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A natural tapasin isoform lacking exon 3 modifies peptide loading complex function.

Nele Beutler1, Sebastian Hauka, Alexandra Niepel

  • 1Institute for Virology, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.

European Journal of Immunology
|March 23, 2013
PubMed
Summary
This summary is machine-generated.

An alternatively spliced tapasin (tpn) variant lacking exon 3 impairs MHC-I loading and alters peptide ligandome, potentially impacting CD8(+) T-cell responses. This variant affects MHC-I surface expression and interacts with TAP, modifying the peptide loading complex.

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Area of Science:

  • Immunology
  • Molecular Biology
  • Virology

Background:

  • Efficient MHC class I (MHC-I) peptide loading is crucial for adaptive immunity.
  • The peptide loading complex (PLC), including tapasin (tpn), ERp57, and TAP, facilitates MHC-I peptide binding.
  • Human cytomegalovirus (HCMV) infection can alter host cell protein expression.

Purpose of the Study:

  • To characterize an alternatively spliced tapasin (tpn) transcript lacking exon 3 (ΔExon3) found during HCMV infection.
  • To investigate the functional consequences of the ΔExon3 tpn variant on MHC-I assembly, peptide loading, and T-cell recognition.

Main Methods:

  • Analysis of alternatively spliced tpn transcripts using molecular techniques.
  • Assessment of MHC-I surface expression and peptide loading in cells expressing wild-type and ΔExon3 tpn.
  • Co-immunoprecipitation assays to study protein interactions within the PLC.
  • Mass spectrometry-based analysis of the MHC-I ligandome.

Main Results:

  • The ΔExon3 tpn variant lacks Cys-95, impairing its disulfide bond formation with ERp57.
  • In tpn-deficient cells, ΔExon3 tpn stabilized TAP but not MHC-I.
  • In tpn-proficient cells, ΔExon3 tpn reduced cell surface expression of tpn-dependent HLA-B*44:02 but not tpn-independent HLA-B*44:05.
  • ΔExon3 tpn bound simultaneously with wild-type tpn to TAP, altering PLC function and the MHC-I ligandome.

Conclusions:

  • Alternative splicing of tpn generates a variant (ΔExon3) that modulates MHC-I peptide loading and cell surface expression.
  • The ΔExon3 tpn variant can alter the MHC-I ligandome, potentially impacting CD8(+) T-cell responses during viral infections.
  • Heterogeneous nuclear ribonucleoprotein (hnRNP) family members may regulate the expression of this alternatively spliced tpn variant.