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Short peptide sequence identity between human viruses and HLA-B27-binding human 'self' peptides

Shipeng Sun1, Tao Wang, Bo Pang

  • 1Clinical Laboratories, Guang'anmen Hospital, China Academy of Chinese Medical Sciences, No. 5 Bei Xian Ge St., Xi Cheng District, Beijing, 100053, People's Republic of China, shipengsun@gmail.com.

Theory in Biosciences = Theorie in Den Biowissenschaften
|December 24, 2013
PubMed

Insights

Certain viruses may trigger ankylosing spondylitis (AS) by mimicking human peptides recognized by HLA-B27. This molecular mimicry could explain the autoimmune disease

Area of Science:

  • Immunology
  • Virology
  • Genetics

Background:

  • Ankylosing spondylitis (AS) pathogenesis is hypothesized to involve molecular mimicry and arthritogenic peptides.
  • The human leukocyte antigen (HLA)-B27 gene is strongly associated with AS, suggesting its critical role.

Purpose of the Study:

  • To investigate if human viruses possess peptide sequences that mimic HLA-B27-binding self-peptides.
  • To explore the potential role of viral mimicry in the development of HLA-B27-positive ankylosing spondylitis.

Main Methods:

  • Bioinformatic analysis using BLASTP.
  • Comparison of human virus proteomes with HLA-B27-binding self-peptides, including arthritogenic sequences.

Main Results:

  • Identification of highly similar peptide sequences between certain chronic infection-causing viruses and HLA-B27-binding peptides.
  • Specific similarity noted in peptides derived from cartilage and bone proteins.

Conclusions:

  • Shared short amino acid sequences between human viruses and HLA-B27 peptides may contribute to AS pathogenesis.
  • Molecular mimicry by viral peptides is a plausible mechanism in HLA-B27-associated ankylosing spondylitis.

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