Table 1.
Possible mechanism for molecular mimicry and examples from pathogens.
Figure 1.
Scatter plot of the blast scores of all proteins from B. malayi (left) and S. mansoni (right) vs. the host H. sapiens (x-axis) and the control C. elegans (y-axis).
Points below the blue dotted line represent parasite proteins with better scores to H. sapiens than to C. elegans.
Figure 2.
ClustalW alignment of the candidate mimicry region in A8NPN8 from B. malayi to H. sapiens SOCS5.
The SH2 domain is shaded in yellow, the SOCS box domain in blue. The N-terminal parts of the two proteins do not share any similarity (not shown).
Table 2.
Organisms used in this study.
Figure 3.
The in silico pipeline for identification of molecular mimicry candidates from parasites.
See Methods for details. The process is illustrated with the actual numbers from the analysis of the P. falciparum proteome in blue, respectively a randomized version of it in grey, vs. the host H. sapiens.
Figure 4.
Numbers of identified candidate molecular mimicry 14-mers from parasite proteomes and randomized versions thereof (R).
Numbers of amino acid identities between the 14-mers and their best hit in the human proteome are color-coded as indicated.
Table 3.
Selected mimicry candidates.
Figure 5.
Alignment of human vitronectin (top) and P. falciparum PfEMP1 variants (bottom).
Identities to vitronectin are printed in bold black, similarities in black. The known vitronectin domains are the signal sequence (blue), somatomedin-B (green), and hemopexin (red). The known PfEMP1 domains are the N-terminal segment (dark blue), Duffy Binding Like α (light blue), cysteine-rich interdomain region α (yellow), Duffy Binding Like 2d (orange), cysteine-rich interdomain region ß (purple), transmembrane domain (cyan), acidic terminal segment (green).