An Improved Interactive Streaming Algorithm for the Distinct Elements Problem

The exact computation of the number of distinct elements (frequency moment $F_0$) is a fundamental problem in the study of data streaming algorithms. We denote the length of the stream by $n$ where each symbol is drawn from a universe of size $m$. While it is well known that the moments $F_0,F_1,F_2$ can be approximated by efficient streaming algorithms, it is easy to see that exact computation of $F_0,F_2$ requires space $\Omega(m)$. In previous work, Cormode et al. therefore considered a model where the data stream is also processed by a powerful helper, who provides an interactive proof of the result. They gave such protocols with a polylogarithmic number of rounds of communication between helper and verifier for all functions in NC. This number of rounds $\left(O(\log^2 m) \;\text{in the case of} \;F_0 \right)$ can quickly make such protocols impractical. Cormode et al. also gave a protocol with $\log m +1$ rounds for the exact computation of $F_0$ where the space complexity is $O\left(\log m \log n+\log^2 m\right)$ but the total communication $O\left(\sqrt{n}\log m\left(\log n+ \log m \right)\right)$. They managed to give $\log m$ round protocols with $\operatorname{polylog}(m,n)$ complexity for many other interesting problems including $F_2$, Inner product, and Range-sum, but computing $F_0$ exactly with polylogarithmic space and communication and $O(\log m)$ rounds remained open. In this work, we give a streaming interactive protocol with $\log m$ rounds for exact computation of $F_0$ using $O\left(\log m \left(\,\log n + \log m \log\log m\,\right)\right)$ bits of space and the communication is $O\left( \log m \left(\,\log n +\log^3 m (\log\log m)^2 \,\right)\right)$. The update time of the verifier per symbol received is $O(\log^2 m)$.Comment: Submitted to ICALP 201

EPIC 219217635: A Doubly Eclipsing Quadruple System Containing an Evolved Binary

We have discovered a doubly eclipsing, bound, quadruple star system in the field of K2 Campaign 7. EPIC 219217635 is a stellar image with $Kp = 12.7$ that contains an eclipsing binary (`EB') with $P_A = 3.59470$ d and a second EB with $P_B = 0.61825$ d. We have obtained followup radial-velocity (`RV') spectroscopy observations, adaptive optics imaging, as well as ground-based photometric observations. From our analysis of all the observations, we derive good estimates for a number of the system parameters. We conclude that (1) both binaries are bound in a quadruple star system; (2) a linear trend to the RV curve of binary A is found over a 2-year interval, corresponding to an acceleration, $\dot \gamma = 0.0024 \pm 0.0007$ cm s$^{-2}$; (3) small irregular variations are seen in the eclipse-timing variations (`ETVs') detected over the same interval; (4) the orbital separation of the quadruple system is probably in the range of 8-25 AU; and (5) the orbital planes of the two binaries must be inclined with respect to each other by at least 25$^\circ$. In addition, we find that binary B is evolved, and the cooler and currently less massive star has transferred much of its envelope to the currently more massive star. We have also demonstrated that the system is sufficiently bright that the eclipses can be followed using small ground-based telescopes, and that this system may be profitably studied over the next decade when the outer orbit of the quadruple is expected to manifest itself in the ETV and/or RV curves.Comment: Accepted for publication in MNRA

The optimization and validation of the Biotyper MALDI-TOF MS database for the identification of Gram-positive anaerobic cocci

OBJECTIVES: Gram-positive anaerobic cocci (GPAC) account for 24-31% of the anaerobic bacteria isolated from human clinical specimens. At present GPAC are underrepresented in the Biotyper MALDI-TOF MS database. Profiles of new species have yet to be added. We present the optimization of the MALDI-TOF MS database for the identification of GPAC. METHODS: Main Spectral Profiles (MSPs) were created for 108 clinical GPAC isolates. Identity was confirmed using 16S rRNA gene sequencing. Species identification was considered to be reliable if the sequence similarity with its closest relative was ≥98.7%. The optimized database was validated using 140 clinical isolates. The 16S rRNA sequencing identity was compared with the MALDI-TOF MS result. RESULTS: MSPs were added from 17 species that were not yet represented in the MALDI-TOF MS database or were underrepresented (<5 MSPs). This resulted in an increase from 53.6% (75/140) to 82.1% (115/140) of GPAC isolates that could be identified at the species level using MALDI-TOF MS. An improved log score was obtained for 51.4% (72/140) of the strains. For strains with a sequence similarity <98.7% with their closest relative (n=5) or with an inconclusive sequence identity (n=4), no identification was obtained by MALDI-TOF MS or in the latter case an identity with one of its relatives. CONCLUSIONS: For some species the MSP of the type strain was not a part of the confined cluster of the corresponding clinical isolates. Also, not all species formed a homogeneous cluster. It emphasizes the necessity of adding sufficient MSPs of human clinical isolates

HLA Class I Binding 9mer Peptides from Influenza A Virus Induce CD4+ T Cell Responses

BACKGROUND: Identification of human leukocyte antigen class I (HLA-I) restricted cytotoxic T cell (CTL) epitopes from influenza virus is of importance for the development of new effective peptide-based vaccines. METHODOLOGY/PRINCIPAL FINDINGS: In the present work, bioinformatics was used to predict 9mer peptides derived from available influenza A viral proteins with binding affinity for at least one of the 12 HLA-I supertypes. The predicted peptides were then selected in a way that ensured maximal coverage of the available influenza A strains. One hundred and thirty one peptides were synthesized and their binding affinities for the HLA-I supertypes were measured in a biochemical assay. Influenza-specific T cell responses towards the peptides were quantified using IFNgamma ELISPOT assays with peripheral blood mononuclear cells (PBMC) from adult healthy HLA-I typed donors as responder cells. Of the 131 peptides, 21 were found to induce T cell responses in 19 donors. In the ELISPOT assay, five peptides induced responses that could be totally blocked by the pan-specific anti-HLA-I antibody W6/32, whereas 15 peptides induced responses that could be completely blocked in the presence of the pan-specific anti-HLA class II (HLA-II) antibody IVA12. Blocking of HLA-II subtype reactivity revealed that 8 and 6 peptide responses were blocked by anti-HLA-DR and -DP antibodies, respectively. Peptide reactivity of PBMC depleted of CD4(+) or CD8(+) T cells prior to the ELISPOT culture revealed that effectors are either CD4(+) (the majority of reactivities) or CD8(+) T cells, never a mixture of these subsets. Three of the peptides, recognized by CD4(+) T cells showed binding to recombinant DRA1*0101/DRB1*0401 or DRA1*0101/DRB5*0101 molecules in a recently developed biochemical assay. CONCLUSIONS/SIGNIFICANCE: HLA-I binding 9mer influenza virus-derived peptides induce in many cases CD4(+) T cell responses restricted by HLA-II molecules