Identification and characterization of a laminin-binding protein of Aspergillus fumigatus: extracellular thaumatin domain protein (AfCalAp), by S. K. Upadhyay, L. Mahajan, S. Ramjee, Y. Singh, S. F. Basir and T. Madan
Journal of Medical Microbiology vol. 58, part 6, pp. 714 - 722
Supplementary Fig. S1
AfCalAp aligned with previously characterized thaumatin domain proteins. (a) Alignment with PR-5d, antifungal protein from Nicotiana tobacum, and (b) alignment with thaumatin A, sweet tasting protein from Thaumatococcus danielii. Residues crucial for antifungal activity have been highlighted in green, whereas those described as being important for sweet taste are highlighted in pink. Yellow highlighting indicates the position of the signal peptide in AfCalAp. Stretches of amino acids shown in orange indicate the position of the thaumatin consensus sequence in AfCalAp as determined using InterProScan. [PDF file] (33 KB)
Supplementary Fig. S2
Expression of AfCalA and Actin is not modulated in swollen conidia, by the presence of A549-derived extracellular matrix. Lane 1, 100 bp DNA ladder (New England Biolabs); lanes 2 and 3, RT-PCR of AfCalA using RNA isolated from 1 h swollen conidia in the presence and absence of A549-derived ECM, respectively; lanes 4 and 5, RT-PCR of Actin using RNA isolated from 1 h swollen conidia in the presence and absence of A549-derived ECM, respectively. [PDF file] (37 KB)
