Structure and function of Photorhabdus asymbiotica lectins:
Studies of potential virulence factors from emerging human
pathogen

a 2016

Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen

POKORNÝ, Daniel, Gita JANČAŘÍKOVÁ, Jan KOMÁREK and Michaela WIMMEROVÁ

Basic information

Original name

Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen

Authors

POKORNÝ, Daniel (203 Czech Republic, belonging to the institution), Gita JANČAŘÍKOVÁ (203 Czech Republic, belonging to the institution), Jan KOMÁREK (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor)

Edition

XXV. Biochemický sjezd, 2016. 2016

Other information

Language

English

Type of outcome

Konferenční abstrakt

Field of Study

10600 1.6 Biological sciences

Country of publisher

Czech Republic

Confidentiality degree

není předmětem státního či obchodního tajemství

RIV identification code

RIV/00216224:14310/16:00088181

Organization unit

Faculty of Science

ISBN

978-80-270-0331-0

Keywords (in Czech)

lektiny; patogen; photorhabdus; strukturně-funkční charakterizace

Keywords in English

lectins; pathogen; photorhabdus; structure and function characterization

Změněno: 26/4/2017 22:17, Ing. Andrea Mikešková

Abstract

V originále

Lectins are ubiquitous carbohydrate-binding proteins found in bacteria, plants, animals, fungi and viruses where they play a key role in various processes. Our research is focused on lectins from Photorhabdus genus - gram-negative bioluminescent bacteria. Photorhabdus genus contains three species all of which are insect pathogens: P. luminescens, P. temperata and P. asymbiotica. Unlike other species in this genus, P. asymbiotica is also able to infect humans. In the P. asymbiotica genome, three genes of putative lectins named PHL, PHL2 and PHL3 were found. Recombinant lectins were studied using broad range of biophysical methods. For affinity measurements we employed isothermal titration calorimetry, micro-scale thermophoresis and surface plasmon resonance. The oligomeric state of the proteins was determined by analytical ultracentrifugation. We have optimized crystallization conditions using high throughput screening, and diffracting-quality crystals were used for structure determination. Structure-supported functional studies help us to understand molecular details of lectin function and their contribution to pathogenesis. Understanding the lectins role in pathogenic processes may be exploited for designing new therapeutic strategies.

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

Citovat

POKORNÝ, Daniel, Gita JANČAŘÍKOVÁ, Jan KOMÁREK and Michaela WIMMEROVÁ. Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen. In XXV. Biochemický sjezd, 2016. 2016. ISBN 978-80-270-0331-0.

@proceedings{1354852,
   author = {Pokorný, Daniel and Jančaříková, Gita and Komárek, Jan and Wimmerová, Michaela},
   booktitle = {XXV. Biochemický sjezd, 2016.},
   keywords = {lectins; pathogen; photorhabdus; structure and function characterization},
   language = {eng},
   isbn = {978-80-270-0331-0},
   title = {Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen},
   year = {2016}
}

TY  - CONF
ID  - 1354852
AU  - Pokorný, Daniel - Jančaříková, Gita - Komárek, Jan - Wimmerová, Michaela
PY  - 2016
TI  - Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen
SN  - 9788027003310
KW  - lectins
KW  - pathogen
KW  - photorhabdus
KW  - structure and function characterization
N2  - Lectins are ubiquitous carbohydrate-binding proteins found in bacteria, plants, animals, fungi and viruses where they play a key role in various processes. Our research is focused on lectins from Photorhabdus genus - gram-negative bioluminescent bacteria. Photorhabdus genus contains three species all of which are insect pathogens: P. luminescens, P. temperata and P. asymbiotica. Unlike other species in this genus, P. asymbiotica is also able to infect humans. In the P. asymbiotica genome, three genes of putative lectins named PHL, PHL2 and PHL3 were found. Recombinant lectins were studied using broad range of biophysical methods. For affinity measurements we employed isothermal titration calorimetry, micro-scale thermophoresis and surface plasmon resonance. The oligomeric state of the proteins was determined by analytical ultracentrifugation. We have optimized crystallization conditions using high throughput screening, and diffracting-quality crystals were used for structure determination. Structure-supported functional studies help us to understand molecular details of lectin function and their contribution to pathogenesis. Understanding the lectins role in pathogenic processes may be exploited for designing new therapeutic strategies.
ER  -

POKORNÝ, Daniel, Gita JANČAŘÍKOVÁ, Jan KOMÁREK and Michaela WIMMEROVÁ. Structure and function of Photorhabdus asymbiotica lectins: Studies of potential virulence factors from emerging human pathogen. In \textit{XXV. Biochemický sjezd, 2016.}. 2016. ISBN~978-80-270-0331-0.

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