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The intracellular localization and oligomerization of chicken invariant chain with major histocompatibility complex

H Ye1, F Z Xu, W Y Yu

  • 1Anhui Agricultural University, Hefei, China 230036. yuweiyi@ahau.edu.cn

Poultry Science
|July 11, 2009
PubMed

Insights

Chicken invariant chain (Ii) binds to MHC class II (MHCII) to form complexes. Maintaining Ii's structure, even with CLIP alterations, allows MHCII polymer assembly, suggesting varied binding models.

Area of Science:

  • Immunology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Invariant chain (Ii) is crucial for MHC class II (MHCII) assembly and function.
  • The CLIP region of Ii occupies the MHCII peptide-binding groove, preventing premature antigen loading.

Purpose of the Study:

  • To investigate the intracellular localization and oligomerization of chicken Ii with single chicken MHCII subunits.
  • To determine the role of the CLIP sequence in the association between chicken Ii and MHCII.

Main Methods:

  • Utilized green or red fluorescent protein-fused Ii and MHCII subunits for detection.
  • Analyzed intracellular localization and oligomerization patterns.

Main Results:

  • Chicken Ii associates with single MHCII subunits and forms oligomers.
  • Deletion of the CLIP sequence in Ii disrupts its association with MHCII.
  • Replacing CLIP with the Newcastle disease virus F(343) epitope restores Ii-MHCII association.

Conclusions:

  • MHCII polymer assembly is maintained if the basic steric structure of Ii is preserved.
  • Different species or MHCII isotypes may exhibit distinct Ii-MHCII binding models.

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