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SH3 BINDING DOMAINS FROM PHAGE ENDOLYSINS: HOW TO USE THEM FOR DETECTION OF GRAMPOSITIVE PATHOGENS

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F20%3A00116228" target="_blank" >RIV/00216224:14310/20:00116228 - isvavai.cz</a>

  • Výsledek na webu

    <a href="https://www.jmbfs.org/wp-content/uploads/2020/06/jmbfs_1692_Jarabkova.pdf" target="_blank" >https://www.jmbfs.org/wp-content/uploads/2020/06/jmbfs_1692_Jarabkova.pdf</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.15414/jmbfs.2020.9.6.1215-1220" target="_blank" >10.15414/jmbfs.2020.9.6.1215-1220</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    SH3 BINDING DOMAINS FROM PHAGE ENDOLYSINS: HOW TO USE THEM FOR DETECTION OF GRAMPOSITIVE PATHOGENS

  • Popis výsledku v původním jazyce

    Phage-encoded enzymes, called endolysins, could be linked to the purpose of specifically detecting and treating Gram-positive pathogens, such as drug-resistant bacteria Staphylococcus aureus or Streptococcus agalactiae. Most endolysins encoded by staphylococcal phages are composed of a C-terminal SH3b type domain, an amidase catalytic domain in the central position and an Nterminal catalytic domain with endopeptidase activity. Furthermore, endolysins from a streptococcal phage, e.g. B30 consist of a dualenzyme active domain (EAD)- muramidase and endopeptidase and one or several cell wall binding domains (CBD), in this case SH3. An nderstanding of CBDs and domain design that has a high degree of host specificity may lead to shifts in the lytic spectrum of a chimeric endolysin. Our research was focused on the in silico analysis of CBDs of endolysins encoded by staphylococcal and streptococcal phages. Gene for specific binding domain (SBD) was designed based on bioinformatics approaches. The coding gene sequence of the SBD domain was subsequently fused with thegene for GFP (green fluorescent protein) and subcloned into the pET21 expression vector. The domain was prepared as a fusion recombinant protein and analyzed for its binding function. This capability was shown by the fusion of SBD with fluorescent tag - GFP, followed by fluorescent microscopy. Binding assays showed that SBD was able to bind to living cells of Staphylococcus aureus and Streptococcus agalactiae. Because of these properties, CBDs may be used as tools in alternative diagnostic methods. The fusions of SBD and EAD may bring the chimeric endolysin for being utilized as novel therapeutic agents.

  • Název v anglickém jazyce

    SH3 BINDING DOMAINS FROM PHAGE ENDOLYSINS: HOW TO USE THEM FOR DETECTION OF GRAMPOSITIVE PATHOGENS

  • Popis výsledku anglicky

    Phage-encoded enzymes, called endolysins, could be linked to the purpose of specifically detecting and treating Gram-positive pathogens, such as drug-resistant bacteria Staphylococcus aureus or Streptococcus agalactiae. Most endolysins encoded by staphylococcal phages are composed of a C-terminal SH3b type domain, an amidase catalytic domain in the central position and an Nterminal catalytic domain with endopeptidase activity. Furthermore, endolysins from a streptococcal phage, e.g. B30 consist of a dualenzyme active domain (EAD)- muramidase and endopeptidase and one or several cell wall binding domains (CBD), in this case SH3. An nderstanding of CBDs and domain design that has a high degree of host specificity may lead to shifts in the lytic spectrum of a chimeric endolysin. Our research was focused on the in silico analysis of CBDs of endolysins encoded by staphylococcal and streptococcal phages. Gene for specific binding domain (SBD) was designed based on bioinformatics approaches. The coding gene sequence of the SBD domain was subsequently fused with thegene for GFP (green fluorescent protein) and subcloned into the pET21 expression vector. The domain was prepared as a fusion recombinant protein and analyzed for its binding function. This capability was shown by the fusion of SBD with fluorescent tag - GFP, followed by fluorescent microscopy. Binding assays showed that SBD was able to bind to living cells of Staphylococcus aureus and Streptococcus agalactiae. Because of these properties, CBDs may be used as tools in alternative diagnostic methods. The fusions of SBD and EAD may bring the chimeric endolysin for being utilized as novel therapeutic agents.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10600 - Biological sciences

Návaznosti výsledku

  • Projekt

  • Návaznosti

    S - Specificky vyzkum na vysokych skolach

Ostatní

  • Rok uplatnění

    2020

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    Journal of Microbiology, Biotechnology & Food Sciences

  • ISSN

    1338-5178

  • e-ISSN

  • Svazek periodika

    9

  • Číslo periodika v rámci svazku

    6

  • Stát vydavatele periodika

    SK - Slovenská republika

  • Počet stran výsledku

    6

  • Strana od-do

    1215-1220

  • Kód UT WoS článku

    000579127100031

  • EID výsledku v databázi Scopus

    2-s2.0-85089347252