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1.
Appl Opt ; 57(22): E64-E70, 2018 Aug 01.
Article in English | MEDLINE | ID: mdl-30117923

ABSTRACT

This paper discusses the potential for opening a new wavelength window at the 2 µm waveband for optical communications, showing current limitations of the system's performance. It focuses on novel results for key enabling technologies, including the analysis of laser injection locking at this waveband, an improved responsivity for bulk and strained InGaAs edge-couple detectors, and also an increased gain profile for thulium-doped fiber amplifiers.

2.
Opt Express ; 23(4): 4946-51, 2015 Feb 23.
Article in English | MEDLINE | ID: mdl-25836529

ABSTRACT

We show for the first time 100 Gbit/s total capacity at 2 µm waveband, using 4 × 9.3 Gbit/s 4-ASK Fast-OFDM direct modulation and 4 × 15.7 Gbit/s NRZ-OOK external modulation, spanning a 36.3 nm wide wavelength range. WDM transmission was successfully demonstrated over 1.15 km of low-loss hollow core photonic bandgap fiber (HC-PBGF) and over 1 km of solid core fiber (SCF). We conclude that the OSNR penalty associated with the SCF is minimal, while a ~1-2 dB penalty was observed after the HC-PBGF probably due to mode coupling to higher-order modes.

3.
Opt Lett ; 40(14): 3308-11, 2015 Jul 15.
Article in English | MEDLINE | ID: mdl-26176456

ABSTRACT

We show, for the first time, dense WDM (8×20 Gbit/s) transmission at 2 µm enabled by advanced modulation formats (4-ASK Fast-OFDM) and the development of key components, including a new arrayed waveguide grating (AWGr) at 2 µm. The AWGr shows -12.8±1.78 dB of excess loss with an 18-dB extinction ratio and a thermal tunability of 0.108 nm/°C.

4.
J Hosp Infect ; 151: 11-20, 2024 Sep.
Article in English | MEDLINE | ID: mdl-38944282

ABSTRACT

BACKGROUND: Vancomycin-resistant Enterococcus faecium (VREfm) are significant nosocomial pathogens. Sequence type (ST) 80 vanA-encoding VREfm predominate in Irish hospitals, but their transmission is poorly understood. AIMS: To investigate transmission and persistence of predominant complex type (CT) VREfm in two wards of an Irish hospital (H1) using whole-genome sequencing, and their intra- and inter-hospital dissemination. METHODS: Rectal screening (N = 330, September 2019 to December 2022) and environmental (N = 48, November 2022 to December 2022) E. faecium were investigated. Isolate relatedness was assessed by core-genome multi-locus sequence typing (cgMLST) and core-genome single nucleotide polymorphism (cgSNP) analysis. Likely transmission chains were identified using SeqTrack (https://graphsnp.fordelab.com/graphsnp) using cgSNP data and recovery location. Well-characterized E. faecium (N = 908) from seven Irish hospitals including H1 (June 2017 to July 2022) were also investigated. FINDINGS: Conventional MLST assigned isolates to nine STs (ST80, 82%). cgMLST identified three predominant ST80 CTs (CT2933, CT2932 and CT1916) (55% of isolates) of related isolates (≤20 allelic differences). cgSNP analysis differentiated these CTs into multiple distinct closely related genomic clusters (≤10 cgSNPs). Parisimonious network construction identified 55 likely inter- and intra-ward transmissions with epidemiological support between patients ≤30 days involving 73 isolates (≤10 cgSNPs) from seven genomic clusters. Numerous other likely transmissions over longer time periods without evident epidemiological links were identified, suggesting persistence and unidentified reservoirs contribute to dissemination. The three CTs predominated among E. faecium (N = 1286) in seven hospitals, highlighting inter-hospital spread without known epidemiological links. CONCLUSION: This study revealed the long-term intra- and inter-hospital dominance of three major CT ST80 VREfm lineages, widespread transmission and persistence, implicating unidentified reservoirs.


