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Surface Display of Designer Protein Scaffolds on Genome-Reduced Strains of Pseudomonas putida

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F20%3A00114419" target="_blank" >RIV/00216224:14310/20:00114419 - isvavai.cz</a>

  • Result on the web

    <a href="https://doi.org/10.1021/acssynbio.0c00276" target="_blank" >https://doi.org/10.1021/acssynbio.0c00276</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1021/acssynbio.0c00276" target="_blank" >10.1021/acssynbio.0c00276</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Surface Display of Designer Protein Scaffolds on Genome-Reduced Strains of Pseudomonas putida

  • Original language description

    The bacterium Pseudomonas putida KT2440 is gaining considerable interest as a microbial platform for biotechnological valorization of polymeric organic materials, such as lignocellulosic residues or plastics. However, P. putida on its own cannot make much use of such complex substrates, mainly because it lacks an efficient extracellular depolymerizing apparatus. We seek to address this limitation by adopting a recombinant cellulosome strategy for this host. In this work, we report an essential step in this endeavor—a display of designer enzyme-anchoring protein “scaffoldins”, encompassing cohesin binding domains from divergent cellulolytic bacterial species on the P. putida surface. Two P. putida chassis strains, EM42 and EM371, with streamlined genomes and differences in the composition of the outer membrane were employed in this study. Scaffoldin variants were optimally delivered to their surface with one of four tested autotransporter systems (Ag43 from Escherichia coli), and the efficient display was confirmed by extracellular attachment of chimeric beta-glucosidase and fluorescent proteins. Our results not only highlight the value of cell surface engineering for presentation of recombinant proteins on the envelope of Gram-negative bacteria but also pave the way toward designer cellulosome strategies tailored for P. putida.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    <a href="/en/project/GJ19-06511Y" target="_blank" >GJ19-06511Y: Orthogonalisation of carbohydrate metabolism in bacterial chassis Pseudomonas putida EM42 for co-utilisation of lignocellulose-derived sugars</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    ACS Synthetic Biology

  • ISSN

    2161-5063

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    10

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    16

  • Pages from-to

    2749-2764

  • UT code for WoS article

    000582582100014

  • EID of the result in the Scopus database

    2-s2.0-85093538854