Fig. 7: Partial amino acid alignments of the DM-associated TRIM proteins that share amino acid similarity with viral species. | Communications Biology

Fig. 7: Partial amino acid alignments of the DM-associated TRIM proteins that share amino acid similarity with viral species.

From: Analysis of human total antibody repertoires in TIF1γ autoantibody positive dermatomyositis

Fig. 7

Alignment of all identified TRIM proteins in DM (Fig. 5a); TRIM3 is located on the bottom of the alignments plots. Above TRIM3 (sp|O75382) are TRIM33 (sp|Q9UPN9) and TRIM47 (sp|Q96LD4); cross-marked. Conservation level is presented as a colour gradient (high; red, low; blue). a Partial alignment of the region where the TRIM3-Variola high similarity epitopes were identified. The TRIM3 protein sequence is presented next to the alignment plot. Yellow: the two TRIM3 epitopes with high amino acid (AA) similarity to Variola and poxviruses (Fig. 6). Black font: identical AAs between TRIM3 and Variola virus. Red font; different AAs between TRIM3 and Variola virus. Both epitopes are located only 6 AAs apart (relative to TRIM3 protein sequence). TRIM3 presents high similarity with TRIM33 in respect to the specific AA epitopes. b Partial alignment of the region where the TRIM47-HIV-syn9 high similarity epitope was identified. The TRIM47 protein sequence is presented next to the alignment plot. Yellow: the TRIM47 epitopes with high AA similarity to HIV and syn9 phage (Supplementary Fig. 7d). Black font: identical AAs amongst TRIM47 and the two viruses. Red font; different AAs amongst TRIM47 and the two viruses. The epitope is poorly conserved amongst the DM-specific TRIM proteins.

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