Subject(s)
Cross Infection , Enterococcus faecium , Gram-Positive Bacterial Infections , Hospitals , Vancomycin-Resistant Enterococci , Whole Genome Sequencing , Humans , Ireland/epidemiology , Enterococcus faecium/genetics , Enterococcus faecium/isolation & purification , Enterococcus faecium/drug effects , Enterococcus faecium/classification , Vancomycin-Resistant Enterococci/genetics , Vancomycin-Resistant Enterococci/isolation & purification , Vancomycin-Resistant Enterococci/classification , Gram-Positive Bacterial Infections/microbiology , Gram-Positive Bacterial Infections/transmission , Gram-Positive Bacterial Infections/epidemiology , Cross Infection/microbiology , Cross Infection/epidemiology , Cross Infection/transmission , Multilocus Sequence Typing , Polymorphism, Single Nucleotide , Genome, Bacterial , Genotype
5.
Biochim Biophys Acta ; 1457(1-2): 57-70, 2000 Feb 24.
Article in English | MEDLINE | ID: mdl-10692550

ABSTRACT

Activation of oxidative phosphorylation by physiological levels of calcium in mitochondria from rat skeletal muscle was analysed using top-down elasticity and regulation analysis. Oxidative phosphorylation was conceptually divided into three subsystems (substrate oxidation, proton leak and phosphorylation) connected by the membrane potential or the protonmotive force. Calcium directly activated the phosphorylation subsystem and (with sub-saturating 2-oxoglutarate) the substrate oxidation subsystem but had no effect on the proton leak kinetics. The response of mitochondria respiring on 2-oxoglutarate at two physiological concentrations of free calcium was quantified using control and regulation analysis. The partial integrated response coefficients showed that direct stimulation of substrate oxidation contributed 86% of the effect of calcium on state 3 oxygen consumption, and direct activation of the phosphorylation reactions caused 37% of the increase in phosphorylation flux. Calcium directly activated phosphorylation more strongly than substrate oxidation (78% compared to 45%) to achieve homeostasis of mitochondrial membrane potential during large increases in flux.


Subject(s)
Calcium/pharmacology , Mitochondria, Muscle/drug effects , Muscle, Skeletal/drug effects , Animals , Enzyme Activation/drug effects , Female , In Vitro Techniques , Ketoglutaric Acids/metabolism , Mitochondria, Muscle/metabolism , Muscle, Skeletal/metabolism , Oxidative Phosphorylation/drug effects , Oxygen Consumption , Rats , Rats, Wistar , Succinic Acid/metabolism
6.
Microbes Infect ; 17(6): 395-401, 2015 Jun.
Article in English | MEDLINE | ID: mdl-25749709

ABSTRACT

Staphylococcus epidermidis is the leading etiologic agent of orthopaedic implant infection. Contamination of the implanted device during insertion allows bacteria gain entry into the sterile bone environment leading to condition known as osteomyelitis. Osteomyelitis is characterised by weakened bones associated with progressive bone loss. The mechanism through which S. epidermidis interacts with bone cells to cause osteomyelitis is poorly understood. We demonstrate here that S. epidermidis can bind to osteoblasts in the absence of matrix proteins. S. epidermidis strains lacking the cell wall protein SdrG had a significantly reduced ability to bind to osteoblasts. Consistent with this, expression of SdrG in Lactococcus lactis resulted in significantly increased binding to the osteoblasts. Protein analysis identified that SdrG contains a potential integrin recognition motif. αVß3 is a major integrin expressed on osteoblasts and typically recognises RGD motifs in its ligands. Our results demonstrate that S. epidermidis binds to recombinant purified αVß3, and that a mutant lacking SdrG failed to bind. Blocking αVß3 on osteoblasts significantly reduced binding to S. epidermidis. These studies are the first to identify a mechanism through which S. epidermidis binds to osteoblasts and potentially offers a mechanism through which implant infection caused by S. epidermidis leads to osteomyelitis.


Subject(s)
Bacterial Proteins/metabolism , Carrier Proteins/metabolism , Integrin alphaVbeta3/metabolism , Osteoblasts/metabolism , Staphylococcus epidermidis/growth & development , Carrier Proteins/immunology , Humans , Osteomyelitis/etiology , Osteomyelitis/immunology , Osteomyelitis/therapy , Protein Binding/immunology , Serine/antagonists & inhibitors , Serine/immunology , Staphylococcus epidermidis/immunology
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