TY  - JOUR
AU  - Lázár, Viktória
AU  - Martins, Ana
AU  - Spohn, Réka
AU  - Daruka, Lejla
AU  - Grézal, Gábor
AU  - Fekete, Gergely
AU  - Számel, Mónika
AU  - Jangir, Pramod Kumar
AU  - Kintses, Bálint
AU  - Csörgő, Bálint
AU  - Nyerges, Ákos
AU  - Györkei, Ádám
AU  - Kincses, András
AU  - Dér, András
AU  - Walter, Fruzsina
AU  - Deli, Mária Anna
AU  - Zsoldiné Urbán, Edit
AU  - Hegedüs, Zsófia
AU  - Olajos, Gábor
AU  - Méhi, Orsolya Katinka
AU  - Bálint, Balázs
AU  - Nagy, István
AU  - Martinek, Tamás
AU  - Papp, Balázs
AU  - Pál, Csaba
TI  - Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides
JF  - NATURE MICROBIOLOGY
J2  - NAT MICROBIOL
VL  - 3
PY  - 2018
IS  - 6
SP  - 718
EP  - 731
PG  - 14
SN  - 2058-5276
DO  - 10.1038/s41564-018-0164-0
UR  - https://m2.mtmt.hu/api/publication/3378998
ID  - 3378998
N1  - Megosztott első szerzőség. These authors contributed equally to this work: Viktória Lázár and Ana Martins.
AB  - Antimicrobial peptides are promising alternative antimicrobial agents. However, little is known about whether resistance to small-molecule antibiotics leads to cross-resistance (decreased sensitivity) or collateral sensitivity (increased sensitivity) to antimicrobial peptides. We systematically addressed this question by studying the susceptibilities of a comprehensive set of 60 antibiotic-resistant Escherichia coli strains towards 24 antimicrobial peptides. Strikingly, antibiotic-resistant bacteria show a high frequency of collateral sensitivity to antimicrobial peptides, whereas cross-resistance is relatively rare. We identify clinically relevant multidrug-resistance mutations that increase bacterial sensitivity to antimicrobial peptides. Collateral sensitivity in multidrug-resistant bacteria arises partly through regulatory changes shaping the lipopolysaccharide composition of the bacterial outer membrane. These advances allow the identification of antimicrobial peptide-antibiotic combinations that enhance antibiotic activity against multidrug-resistant bacteria and slow down de novo evolution of resistance. In particular, when co-administered as an adjuvant, the antimicrobial peptide glycine-leucine-amide caused up to 30-fold decrease in the antibiotic resistance level of resistant bacteria. Our work provides guidelines for the development of efficient peptide-based therapies of antibiotic-resistant infections.
LA  - English
DB  - MTMT
ER  - 

TY  - JOUR
AU  - Szabados, László
AU  - Savoure, A
TI  - Proline: a multifunctional amino acid
JF  - TRENDS IN PLANT SCIENCE
J2  - TRENDS PLANT SCI
VL  - 15
PY  - 2010
IS  - 2
SP  - 89
EP  - 97
PG  - 9
SN  - 1360-1385
DO  - 10.1016/j.tplants.2009.11.009
UR  - https://m2.mtmt.hu/api/publication/1920999
ID  - 1920999
N1  - Megjegyzés-21565663
DI: 10.1016/j.tplants.2009.11.009
Megjegyzés-22128219
DI: 10.1016/j.tplants.2009.11.009
Megjegyzés-22183017
DI: 10.1016/j.tplants.2009.11.009
Megjegyzés-22184024
DI: 10.1016/j.tplants.2009.11.009
AB  - Proline accumulates in many plant species in response to environmental stress. Although much is now known about proline metabolism, some aspects of its biological functions are still unclear. Here, we discuss the compartmentalization of proline biosynthesis, accumulation and degradation in the cytosol, chloroplast and mitochondria. We also describe the role of proline in cellular homeostasis, including redox balance and energy status. Proline can act as a signaling molecule to modulate mitochondrial functions, influence cell proliferation or cell death and trigger specific gene expression, which can be essential for plant recovery from stress. Although the regulation and function of proline accumulation are not yet completely understood, the engineering of proline metabolism could lead to new opportunities to improve plant tolerance of environmental stresses.
LA  - English
DB  - MTMT
ER  -