, Southwestern Medical Center, Dallas 75235-9048.

Proceedings of the National Academy of Sciences of the United States of America
|August 30, 1994
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

One from column A, one from column B.

Immunology today·2014
Same author

The cross-reactive idiotype of A-strain mice Serological and structural analyses.

Immunology today·2014
Same author

Are anti-arsonate antibody N-segments selected at both the protein and the DNA level?

Immunology today·2014
Same author

Professor emeritus Jacob B. Natvig, one of the founders of Scandinavian journal of immunology, turns 75.

Scandinavian journal of immunology·2009
Same author

The coding properties of methyl-deficient leucyl-transfer RNA.

Journal of molecular biology·2009
Same author

CD45RO: a marker for BCR-mediated selection.

Scandinavian journal of immunology·2007

Researchers created recombinant human Immunoglobulin A (IgA) in insect cells to study its functions. They found that glycosylation of the IgA constant region (C alpha) is essential for binding to the IgA Fc receptor.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • Immunoglobulin A (IgA) is crucial for mucosal immunity.
  • Understanding IgA's interactions with immune molecules is vital.

Purpose of the Study:

  • To map interaction sites between immune effectors and the IgA constant region (C alpha).
  • To develop a system for studying IgA structure-function relationships.

Main Methods:

  • Expression of soluble, chimeric human IgA in insect cells using recombinant baculoviruses.
  • Construction of viruses encoding altered IgA heavy chains.
  • Assessment of recombinant IgA authenticity via antigen-binding, antibody recognition, complement fixation, and Fc receptor binding.

Main Results:

Related Experiment Videos

  • Recombinant IgA was correctly assembled, N-glycosylated, and secreted as heterodimers and dimers (with J chain).
  • The recombinant IgA demonstrated authentic functional properties.
  • Glycosylation of the second C alpha domain was necessary for monocyte IgA Fc receptor interaction.

Conclusions:

  • A functional system for producing recombinant human IgA in insect cells was established.
  • This system facilitates the study of IgA structure-function relationships.
  • Specific glycosylation of the C alpha domain is critical for IgA-Fc receptor binding.