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The Hyr1 protein from the fungus Candida albicans is a cross kingdom immunotherapeutic target for Acinetobacter bacterial infection

Fig 1

Striking 3 D structural homology between C. albicans Hyr1p and A. baumannii FhaB.

Ribbon diagram depicting the full scale model for C. albicans Hyr1 as computed by the iTasser server (A). The region of Hyr1 corresponding to homologous domains in the viral tailspike, BP FhaB and HI HMW1 proteins is indicated in blue. Note the striking similarity in 3D structure of Hyr1p and FhaBp (B). Hyr1 models showing the sequence and location of the eight peptides used as antigens in the study in red as van der Waals space-filling spheres (C). Note the similar location of peptide 5 on Fhab (B) and on Hyr1p (C) (red regions). Models for three putative cross-reactive A. baumannii targets (FhaBp, OmpA, BIg) are shown with domains homologous to peptide 5 in red (D). In addition, the A. baumannii BIg protein has many additional near matches (6 identical residues) which are shown on the full model as orange. Sequence alignments between C. albicans (CA) peptide 5 and putative cross-reactive A. baumannii (AB) targets with identical residues are depicted in boxes. Higher resolution views of identified domains showing identical and physicochemically conserved residues are visualized as space-filling spheres. Coloration is a modified RasMol schema (Gly, Ala—cream; Asn, Gln—light brown; Thr—orange; Val, Ile—green; Trp—olive green; Asp—red; His—sky blue; Pro—chartreuse).

Fig 1