a 2014

Structure-functional study of PHL lectin from Photorhabdus asymbiotica

JANČAŘÍKOVÁ, Gita, Gabriel DEMO, Jan KOMÁREK and Michaela WIMMEROVÁ

Basic information

Original name

Structure-functional study of PHL lectin from Photorhabdus asymbiotica

Authors

JANČAŘÍKOVÁ, Gita (203 Czech Republic, belonging to the institution), Gabriel DEMO (703 Slovakia, belonging to the institution), Jan KOMÁREK (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor)

Edition

FEBS Young Scientists' Forum, 2014

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10600 1.6 Biological sciences

Country of publisher

France

Confidentiality degree

není předmětem státního či obchodního tajemství

RIV identification code

RIV/00216224:14740/14:00074015

Organization unit

Central European Institute of Technology

Keywords (in Czech)

lektin Photorhabdus asymbiotica

Keywords in English

lectin Photorhabdus asymbiotica
Změněno: 30/12/2014 15:56, Mgr. Gabriel Demo, Ph.D.

Abstract

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.

Links

ED1.1.00/02.0068, research and development project
Name: CEITEC - central european institute of technology
GA13-25401S, research and development project
Name: Studium proteinů z patogenů zapojených do rozpoznávání hostitelského organismu
Investor: Czech Science Foundation