Structural insights into Aspergillus fumigatus lectin
specificity: AFL binding sites are functionally non-equivalent

J 2015

Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent

HOUSER, Josef; Jan KOMÁREK; Gianluca CIOCI; Annabelle VARROT; Anne IMBERTY et al.

Základní údaje

Originální název

Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent

Název česky

Strukturní pohled na specifitu lektinu z Aspergillus fumigatus: vazebná místa AFL jsou funkčně neekvivalentní

Autoři

HOUSER, Josef; Jan KOMÁREK ; Gianluca CIOCI; Annabelle VARROT; Anne IMBERTY a Michaela WIMMEROVÁ

Vydání

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, HOBOKEN, WILEY-BLACKWELL, 2015, 1399-0047

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.680 v roce 2014

Kód RIV

RIV/00216224:14740/15:00080833

Organizační jednotka

Středoevropský technologický institut

DOI

https://doi.org/10.1107/S1399004714026595

UT WoS

000351155400003

EID Scopus

2-s2.0-84924808307

Klíčová slova česky

Aspergillus fumigatus; lektin; SPR; komplex protein-sacharid; patogen

Klíčová slova anglicky

Aspergillus fumigatus; lectin; SPR; protein-saccharide complex; pathogen

Štítky

rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 4. 2016 16:02, Mgr. Eva Špillingová

Anotace

V originále

The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications.

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

LH13055, projekt VaV

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

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Multidisciplinární přístup k návrhu léčiv - Inhibice proteinů s návazností na sacharidy

286154, interní kód MU

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

Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity

Citovat

HOUSER, Josef; Jan KOMÁREK; Gianluca CIOCI; Annabelle VARROT; Anne IMBERTY a Michaela WIMMEROVÁ. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. HOBOKEN: WILEY-BLACKWELL, 2015, roč. 71, March, s. 442-453. ISSN 1399-0047. Dostupné z: https://doi.org/10.1107/S1399004714026595.

@article{1300635,
   author = {Houser, Josef and Komárek, Jan and Cioci, Gianluca and Varrot, Annabelle and Imberty, Anne and Wimmerová, Michaela},
   article_location = {HOBOKEN},
   article_number = {March},
   doi = {https://doi.org/10.1107/S1399004714026595},
   keywords = {Aspergillus fumigatus; lectin; SPR; protein-saccharide complex; pathogen},
   language = {eng},
   issn = {1399-0047},
   journal = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
   title = {Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent},
   url = {http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf},
   volume = {71},
   year = {2015}
}

TY  - JOUR
ID  - 1300635
AU  - Houser, Josef - Komárek, Jan - Cioci, Gianluca - Varrot, Annabelle - Imberty, Anne - Wimmerová, Michaela
PY  - 2015
TI  - Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
JF  - ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
VL  - 71
IS  - March
SP  - 442-453
EP  - 442-453
PB  - WILEY-BLACKWELL
SN  - 13990047
KW  - Aspergillus fumigatus
KW  - lectin
KW  - SPR
KW  - protein-saccharide complex
KW  - pathogen
UR  - http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf
L2  - http://journals.iucr.org/d/issues/2015/03/00/mh5137/mh5137.pdf
N2  - The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications.
ER  -

HOUSER, Josef; Jan KOMÁREK; Gianluca CIOCI; Annabelle VARROT; Anne IMBERTY a Michaela WIMMEROVÁ. Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent. \textit{ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY}. HOBOKEN: WILEY-BLACKWELL, 2015, roč.~71, March, s.~442-453. ISSN~1399-0047. Dostupné z: https://doi.org/10.1107/S1399004714026595.

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