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001-es BibID:BIBFORM079276
035-os BibID:(cikkazonosító)355
Első szerző:Fu, Tse-Kai (vegyész)
Cím:Rhamnose Binding Protein as an Anti-Bacterial Agent-Targeting Biofilm of Pseudomonas aeruginosa / Tse-Kai Fu, Sim-Kun Ng, Yi-En Chen, Yuan-Chuan Lee, Fruzsina Demeter, Mihály Herczeg, Anikó Borbás, Cheng-Hsun Chiu, Chung-Yu Lan, Chyi-Liang Chen, Margaret Dah-Tsyr Chang
Dátum:2019
ISSN:1660-3397 1660-3397
Megjegyzések:More than 80% of infectious bacteria form biofilm, which is a bacterial cell community surrounded by secreted polysaccharides, proteins and glycolipids. Such bacterial superstructure increases resistance to antimicrobials and host defenses. Thus, to control these biofilm-forming pathogenic bacteria requires antimicrobial agents with novel mechanisms or properties. Pseudomonas aeruginosa, a Gram-negative opportunistic nosocomial pathogen, is a model strain to study biofilm development and correlation between biofilm formation and infection. In this study, a recombinant hemolymph plasma lectin (rHPLOE) cloned from Taiwanese Tachypleus tridentatus was expressed in an Escherichia coli system. This rHPLOE was shown to have the following properties: (1) Binding to P. aeruginosa PA14 biofilm through a unique molecular interaction with rhamnose-containing moieties on bacteria, leading to reduction of extracellular di-rhamnolipid (a biofilm regulator); (2) decreasing downstream quorum sensing factors, and inhibiting biofilm formation; (3) dispersing the mature biofilm of P. aeruginosa PA14 to improve the e cacies of antibiotics; (4) reducing P. aeruginosa PA14 cytotoxicity to human lung epithelial cells in vitro and (5) inhibiting P. aeruginosa PA14 infection of zebrafish embryos in vivo. Taken together, rHPLOE serves as an anti-biofilm agent with a novel mechanism of recognizing rhamnose moieties in lipopolysaccharides, di-rhamnolipid and structural polysaccharides (Psl) in biofilms. Thus rHPLOE links glycan-recognition to novel anti-biofilm strategies against pathogenic bacteria.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
rhamnose-binding protein
anti-biofilm
quorum sensing factor
anti-infection
Megjelenés:Marine Drugs. - 17 : 6 (2019), p. 1-19. -
További szerzők:Ng, Sim-Kun (1980-) (vegyész) Chen, Yi-En (1980-) (vegyész) Lee, Yuan-Chuan (1932-) (biokémikus) Demeter Fruzsina (1991-) (okleveles vegyész) Herczeg Mihály (1979-) (vegyész, biológia-kémia tanár) Borbás Anikó (1965-) (vegyész) Chiu, Cheng-Hsun (1975-) (vegyész) Lan, Chung-Yu (1980-) (vegyész) Chen, Chyi-Liang (1974-) (vegyész) Dah-Tsyr Chang, Margaret (1956-) (vegyész)
Pályázati támogatás:GINOP-2.3.2-15-2016-00008
GINOP
ÚNKP-18-3 New National Excellence Program of the Ministry of Human Capacities of Hungary
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001-es BibID:BIBFORM066145
Első szerző:Herczeg Mihály (vegyész, biológia-kémia tanár)
Cím:Inhibitory Effect of Multivalent Rhamnobiosides on Recombinant Horseshoe Crab Plasma Lectin Interactions with PAO1 / Herczeg Mihály, Mező Erika, Molnár Nikolett, Ng Sim-Kun, Lee Yuan-Chuan, Dah-Tsyr Chang Margaret, Borbás Anikó
Dátum:2016
ISSN:1861-4728
Megjegyzések:To evaluate the molecular interaction of recombi-nant horseshoe crab plasma lectin (rHPL) withPseudomonasaeruginosaPAO1, multivalent rhamnobioside derivativeswere designed. Eight rhamnoclusters with three or foura(1?3)-rhamnobiosides attached to different central cores, suchas methyl gallate, pentaerythritol, andN-Boc Tris, througheither an ethylene glycol or a tetraethylene glycol linker,were assembled in two consecutive azide?alkyne cycloaddi-tion click reactions. The synthetic method embraced thepreparation of twoa(1?3)-rhamnobiosides with differentlinker arms and their conjugation, in stoichiometric or sub-stoichiometric amounts, to propargyl ether-functionalizedtri- or tetravalent scaffolds. A divalent derivative and twoself-assembling rhamnobiosides were also prepared. The dif-ferent architectures and valences of the rhamnoclusters pro-vided an opportunity to evaluate the impact of topologyand valency on the binding properties toward rHPL. Inhibito-ry ELISA data showed that all covalently linked rhamnoclus-ters could inhibitP. aeruginosaPAO1 recognition activity ofrHPL with high efficacy. Trivalent rhamnobiosides showeda stronger inhibitory effect onP. aeruginosaPAO1 binding,and the more flexible clusters on a pentaerythritol or a Triscore were superior to the less flexible methyl gallate-basedclusters. Interestingly, the length of the linker arms hada very low impact on the binding ability of the rhamnoclus-ters. Herein, the two trivalent derivatives on anN-Boc pro-tected Tris central core were the best inhibitors. The self-as-sembling amphiphilic rhamnobioside derivatives were foundto display no multivalent effect.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
carbohydrates
click chemistry
inhibitors
lectin
multivalency
Megjelenés:Chemistry - An Asian Journal 11 : 23 (2016), p. 3398-3413. -
További szerzők:Mező Erika (1986-) (vegyész) Molnár Nikolett (1992-) (gyógyszerész) Ng, Sim-Kun (1980-) (vegyész) Lee, Yuan-Chuan (1932-) (biokémikus) Dah-Tsyr Chang, Margaret (1956-) (vegyész) Borbás Anikó (1965-) (vegyész)
Pályázati támogatás:K109208
OTKA
PD115645
OTKA
Ministry of Science and Technology MOST 105-2627M-007-003 to M.D.-T.C.)
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