Lethality of sortase depletion in Actinomyces oris caused by excessive membrane accumulation of a surface glycoprotein.
作者： Chenggang Wu , I‐Hsiu Huang , Chungyu Chang , Melissa Elizabeth Reardon‐Robinson , Asis Das
DOI: 10.1111/MMI.12780
关键词:
摘要: Summary Sortase, a cysteine-transpeptidase conserved in Gram-positive bacteria, anchors on the cell wall many surface proteins that facilitate bacterial pathogenesis and fitness. Genetic disruption of housekeeping sortase several pathogens reported thus far attenuates virulence, but not growth. Paradoxically, we discovered depletion SrtA was lethal for Actinomyces oris; yet, all its predicted wall-anchored protein substrates (AcaA-N) were individually dispensable viability. Using Tn5-transposon mutagenesis to identify factors upend lethality srtA deletion, uncovered set genetic suppressors harbouring transposon insertions within genes locus encoding AcaC LytR-CpsA-Psr (LCP)-like protein. shown be highly glycosylated dependent LCP glycosylation. Upon depletion, form AcaC, hereby renamed GspA, accumulated membrane. Overexpression GspA mutant lacking gspA lethal; conversely, cells overexpressing missing membrane-localization domain viable. The results reveal unique glycosylation pathway A. oris is coupled anchoring catalysed by SrtA. Significantly, this novel phenomenon glyco-stress provides convenient cell-based assays developing new class inhibitors against pathogens.
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