Structure-functional study of PHL lectin from Photorhabdus
asymbiotica

a 2014

Structure-functional study of PHL lectin from Photorhabdus asymbiotica

JANČAŘÍKOVÁ, Gita; Gabriel DEMO; Jan KOMÁREK a Michaela WIMMEROVÁ

Základní údaje

Originální název

Structure-functional study of PHL lectin from Photorhabdus asymbiotica

Autoři

JANČAŘÍKOVÁ, Gita; Gabriel DEMO; Jan KOMÁREK a Michaela WIMMEROVÁ

Vydání

FEBS Young Scientists' Forum, 2014

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Stát vydavatele

Francie

Utajení

není předmětem státního či obchodního tajemství

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/14:00074015

Organizační jednotka

Středoevropský technologický institut

Klíčová slova česky

lektin Photorhabdus asymbiotica

Klíčová slova anglicky

lectin Photorhabdus asymbiotica

Změněno: 30. 12. 2014 15:56, Mgr. Gabriel Demo, Ph.D.

Anotace

V originále

Lectins are a very important group of proteins and glycoproteins, which specifically recognize and reversibly bind glycoconjugates. Due to this interaction, lectins play a crucial role in many physiological and pathophysiological processes including immunological reactions or interactions between tissue’s cells. They also play a very important role in interactions between a pathogen and its host as they can mediate the first step of an expansion of infection. Our project is focused on study of a new lectin from the Photorhabdus asymbiotica bacterium. This bacterium is characterized as pathogen of both insects and humans. We have identified a new putative lectin (PHL) in the P. asymbiotica genome with the predicted structure similarity to the lectins from so-called AAL family, which are specific for fucosylated oligosaccharides. The AAL family contains AAL from Aleuria aurantia which inhibits a repair of epithelia or the RSL lectin from Ralstonia solanaccearum predicted as one of the key virulent factors of this plant pathogen. A wide range of methods was used for structural a functional studies of PHL. The crystal structure of PHL revealed a presence of fourteen potential binding sites per monomer. PHL belongs to seven beta-propellers, which makes this protein unique compared to proteins from AAL family, which share the six beta-propeller fold. Crystal structures of PHL with different saccharides demonstrated two types of binding sites, which could bind ligands with different polarity. PHL showed highest affinity to fucose among studied monosaccharides and binding properties of PHL will be further studied with more complex saccharides.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GA13-25401S, projekt VaV

Název: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu

Investor: Grantová agentura ČR, Studium proteinu z patogenu zapojených do rozpoznávání hostitelského organismu

Citovat

JANČAŘÍKOVÁ, Gita; Gabriel DEMO; Jan KOMÁREK a Michaela WIMMEROVÁ. Structure-functional study of PHL lectin from Photorhabdus asymbiotica. In FEBS Young Scientists' Forum. 2014.

@proceedings{1204397,
   author = {Jančaříková, Gita and Demo, Gabriel and Komárek, Jan and Wimmerová, Michaela},
   booktitle = {FEBS Young Scientists' Forum},
   keywords = {lectin Photorhabdus asymbiotica},
   language = {eng},
   title = {Structure-functional study of PHL lectin from Photorhabdus asymbiotica},
   year = {2014}
}

TY  - CONF
ID  - 1204397
AU  - Jančaříková, Gita - Demo, Gabriel - Komárek, Jan - Wimmerová, Michaela
PY  - 2014
TI  - Structure-functional study of PHL lectin from Photorhabdus asymbiotica
KW  - lectin Photorhabdus asymbiotica
N2  - Lectins are a very important group of proteins and glycoproteins, which specifically recognize and reversibly bind glycoconjugates. Due to this interaction, lectins play a crucial role in many physiological and pathophysiological processes including immunological reactions or interactions between tissue’s cells. They also play a very important role in interactions between a pathogen and its host as they can mediate the first step of an expansion of infection. Our project is focused on study of a new lectin from the Photorhabdus asymbiotica bacterium. This bacterium is characterized as pathogen of both insects and humans. We have identified a new putative lectin (PHL) in the P. asymbiotica genome with the predicted structure similarity to the lectins from so-called AAL family, which are specific for fucosylated oligosaccharides. The AAL family contains AAL from Aleuria aurantia which inhibits a repair of epithelia or the RSL lectin from Ralstonia solanaccearum predicted as one of the key virulent factors of this plant pathogen. A wide range of methods was used for structural a functional studies of PHL. The crystal structure of PHL revealed a presence of fourteen potential binding sites per monomer. PHL belongs to seven beta-propellers, which makes this protein unique compared to proteins from AAL family, which share the six beta-propeller fold. Crystal structures of PHL with different saccharides demonstrated two types of binding sites, which could bind ligands with different polarity. PHL showed highest affinity to fucose among studied monosaccharides and binding properties of PHL will be further studied with more complex saccharides.
ER  -

JANČAŘÍKOVÁ, Gita; Gabriel DEMO; Jan KOMÁREK a Michaela WIMMEROVÁ. Structure-functional study of PHL lectin from Photorhabdus asymbiotica. In \textit{FEBS Young Scientists' Forum}. 2014.

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