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Author
- Howell, P Lynne2
- Andole Pannuri, Archana1
- Azadi, Parastoo1
- Cao, Xiou1
- Carlson, Russell W1
- Ferreira, Ana Sofia1
- Heiss, Christian1
- Hjuler, Christian T1
- Hobley, Laura1
- Huang, Yihua1
- Kelly, Simon J1
- Khomutov, Alexey1
- Khomutov, Maxim1
- Kim, Sok Ho1
- Li, Bin1
- Lobsanov, Yuri D1
- Lu, Xiaomei1
- Marmont, Lindsey S1
- Maunders, Eve A1
- Michael, Anthony J1
- Muszyński, Artur1
- Naidoo, Jacinth1
- Neculai, A Mirela1
- Ni, Dongchun1
- Ohman, Dennis E1
Keyword
- biofilm4
- polysaccharide3
- bacterial adhesion2
- extracellular matrix2
- Pseudomonas aeruginosa (P. aeruginosa)2
- transcriptomics2
- acetylation1
- agmatine1
- alginate1
- aminoglycoside1
- aminopropyl1
- antibiotic resistance1
- Bacillus subtilis1
- bacteria1
- carbohydrate biosynthesis1
- FusA11
- Mesorhizobium loti1
- PgaA1
- PilZ1
- Pseudomonas aeruginosa1
- Type III secretion1
- Type III secretion system (T3SS)1
- Type VI secretion1
- Type VI secretion system1
Microbiology
6 Results
- MicrobiologyOpen Access
Global reprogramming of virulence and antibiotic resistance in Pseudomonas aeruginosa by a single nucleotide polymorphism in elongation factor, fusA1
Journal of Biological ChemistryVol. 295Issue 48p16411–16426Published online: September 17, 2020- Eve A. Maunders
- Rory C. Triniman
- Joshua Western
- Taufiq Rahman
- Martin Welch
Cited in Scopus: 12Clinical isolates of the opportunistic pathogen Pseudomonas aeruginosa from patients with cystic fibrosis (CF) frequently contain mutations in the gene encoding an elongation factor, FusA1. Recent work has shown that fusA1 mutants often display elevated aminoglycoside resistance due to increased expression of the efflux pump, MexXY. However, we wondered whether these mutants might also be affected in other virulence-associated phenotypes. Here, we isolated a spontaneous gentamicin-resistant fusA1 mutant (FusA1P443L) in which mexXY expression was increased. - MicrobiologyOpen Access
Spermidine promotes Bacillus subtilis biofilm formation by activating expression of the matrix regulator slrR
Journal of Biological ChemistryVol. 292Issue 29p12041–12053Published online: May 25, 2017- Laura Hobley
- Bin Li
- Jennifer L. Wood
- Sok Ho Kim
- Jacinth Naidoo
- Ana Sofia Ferreira
- and others
Cited in Scopus: 28Ubiquitous polyamine spermidine is not required for normal planktonic growth of Bacillus subtilis but is essential for robust biofilm formation. However, the structural features of spermidine required for B. subtilis biofilm formation are unknown and so are the molecular mechanisms of spermidine-stimulated biofilm development. We report here that in a spermidine-deficient B. subtilis mutant, the structural analogue norspermidine, but not homospermidine, restored biofilm formation. Intracellular biosynthesis of another spermidine analogue, aminopropylcadaverine, from exogenously supplied homoagmatine also restored biofilm formation. - Glycobiology and Extracellular MatricesOpen Access
Structures of Exopolysaccharides Involved in Receptor-mediated Perception of Mesorhizobium loti by Lotus japonicus
Journal of Biological ChemistryVol. 291Issue 40p20946–20961Published online: September 1, 2016- Artur Muszyński
- Christian Heiss
- Christian T. Hjuler
- John T. Sullivan
- Simon J. Kelly
- Mikkel B. Thygesen
- and others
Cited in Scopus: 26In the symbiosis formed between Mesorhizobium loti strain R7A and Lotus japonicus Gifu, rhizobial exopolysaccharide (EPS) plays an important role in infection thread formation. Mutants of strain R7A affected in early exopolysaccharide biosynthetic steps form nitrogen-fixing nodules on L. japonicus Gifu after a delay, whereas mutants affected in mid or late biosynthetic steps induce uninfected nodule primordia. Recently, it was shown that a plant receptor-like kinase, EPR3, binds low molecular mass exopolysaccharide from strain R7A to regulate bacterial passage through the plant's epidermal cell layer (Kawaharada, Y., Kelly, S., Nielsen, M. - MinireviewsOpen Access
Biofilm Exopolysaccharides of Pathogenic Fungi: Lessons from Bacteria
Journal of Biological ChemistryVol. 291Issue 24p12529–12537Published online: April 21, 2016- Donald C. Sheppard
- P. Lynne Howell
Cited in Scopus: 79Exopolysaccharides play an important structural and functional role in the development and maintenance of microbial biofilms. Although the majority of research to date has focused on the exopolysaccharide systems of biofilm-forming bacteria, recent studies have demonstrated that medically relevant fungi such as Candida albicans and Aspergillus fumigatus also form biofilms during infection. These fungal biofilms share many similarities with those of bacteria, including the presence of secreted exopolysaccharides as core components of the extracellular matrix. - Protein Structure and FoldingOpen Access
Structural Basis for Translocation of a Biofilm-supporting Exopolysaccharide across the Bacterial Outer Membrane
Journal of Biological ChemistryVol. 291Issue 19p10046–10057Published online: March 8, 2016- Yan Wang
- Archana Andole Pannuri
- Dongchun Ni
- Haizhen Zhou
- Xiou Cao
- Xiaomei Lu
- and others
Cited in Scopus: 33The partially de-N-acetylated poly-β-1,6-N-acetyl-d-glucosamine (dPNAG) polymer serves as an intercellular biofilm adhesin that plays an essential role for the development and maintenance of integrity of biofilms of diverse bacterial species. Translocation of dPNAG across the bacterial outer membrane is mediated by a tetratricopeptide repeat-containing outer membrane protein, PgaA. To understand the molecular basis of dPNAG translocation, we determined the crystal structure of the C-terminal transmembrane domain of PgaA (residues 513–807). - MicrobiologyOpen Access
Dimeric c-di-GMP Is Required for Post-translational Regulation of Alginate Production in Pseudomonas aeruginosa
Journal of Biological ChemistryVol. 290Issue 20p12451–12462Published online: March 27, 2015- John C. Whitney
- Gregory B. Whitfield
- Lindsey S. Marmont
- Patrick Yip
- A. Mirela Neculai
- Yuri D. Lobsanov
- and others
Cited in Scopus: 60Background:Alg44 regulates the production of alginate in Pseudomonas aeruginosa via c-di-GMP binding.Results:The structure of the PilZ domain of Alg44 in complex with c-di-GMP reveals residues that control c-di-GMP/Alg44 stoichiometry.Conclusion:Binding of dimeric c-di-GMP is required for alginate biosynthesis.Significance:This is the first example of a receptor requiring a specific form of c-di-GMP for activation.