Detailed Information on Publication Record
2011
Specificity and affinity modulation of PA-IIL lectin
POKORNÁ, Martina, Jana MRÁZKOVÁ and Michaela WIMMEROVÁBasic information
Original name
Specificity and affinity modulation of PA-IIL lectin
Authors
POKORNÁ, Martina (203 Czech Republic, belonging to the institution), Jana MRÁZKOVÁ (203 Czech Republic, belonging to the institution) and Michaela WIMMEROVÁ (203 Czech Republic, guarantor, belonging to the institution)
Edition
36th FEBS Congress, 2011
Other information
Language
English
Type of outcome
Konferenční abstrakt
Field of Study
10600 1.6 Biological sciences
Country of publisher
Italy
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 3.790
RIV identification code
RIV/00216224:14740/11:00050179
Organization unit
Central European Institute of Technology
ISSN
UT WoS
000292333102532
Keywords in English
PA-IIL; PA-IL; Pseudomonas aeruginosa; mutagenesis
Tags
Změněno: 28/12/2011 13:24, Mgr. Martina Pokorná, Ph.D., MBA
Abstract
V originále
Pseudomonas aeruginosa is a clinically important pathogen, which is responsible for numerous nosocomial infections in immunocompromised patients. The bacterium colonises patients with chronic lung diseases and its infection is fatal in cystic fibrosis patients. P. aeruginosa produces high levels of D galactose and L-fucose binding lectins, PA-IL (LecA) and PA-IIL (LecB) respectively, which are associated with its cytotoxic virulence and could be involved in primary recognition of the host organism and in biofilm formation.Additional experiments have been performed to order to understand the molecular basis of both specificity and affinity of PA-IIL for monosaccharides. Three single point mutants in position 22-23-24 have prepared and structure-functioned characterized. The mutated amino acids belong to the “specificity-binding loop”. The in vitro mutagenesis in combination with computational methods allowed the key importance of amino acid 22 for the specificity of the lectin to be identified.
Links
GPP207/11/P185, research and development project |
|