Engineering the Pseudomonas aeruginosa II lectin: designing
mutants with changed affinity and specificity

J 2014

Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity

KŘÍŽ, Zdeněk, Jan ADAM, Jana MRÁZKOVÁ, Petros ZOTOS, Thomais CHATZIPAVLOU et. al.

Basic information

Original name

Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity

Name in Czech

Projektování II lektinu z Pseudomonas aeruginosa: navrhování mutantů se změněnou afinitou a specifitou

Authors

KŘÍŽ, Zdeněk (203 Czech Republic, belonging to the institution), Jan ADAM (203 Czech Republic, belonging to the institution), Jana MRÁZKOVÁ (203 Czech Republic, belonging to the institution), Petros ZOTOS (300 Greece, belonging to the institution), Thomais CHATZIPAVLOU (300 Greece, belonging to the institution), Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution) and Jaroslav KOČA (203 Czech Republic, belonging to the institution)

Edition

Journal of Computer-Aided Molecular Design, Dordrecht (Netherlands), Springer International Publishing, 2014, 0920-654X

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Switzerland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 2.990

RIV identification code

RIV/00216224:14740/14:00073859

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1007/s10822-014-9774-7

UT WoS

000342439000006

Keywords (in Czech)

Lektin; Cukr; Mutageneze; Docking; Molekularni dynamika

Keywords in English

Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics

Abstract

V originále

This article focuses on designing mutations of the PA-IIL lectin from Pseudomonas aeruginosa that lead to change in specificity. Following the previous results revealing the importance of the amino acid triad 22–23–24 (so-called specificity-binding loop), saturation in silico mutagenesis was performed, with the intent of finding mutations that increase the lectin’s affinity and modify its specificity. For that purpose, a combination of docking, molecular dynamics and binding free energy calculation was used. The combination of methods revealed mutations that changed the performance of the wild-type lectin and its mutants to their preferred partners. The mutation at position 22 resulted in 85 % in inactivation of the binding site, and the mutation at 23 did not have strong effects thanks to the side chain being pointed away from the binding site.

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

LH13055, research and development project

Name: Multidisciplinární přístup k návrhu léčiv - Inhibice proteinů s návazností na cukry (Acronym: MADICA)

Investor: Ministry of Education, Youth and Sports of the CR

286154, interní kód MU

Name: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Acronym: SYLICA)

Investor: European Union, Capacities

Citovat

KŘÍŽ, Zdeněk, Jan ADAM, Jana MRÁZKOVÁ, Petros ZOTOS, Thomais CHATZIPAVLOU, Michaela WIMMEROVÁ and Jaroslav KOČA. Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity. Journal of Computer-Aided Molecular Design. Dordrecht (Netherlands): Springer International Publishing, 2014, vol. 28, No 9, p. 951-960. ISSN 0920-654X. Available from: https://dx.doi.org/10.1007/s10822-014-9774-7.

@article{1198038,
   author = {Kříž, Zdeněk and Adam, Jan and Mrázková, Jana and Zotos, Petros and Chatzipavlou, Thomais and Wimmerová, Michaela and Koča, Jaroslav},
   article_location = {Dordrecht (Netherlands)},
   article_number = {9},
   doi = {http://dx.doi.org/10.1007/s10822-014-9774-7},
   keywords = {Lectin; Carbohydrate; Mutagenesis; Docking; Molecular dynamics},
   language = {eng},
   issn = {0920-654X},
   journal = {Journal of Computer-Aided Molecular Design},
   title = {Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity},
   url = {http://link.springer.com/article/10.1007%2Fs10822-014-9774-7},
   volume = {28},
   year = {2014}
}

TY  - JOUR
ID  - 1198038
AU  - Kříž, Zdeněk - Adam, Jan - Mrázková, Jana - Zotos, Petros - Chatzipavlou, Thomais - Wimmerová, Michaela - Koča, Jaroslav
PY  - 2014
TI  - Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity
JF  - Journal of Computer-Aided Molecular Design
VL  - 28
IS  - 9
SP  - 951-960
EP  - 951-960
PB  - Springer International Publishing
SN  - 0920654X
KW  - Lectin
KW  - Carbohydrate
KW  - Mutagenesis
KW  - Docking
KW  - Molecular dynamics
UR  - http://link.springer.com/article/10.1007%2Fs10822-014-9774-7
L2  - http://link.springer.com/article/10.1007%2Fs10822-014-9774-7
N2  - This article focuses on designing mutations of the PA-IIL lectin from Pseudomonas aeruginosa that lead to change in specificity. Following the previous results revealing the importance of the amino acid triad 22–23–24 (so-called specificity-binding loop), saturation in silico mutagenesis was performed, with the intent of finding mutations that increase the lectin’s affinity and modify its specificity. For that purpose, a combination of docking, molecular dynamics and binding free energy calculation was used. The combination of methods revealed mutations that changed the performance of the wild-type lectin and its mutants to their preferred partners. The mutation at position 22 resulted in 85 % in inactivation of the binding site, and the mutation at 23 did not have strong effects thanks to the side chain being pointed away from the binding site.
ER  -

KŘÍŽ, Zdeněk, Jan ADAM, Jana MRÁZKOVÁ, Petros ZOTOS, Thomais CHATZIPAVLOU, Michaela WIMMEROVÁ and Jaroslav KOČA. Engineering the Pseudomonas aeruginosa II lectin: designing mutants with changed affinity and specificity. \textit{Journal of Computer-Aided Molecular Design}. Dordrecht (Netherlands): Springer International Publishing, 2014, vol.~28, No~9, p.~951-960. ISSN~0920-654X. Available from: https://dx.doi.org/10.1007/s10822-014-9774-7.

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