Engineering Escherichia coli to bind to cyanobacteria

Zhang, Zijian; Meng, Liping; Ni, Congjian; Yao, Lanqiu; Zhang, Fengyu; Jin, Yuji; Mu, Xuelang; Zhu, Shiyu; Lu, Xiaoyu; Liu, Shiyu; Yu, Congyu; Wang, Chenggong; Pu, Zheng; Wu, Jie; Li, Kang; Zhang, Haoqian; Ouyang, Qi

doi:10.1016/j.jbiosc.2016.09.010

Cited by 4 publications

(1 citation statement)

References 18 publications

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“…However, in that system, an externally added antibody was necessary to bring the cells together. Attachment between the cyanobacterium Microcystis aeruginosa and an E. coli strain engineered to display a cyanobacterial lectin has also been described (59).…”

Section: Discussionmentioning

confidence: 99%

Surface Display of Small Affinity Proteins on Synechocystis sp. Strain PCC 6803 Mediated by Fusion to the Major Type IV Pilin PilA1

2018

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Functional surface display of small affinity proteins, namely Affibodies (6.5 kDa), was evaluated for the model cyanobacterium sp. PCC 6803, through anchoring to native surface structures. These structures included confirmed or putative subunits of the type IV pili, the S-layer protein, and the heterologous autotransporter antigen 43 system. The most stable display system was determined to be through C-terminal fusion to PilA1, the major type IV pili subunit in , in a strain unable to retract these pili (Δ). Type IV pili synthesis was upheld, albeit reduced, when fusion proteins were incorporated. However, pili-mediated functions such as motility and transformational competency were negatively affected. Display of Affibodies on and the complementary anti-idiotypic Affibodies on or was able to mediate interspecies cell-cell binding by Affibody complex formation. The same strategy was however not able to drive cell-cell binding and aggregation of-only mixtures. Successful Affibody-tagging of the putative minor pilin PilA4 showed that it locates to the type IV pili in , and that its extracellular availability depends on PilA1. In addition, Affibody-tagging of the S-layer protein indicated that the domains responsible for anchoring and secretion of this protein are located at the N- and C-terminus, respectively. This study can serve as a basis for future surface display of proteins on for biotechnological applications. Cyanobacteria are gaining interest for their potential as autotrophic cell factories. Development of efficient surface display strategies could improve their suitability for large-scale applications by providing options for designed microbial consortia, cell immobilization, and biomass harvesting. Here, surface display of small affinity proteins was realized by fusing them to the major subunit of the native type IV pili in sp. PCC 6803. Display of complementary affinity proteins allowed specific cell-cell binding between and or Additionally, successful tagging of the putative pilin PilA4, helped determine its localization to the type IV pili. Analogous tagging of the S-layer protein shed light on the regions involved in its secretion and surface anchoring.

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Section: Discussionmentioning

confidence: 99%

Surface Display of Small Affinity Proteins on Synechocystis sp. Strain PCC 6803 Mediated by Fusion to the Major Type IV Pilin PilA1

2018

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Symbiotic Interactions of Phototrophic Microbes: Engineering Synthetic Consortia for Biotechnology

Fedeson

Ducat

2021

Role of Microbial Communities for Sustainability

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Engineering Adhesion of the Probiotic Strain Escherichia coli Nissle to the Fungal Pathogen Candida albicans

Chamas,

Svensson,

Maneira

et al. 2024

ACS Synth. Biol.

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Engineering live biotherapeutic products against fungal pathogens such as Candida albicans has been suggested as a means to tackle the increasing threat of fungal infections and the development of resistance to classical antifungal treatments. One important challenge in the design of live therapeutics is to control their localization inside the human body. The specific binding capability to target organisms or tissues would greatly increase their effectiveness by increasing the local concentration of effector molecules at the site of infection. In this study, we utilized surface display of carbohydrate binding domains to enable the probiotic E. coli Nissle 1917 to adhere specifically to the pathogenic yeast Candida albicans. Binding was quantified using a newly developed method based on the automated analysis of microscopic images. In addition to a rationally selected chitin binding domain, a synthetic peptide of identical length but distinct sequence also conferred binding. Efficient binding was specific to fungal hyphae, the invasive form of C. albicans, while the yeast form, as well as abiotic cellulose and PET particles, was only weakly recognized.

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Engineering Escherichia coli to bind to cyanobacteria

Cited by 4 publications

References 18 publications

Surface Display of Small Affinity Proteins on Synechocystis sp. Strain PCC 6803 Mediated by Fusion to the Major Type IV Pilin PilA1

Surface Display of Small Affinity Proteins on Synechocystis sp. Strain PCC 6803 Mediated by Fusion to the Major Type IV Pilin PilA1

Symbiotic Interactions of Phototrophic Microbes: Engineering Synthetic Consortia for Biotechnology

Engineering Adhesion of the Probiotic Strain Escherichia coli Nissle to the Fungal Pathogen Candida albicans

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