Table 1.
List of the protein domain families/superfamilies that are populated predominantly with allergenic molecules.
Total number of allergenic molecules (retrieved form Allergome database) in these families/superfamily and their ‘close homologs’ in eukaryotic metazoan parasites are shown.
Fig 1.
Flowchart depicting the workflow involved in the present analysis.
Fig 2.
The distribution of protein molecule entries (dark gray bars) listed in the Allergome database across different species (light gray bars) by taxonomic grouping (Bacteria, Fungi, Plants and Metazoan).
Fig 3.
Distribution of allergenic molecules retrieved from Allergome database across Pfam domain families.
Number of Pfam domain families with no allergenic members have also been represented. The Y-axis is scaled logarithmically (base 10), however true values are represented.
Fig 4.
Pfam domain families that are highly populated with allergenic protein sequences.
Protein domain families considered for this analysis are highlighted in the box based on the families presented in the article co-authored by Fitzsimmons and Dunne [21].
Table 2.
Categorization of 10 protein domain families into groups.
Fig 5.
A. Sequence alignment of the epitopic region from Atlantic salmon (Salmo salar) allergenic parvalbumin-like 1 protein (UniProt accession: B5DH17) and predicted epitopic-like region from worm Schistosoma japonicum (UniProt accession: Q5C262). B. Superposition of the 3D structural model of salmon parvalbumin-like 1 protein (colored in green) and EF hand domain of the Schistosoma japonicum protein (in cyan). Epitope (allergen) and predicted epitopic-like regions (parasite protein) are depicted in the box.
Fig 6.
A. Sequence alignment of the epitopic region from profilin protein (allergenic) from Betula pendula (European white birch) (UniProt accession: P25816) and predicted epitopic-like region from the worm Ascaris lumbricoides (UniProt accession: F1LGV9). B. Superposition of the 3D structure of plant allergenic protein (PDB accession: 1CQA) (colored in green) and the 3D structural model of profilin protein from the worm Ascaris lumbricoides (in cyan). Epitope (allergen) and predicted epitopic-like regions (parasite protein) are depicted in the box.
Fig 7.
A. Superposition of the 3D structure of timothy grass Phl p 1 (PDB accession: 1N10) (in green) and the 3D structural model of mite protein (in cyan). Epitope (allergen) and predicted epitopic-like regions (parasite protein) are depicted in the box. B. Sequence alignment of the epitopic region from Phleum pratense ‘Phl p 1’, a major timothy grass pollen allergen (UniProt accession: P43213) and predicted epitopic-like region from Mite group 2 allergen ‘Pso o 2’ protein (UniProt accession: Q965E2) from Psoroptes ovis.
Fig 8.
Magnitudes of specific IgE, IgG4 and IgG1 responses to S. mansoni Bet v 1-like protein, SmBv1L, in a population of 222 individuals infected with S. mansoni, dotted lines indicate threshold of magnitude for a response.
Data were normalized for expression on a log scale by the addition of constants so as to include zero values.
Fig 9.
Venn diagram showing the distribution of Ab isotype responses to SmBv1L within IgG1, IgG4 and IgE responders in a population of 222 individuals endemically infected with S. mansoni.