@article{mbs:/content/journal/micro/10.1099/mic.0.057653-0, author = "Mishra, Arun K. and Krumbach, Karin and Rittmann, Doris and Batt, Sarah M. and Lee, Oona Y.-C. and De, Sandip and Frunzke, Julia and Besra, Gurdyal S. and Eggeling, Lothar", title = "Deletion of manC in Corynebacterium glutamicum results in a phospho-myo-inositol mannoside- and lipoglycan-deficient mutant", journal= "Microbiology", year = "2012", volume = "158", number = "7", pages = "1908-1917", doi = "https://doi.org/10.1099/mic.0.057653-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.057653-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", abstract = "Mannose is an important constituent of the immunomodulatory glycoconjugates of the mycobacterial cell wall: lipoarabinomannan (LAM), lipomannan (LM) and the related phospho-myo-inositol mannosides (PIMs). In Mycobacterium tuberculosis and the related bacillus Corynebacterium glutamicum, mannose is either imported from the medium or derived from glycolysis, and is subsequently converted into the nucleotide-based sugar donor guanosine diphosphomannose (GDP-mannose). This can be utilized by the glycosyltranferases of the GT-A/B superfamily or converted to the lipid-based donor polyprenyl monophosphomannose, and used as a substrate by the transmembrane glycosyltransferases of the GT-C superfamily. To investigate GDP-mannose biosynthesis in detail, the gene encoding a putative ManC in C. glutamicum was deleted. Deletion of manC resulted in a slow-growing mutant, with reduced but not totally abrogated guanosine diphosphomannose pyrophosphorylase activity. However, a comprehensive cell wall analysis revealed that C. glutamicumĪ”manC is deficient in PIMs and LM/LAM. Closer inspection suggests that promiscuous ManC activity is contributed by additional putative nucleotidyltransferases, PmmB, WbbL1, GalU and GlmU, and a hypothetical protein, NCgl0715. Furthermore, complementation analyses of C. glutamicumĪ”manC with Rv3264c suggested that it is a true homologue of ManC in M. tuberculosis, and the essentiality of PIMs in M. tuberculosis makes it an attractive drug target.", }