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 a Michaela WIMMEROVÁ

Základní údaje

Originální název

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

Autoři

POKORNÝ, Daniel; Gita JANČAŘÍKOVÁ; Jan KOMÁREK a Michaela WIMMEROVÁ

Vydání

XXV. Biochemický sjezd, 2016. 2016

Další údaje

Jazyk

angličtina

Typ výsledku

Konferenční abstrakt

Obor

10600 1.6 Biological sciences

Stát vydavatele

Česká republika

Utajení

není předmětem státního či obchodního tajemství

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/16:00088181

Organizační jednotka

Přírodovědecká fakulta

ISBN

978-80-270-0331-0

Klíčová slova česky

lektiny; patogen; photorhabdus; strukturně-funkční charakterizace

Klíčová slova anglicky

lectins; pathogen; photorhabdus; structure and function characterization

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

Anotace

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.

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

POKORNÝ, Daniel; Gita JANČAŘÍKOVÁ; Jan KOMÁREK a 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 a 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.

Přehled o publikaci