Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum

Wael Elhenawy, Nichollas E. Scott, M. Laura Tondo, Elena G. Orellano, Leonard J. Foster, Mario F. Feldman

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

Ralstonia solanacearum is one of the most lethal phytopathogens in the world. Due to its broad host range, it can cause wilting disease in many plant species of economic interest. In this work, we identified the O-oligosaccharyltransferase (O-OTase) responsible for protein O-glycosylation in R. solanacearum. An analysis of the glycoproteome revealed that 20 proteins, including type IV pilins are substrates of this general glycosylation system. Although multiple glycan forms were identified, the majority of the glycopeptides were modified with a pentasaccharide composed of HexNAc-(Pen)-dHex3, similar to the O antigen subunit present in the lipopolysaccharide of multiple R. solanacearum strains. Disruption of the O-OTase led to the total loss of protein glycosylation, together with a defect in biofilm formation and reduced pathogenicity towards tomato plants. Comparative proteomic analysis revealed that the loss of glycosylation is not associated with widespread proteome changes. Only the levels of a single glycoprotein, the type IV pilin, were diminished in the absence of glycosylation. In parallel, disruption of glycosylation triggered an increase in the levels of a surface lectin homologous to Pseudomonas PA-IIL. These results reveal the important role of glycosylation in the pathogenesis of R. solanacearum.

Original languageEnglish
Pages (from-to)301-311
Number of pages11
JournalGlycobiology
Volume26
Issue number3
DOIs
StatePublished - Jul 10 2015

Keywords

  • Type IV pili
  • biofilm
  • protein O-glycosylation

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    Elhenawy, W., Scott, N. E., Tondo, M. L., Orellano, E. G., Foster, L. J., & Feldman, M. F. (2015). Protein O-linked glycosylation in the plant pathogen Ralstonia solanacearum. Glycobiology, 26(3), 301-311. https://doi.org/10.1093/glycob/cwv098