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Abstract
Members of the Corynebacterineae suborder of Actinobacteria have a unique cell surface architecture and, unlike most well-studied bacteria, grow by tip-extension. To investigate the distinct morphogenic mechanisms shared by these organisms, we performed a genome-wide phenotypic profiling analysis using Corynebacterium glutamicum as a model. A high-density transposon mutagenized library was challenged with a panel of antibiotics and other stresses. The fitness of mutants in each gene under each condition was then assessed by transposon-sequencing. Clustering of the resulting phenotypic fingerprints revealed a role for several genes of previously unknown function in surface biogenesis. Further analysis identified CofA (Cgp_0016) as an interaction partner of the peptidoglycan synthase PBP1a that promotes its stable accumulation at sites of polar growth. The related Mycobacterium tuberculosis proteins were also found to interact, highlighting the utility of our dataset for uncovering conserved principles of morphogenesis for this clinically relevant bacterial suborder.
Highlights
Several medically important pathogens belong to the Corynebacterineae suborder of Actinobacteria, including Corynebacterium diphtheriae and Mycobacterium tuberculosis (Mtb)
We found that cognate CofA-PBP proteins from Mycobacterium tuberculosis and a pathogenic corynebacterium participate in specific interactions
The mechanisms underlying envelope biogenesis, polar cell growth, and cell division remain poorly understood for the Corynebacterineae suborder and the Actinobacteria phylum in general
Summary
Several medically important pathogens belong to the Corynebacterineae suborder of Actinobacteria, including Corynebacterium diphtheriae and Mycobacterium tuberculosis (Mtb). Like most bacteria, these organisms surround their cytoplasmic membrane with an essential cell wall matrix made of the heteropolymer peptidoglycan (PG). These organisms surround their cytoplasmic membrane with an essential cell wall matrix made of the heteropolymer peptidoglycan (PG) They uniquely modify the PG layer with an additional polysaccharide made of arabinan and galactan chains (Kieser and Rubin, 2014; Alderwick et al, 2015; Daffeand Marrakchi, 2019). Enhancing our understanding of the assembly mechanisms that construct the mycolata envelope has practical implications for anti-mycobacterial therapeutic discovery in addition to addressing a fundamental problem in microbiology
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