48 research outputs found
A Hard X-Ray View of Two Distant VHE Blazars: 1ES 1101-232 and 1ES 1553+113
TeV blazars are known as prominent nonthermal emitters across the entire
electromagnetic spectrum with their photon power peaking in the X-ray and TeV
bands. If distant, absorption of gamma-ray photons by the extragalactic
background light (EBL) alters the intrinsic TeV spectral shape, thereby
affecting the overall interpretation. Suzaku observations for two of the more
distant TeV blazars known to date, 1ES 1101-232 and 1ES 1553+113, were carried
out in 2006 May and July, respectively, including a quasi-simultaneous coverage
with the state-of-the-art Cerenkov telescope facilities. We report on the
resulting data sets with emphasis on the X-ray band and set in context to their
historical behavior. During our campaign, we did not detect any significant
X-ray or gamma-ray variability. 1ES 1101-232 was found in a quiescent state
with the lowest X-ray flux ever measured. The combined XIS and HXD PIN data for
1ES 1101-232 and 1ES 1553+113 clearly indicate spectral curvature up to the
highest hard X-ray data point (~30 keV), manifesting as softening with
increasing energy. We describe this spectral shape by either a broken power law
or a log-parabolic fit with equal statistical goodness of fits. The combined
1ES 1553+113 very high energy spectrum (90-500 GeV) did not show any
significant changes with respect to earlier observations. The resulting
contemporaneous broadband spectral energy distributions of both TeV blazars are
discussed in view of implications for intrinsic blazar parameter values, taking
into account the gamma-ray absorption in the EBL.Comment: 9 pages, 10 figure
A Soluble Form of the High Affinity IgE Receptor, Fc-Epsilon-RI, Circulates in Human Serum
Soluble IgE receptors are potential in vivo modulators of
IgE-mediated immune responses and are thus important for our basic understanding
of allergic responses. We here characterize a novel soluble version of the
IgE-binding alpha-chain of Fc-epsilon-RI (sFcεRI), the high affinity
receptor for IgE. sFcεRI immunoprecipitates as a protein of ∼40 kDa and
contains an intact IgE-binding site. In human serum, sFcεRI is found as a
soluble free IgE receptor as well as a complex with IgE. Using a newly
established ELISA, we show that serum sFcεRI levels correlate with serum IgE
in patients with elevated IgE. We also show that serum of individuals with
normal IgE levels can be found to contain high levels of sFcεRI. After
IgE-antigen-mediated crosslinking of surface FcεRI, we detect sFcεRI in
the exosome-depleted, soluble fraction of cell culture supernatants. We further
show that sFcεRI can block binding of IgE to FcεRI expressed at the cell
surface. In summary, we here describe the alpha-chain of FcεRI as a
circulating soluble IgE receptor isoform in human serum
IgE binds asymmetrically to its B cell receptor CD23.
The antibody IgE plays a central role in allergic disease mechanisms. Its effector functions are controlled through interactions between the Fc region and two principal cell surface receptors FcεRI and CD23. The interaction with FcεRI is primarily responsible for allergic sensitization and the inflammatory response, while IgE binding to CD23 is involved in the regulation of IgE synthesis and allergen transcytosis. Here we present the crystal structure of a CD23/IgE-Fc complex and conduct isothermal titration calorimetric binding studies. Two lectin-like "head" domains of CD23 bind to IgE-Fc with affinities that differ by more than an order of magnitude, but the crystal structure reveals only one head bound to one of the two identical heavy-chains in the asymmetrically bent IgE-Fc. These results highlight the subtle interplay between receptor binding sites in IgE-Fc and their affinities, the understanding of which may be exploited for therapeutic intervention in allergic disease
Diversity of methicillin-resistant staphylococcus aureus strains isolated from residents of 26 nursing homes in orange county, california
Nursing homes represent a unique and important methicillin-resistant Staphylococcus aureus (MRSA) reservoir. Not only are strains imported from hospitals and the community, strains can be transported back into these settings from nursing homes. Since MRSA bacteria are prevalent in nursing homes and yet relatively poorly studied in this setting, a multicenter, regional assessment of the frequency and diversity of MRSA in the nursing home reservoir was carried out and compared to that of the MRSA from hospitals in the same region. The prospective study collected MRSA from nasal swabbing of residents of 26 nursing homes in Orange County, California, and characterized each isolate by spa typing. A total of 837 MRSA isolates were collected from the nursing homes. Estimates of admission prevalence and point prevalence of MRSA were 16% and 26%, respectively. The spa type genetic diversity was heterogeneous between nursing homes and significantly higher overall (77%) than the diversity in Orange County hospitals (72%). MRSA burden in nursing homes appears largely due to importation from hospitals. As seen in Orange County hospitals, USA300 (sequence type 8 [ST8]/t008), USA100 (ST5/t002), and a USA100 variant (ST5/t242) were the dominant MRSA clones in Orange County nursing homes, representing 83% of all isolates, although the USA100 variant was predominant in nursing homes, whereas USA300 was predominant in hospitals. Control strategies tailored to the complex problem of MRSA transmission and infection in nursing homes are needed in order to minimize the impact of this unique reservoir on the overall regional MRSA burden. Copyright © 2013, American Society for Microbiology. All Rights Reserved