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

Fig 4

Acinetobacter OmpA is the ligand to Candida Hyr1p.

Acinetobacter biotin-labeled cell wall proteins that bound to C. albicans wild-type, hyr1/hyr1, hyr1/hyr1+HYR1, or als3/als3 hyphae were separated on SDS-PAGE, probed with anti-biotin antibody, and the hybridized bands were identified by Mass spectrometry. C. albicans wild-type or hyr1/hyr1+HYR1 complemented hyphae bound a major band at 38 kDa which was identified as OmpA by MS/MS analysis (A). In contrast, the hyr1/hyr1 mutant had severe reduction in its ability to bind OmpA. C. albicans Als3p was not found to be a receptor as proteins equally bound to als3/als3 mutant strain (A). To confirm the identity of the 38 kDa band, blots were probed with an anti-OmpA antibody, which confirmed that the 38 kDa proteins were indeed OmpA (B).

Fig 4

doi: https://doi.org/10.1371/journal.ppat.1007056.g004