Bioinformatics analysis of myelin-microbe interactions suggests multiple types of molecular mimicry in the pathogenesis of multiple sclerosis

Fig 1. Study pipeline overview.

Fig 2. The current PDB structures related to a portion of the MBP sequence.

Fig 3. Alignment of BSH amino acid sequence from the bacteria and associated enzymes that participate in the butyric acid metabolic pathway. The active site’s amino acids are highlighted in red, based on the structure of the BSH from C. perfringens.

Fig 4. The complex metabolic pathway involved in the production of polysaccharide A, a molecule with potential neuroprotective effects.

Fig 5. a) Amino acid sequence alignment of MBP with the HPV-B19 viral capsid protein. The first line displays the viral capsid amino acid sequence, the second line displays the MBP amino acid sequence, and the third line displays the scores associated with the amino acid alignment between the two sequences. In the amino acid alignment, the colors blue and red represent the gap and identity mode, respectively. Stars represent identity between all aligned amino acids. b) Position-specific scoring matrix for amino acid sequence alignment between HPV-B19 viral capsid protein and MBP protein.

Fig 6. a) Alignment of AAV-4 viral capsid protein with MBP amino acids sequence. The first line contains the amino acid sequence of the viral capsid coat, while the second line contains the amino acid sequence of the MBP. The third line depicts the consistency of each amino acid alignment from 0 to 10 (star). The similarity and identity of two amino acids are represented by points, with 0 representing the gap mode and a star indicating identity between all aligned amino acids. b) Scoring matrix for aligning amino acid sequences of AAV-4 viral capsid protein and MBP protein.

Fig 7. a) Alignment of tertiary structure between HPV-B19 capsid protein and MBP. b) Alignment of tertiary structure between AAV-4 capsid protein and MBP.

Fig 8. a) The 3D structure of the HPV-B19 capsid protein with red regions indicating the alignment of amino acids with a score greater than 8 b) The 3D structure of the AAV-4 capsid protein with blue regions indicating the alignment of amino acids with a score greater than 8 c) The alignment of both viral capsid proteins, with overlapping blue and red regions indicating amino acid alignment scores greater than 8. d) The overlapping regions of autoimmune encephalitis-associated amino acids in the HPV-B19 and AAV-4 viral capsid protein structures (GLY82, SER78, THR373, GLY374, SER377, GLN378, GLN379).

Fig 9. a) Multiple alignments of MAP_0106, EBNA1, and MBP proteins. b) Multiple alignments of MAP_4027، BOLF1, and IRF5 proteins.

Fig 10. The multiple alignment results based on the two categories presented in Table 7. a) shows the multiple alignment results of the first group of BLAST protein sequences (EBNA1, MAP 0106, MBP) b) shows the multiple alignment results of the second group of BLAST protein sequences (BOLF1, IRF5, MAP4027).

Fig 11. Diagram of the sequences of epitope antigens obtained from Table 7.

Fig 12. Alignment of epsilon toxin of Clostridium perfringens and ORF3 protein of Nora virus.