Solving the mysteries of novel two-domain lectins from human
pathogens

k 2025

Solving the mysteries of novel two-domain lectins from human pathogens

BURÁŇOVÁ, Tereza; Eva PAULENOVÁ a Michaela WIMMEROVÁ

Základní údaje

Originální název

Solving the mysteries of novel two-domain lectins from human pathogens

Autoři

BURÁŇOVÁ, Tereza ; Eva PAULENOVÁ a Michaela WIMMEROVÁ

Vydání

XXIV. Interdisciplinary Meeting of Young Life Scientists, 2025

Další údaje

Jazyk

angličtina

Typ výsledku

Prezentace na konferencích

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/25:00141771

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova česky

lektiny; dvoudoménové proteiny; rekombinantní proteiny

Klíčová slova anglicky

lectins; two-domain proteins; recombinant proteins

Štítky

143160

Změněno: 11. 8. 2025 15:34, Mgr. Tereza Buráňová

Anotace

V originále

LecB (PA-IIL) is one of two characterized lectins (saccharide-binding proteins) from the bacterium Pseudomonas aeruginosa. Both proteins (LecA and LecB) play a significant role in bacterial infection and biofilm formation in patients with immune deficiencies (e.g. cystic fibrosis patients)1. Several LecB homologs were described in the past, for example, lectins produced by Burkholderia cenocepacia2. Nevertheless, there are still uncharacterized LecB-like proteins in the pathogenic bacteria, some of which contain an additional domain of unknown function. Their characterization could provide insights into the mechanism of infections and lead to the development of novel approaches to disease treatment. The aim of this project is the functional and structural characterization of three potential two-domain lectins containing a LecB-like domain with emphasis on their binding properties. The genes encoding these hypothetical carbohydrate-specific proteins were identified by bioinformatic analysis, cloned into expression vectors, and expressed in Escherichia coli. In addition, new gene constructs were prepared to characterize each domain separately. A variety of methods were used to investigate thermostability (nanoDSF), homogeneity (DLS, AUC), and binding properties (ITC, AUC) of the purified proteins. Several crystallization screens were performed to obtain the crystals of the separate domains. The initial hits for X-ray crystallography are currently optimized to obtain well-diffracting crystals. For the whole proteins, electron microscopy methods are planned because of the expected high dynamics of the whole system.

Návaznosti

LM2023042, projekt VaV

Název: Česká infrastruktura pro integrativní strukturní biologii

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CIISB - Česká infrastruktura pro integrativní strukturní biologii

Citovat

BURÁŇOVÁ, Tereza; Eva PAULENOVÁ a Michaela WIMMEROVÁ. Solving the mysteries of novel two-domain lectins from human pathogens. In XXIV. Interdisciplinary Meeting of Young Life Scientists. 2025.

@proceedings{2511800,
   author = {Buráňová, Tereza and Paulenová, Eva and Wimmerová, Michaela},
   booktitle = {XXIV. Interdisciplinary Meeting of Young Life Scientists},
   keywords = {lectins; two-domain proteins; recombinant proteins},
   language = {eng},
   title = {Solving the mysteries of novel two-domain lectins from human pathogens},
   year = {2025}
}

TY  - CONF
ID  - 2511800
AU  - Buráňová, Tereza - Paulenová, Eva - Wimmerová, Michaela
PY  - 2025
TI  - Solving the mysteries of novel two-domain lectins from human pathogens
KW  - lectins
KW  - two-domain proteins
KW  - recombinant proteins
N2  - LecB (PA-IIL) is one of two characterized lectins (saccharide-binding proteins) from the bacterium Pseudomonas aeruginosa. Both proteins (LecA and LecB) play a significant role in bacterial infection and biofilm formation in patients with immune deficiencies (e.g. cystic fibrosis patients)1. Several LecB homologs were described in the past, for example, lectins produced by Burkholderia cenocepacia2. Nevertheless, there are still uncharacterized LecB-like proteins in the pathogenic bacteria, some of which contain an additional domain of unknown function. Their characterization could provide insights into the mechanism of infections and lead to the development of novel approaches to disease treatment. The aim of this project is the functional and structural characterization of three potential two-domain lectins containing a LecB-like domain with emphasis on their binding properties. The genes encoding these hypothetical carbohydrate-specific proteins were identified by bioinformatic analysis, cloned into expression vectors, and expressed in Escherichia coli. In addition, new gene constructs were prepared to characterize each domain separately. A variety of methods were used to investigate thermostability (nanoDSF), homogeneity (DLS, AUC), and binding properties (ITC, AUC) of the purified proteins. Several crystallization screens were performed to obtain the crystals of the separate domains. The initial hits for X-ray crystallography are currently optimized to obtain well-diffracting crystals. For the whole proteins, electron microscopy methods are planned because of the expected high dynamics of the whole system.
ER  -

BURÁŇOVÁ, Tereza; Eva PAULENOVÁ a Michaela WIMMEROVÁ. Solving the mysteries of novel two-domain lectins from human pathogens. In \textit{XXIV. Interdisciplinary Meeting of Young Life Scientists}. 2025.

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