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Immunopeptidomics: Isolation of Mouse and Human MHC Class I- and II-Associated Peptides for Mass Spectrometry Analysis
Published on: October 15, 2021
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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
Summary
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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