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Ubiquitin is a highly conserved protein required for various fundamental cellular processes in eukaryotes. Herein, we first report the contribution of the ubiquitin fusion protein Ubi1 (a ubiquitin monomer fused with the ribosome protein L40e, Rpl40e) in the growth and pathogenicity of  Cryptococcus neoformans .  UBI1  deletion resulted in severe growth restriction of  C. neoformans , whose growth rate was positively correlated with  UBI1  expression level. The growth defect of the  ubi1 Δ strain could be closely associated with its morphological abnormalities, such as its reduced ribosome particles. In addition, the  ubi1 Δ mutant also displayed increased cell ploidy, cell cycle arrest, and decreased intracellular survival inside macrophages. All these phenotypes were reversed by the reconstitution of the full-length  UBI1  gene or  RPL40a  domain. Mouse survival and fungal burden assays further revealed a severely attenuated pathogenicity for the  ubi1 Δ mutant, which is probably associated with its reduced stress tolerance and the induction of T-helper 1-type immune response. Taken together, Ubi1 is required for maintaining the vegetative growth, morphological homeostasis, cell cycle progression, and pathogenicity  in vivo  of  C. neoformans . The pleiotropic roles of Ubi1 are dependent on the presence of Rpl40e and associated with its regulation of cryptococcal ribosome biogenesis.

frontiers in microbiology

Ribosomal Protein L40e Fused With a Ubiquitin Moiety Is Essential for the Vegetative Growth, Morphological Homeostasis, Cell Cycle Progression, and Pathogenicity of Cryptococcus neoformans