RT Journal Article SR Electronic(1) A1 Herrero, Enrique A1 Sanz, Pascual A1 Sentandreu, RafaelYR 1987 T1 Cell Wall Proteins Liberated by Zymolyase from Several Ascomycetous and Imperfect Yeasts JF Microbiology, VO 133 IS 10 SP 2895 OP 2903 DO https://doi.org/10.1099/00221287-133-10-2895 PB Microbiology Society, SN 1465-2080, AB SUMMARY: Eight yeast species (the ascomycetes Saccharomyces cerevisiae, Zygosaccharomyces rouxii, Hansenula wingei, Saccharomycopsis lipolytica, Schizosaccharomyces pombe and Pichia scolyti, and the imperfect yeasts Candida albicans and Rhodotorula glutinis) have been compared with respect to the proteins solubilized by glucanase treatment of amino-acid-labelled, purified walls. Except for R. glutinis, a significant quantity of radioactively labelled protein material was liberated by this treatment. Among the major protein components solubilized was a material larger than 100 kDa (heterogeneous in size in some species) and a molecule ranging in size from 31.5 to 34 kDa depending on the yeast species. The large material was of glycoprotein nature, with the sugar portion N-glycosidically linked to the protein moiety; in some species, this material did not bind concanavalin A (ConA), indicating the presence of terminal sugar residues different from mannose, glucose or glucosamine. The form of 31.5-34 kDa was present in all the species studied except R. glutinis; it was a mannoprotein, except in Schiz. pombe, which possessed a 31.5 kDa form not sensitive to tunicamycin or endoglycosidase H and not recognized by ConA. Antigenic cross-reactivity was observed between the protein moieties of the 33 kDa form of Sacch. cerevisiae and the species of equivalent size in C. albicans and H. wingei. Similar partial proteolysis patterns were obtained for the 33 kDa form of Sacch. cerevisiae and the 34 kDa forms of C. albicans and P. scolyti., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-133-10-2895