Christopher B. T. Britt

A high C/O ratio and weak thermal inversion in the atmosphere of exoplanet WASP-12b

The carbon-to-oxygen ratio (C/O) in a planet provides critical information about its primordial origins and subsequent evolution. A primordial C/O greater than 0.8 causes a carbide-dominated interior, as opposed to the silicate-dominated composition found on Earth; the atmosphere can also differ from those in the Solar System. The solar C/O is 0.54 (ref. 3). Here we report an analysis of dayside multi-wavelength photometry of the transiting hot-Jupiter WASP-12b (ref. 6) that reveals C/Ou2009≥u20091 in its atmosphere. The atmosphere is abundant in CO. It is depleted in water vapour and enhanced in methane, each by more than two orders of magnitude compared to a solar-abundance chemical-equilibrium model at the expected temperatures. We also find that the extremely irradiated atmosphere (Tu2009>u20092,500u2009K) of WASP-12b lacks a prominent thermal inversion (or stratosphere) and has very efficient day–night energy circulation. The absence of a strong thermal inversion is in stark contrast to theoretical predictions for the most highly irradiated hot-Jupiter atmospheres.

On the Orbit of Exoplanet WASP-12b

We observed two secondary eclipses of the exoplanet WASP-12b using the Infrared Array Camera on the Spitzer Space Telescope. The close proximity of WASP-12b to its G-type star results in extreme tidal forces capable of inducing apsidal precession with a period as short as a few decades. This precession would be measurable if the orbit had a significant eccentricity, leading to an estimate of the tidal Love number and an assessment of the degree of central concentration in the planetary interior. An initial ground-based secondary-eclipse phase reported by Lopez-Morales et al. (0.510 ± 0.002) implied eccentricity at the 4.5σ level. The spectroscopic orbit of Hebb et al. has eccentricity 0.049 ± 0.015, a 3σ result, implying an eclipse phase of 0.509 ± 0.007. However, there is a well-documented tendency of spectroscopic data to overestimate small eccentricities. Our eclipse phases are 0.5010 ± 0.0006 (3.6 and 5.8 μm) and 0.5006 ± 0.0007 (4.5 and 8.0 μm). An unlikely orbital precession scenario invoking an alignment of the orbit during the Spitzer observations could have explained this apparent discrepancy, but the final eclipse phase of Lopez-Morales et al. (0.510 ±+0.007 –0.006) is consistent with a circular orbit at better than 2σ. An orbit fit to all the available transit, eclipse, and radial-velocity data indicates precession at <1σ; a non-precessing solution fits better. We also comment on analysis and reporting for Spitzer exoplanet data in light of recent re-analyses.

SPITZER SECONDARY ECLIPSES OF WASP-18b

The transiting exoplanet WASP-18b was discovered in 2008 by the Wide Angle Search for Planets project. The Spitzer Exoplanet Target of Opportunity Program observed secondary eclipses of WASP-18b using Spitzers Infrared Array Camera in the 3.6 ?m and 5.8 ?m bands on 2008 December 20, and in the 4.5 ?m and 8.0 ?m bands on 2008 December 24. We report eclipse depths of 0.30% ? 0.02%, 0.39% ? 0.02%, 0.37% ? 0.03%, 0.41% ? 0.02%, and brightness temperatures of 3100 ? 90, 3310 ? 130, 3080 ? 140, and 3120 ? 110?K in order of increasing wavelength. WASP-18b is one of the hottest planets yet discovered?as hot as an M-class star. The planets pressure-temperature profile most likely features a thermal inversion. The observations also require WASP-18b to have near-zero albedo and almost no redistribution of energy from the day side to the night side of the planet.

Inhibition of Cholera Toxin and Other AB Toxins by Polyphenolic Compounds.

Cholera toxin (CT) is an AB-type protein toxin that contains a catalytic A1 subunit, an A2 linker, and a cell-binding B homopentamer. The CT holotoxin is released into the extracellular environment, but CTA1 attacks a target within the cytosol of a host cell. We recently reported that grape extract confers substantial resistance to CT. Here, we used a cell culture system to identify twelve individual phenolic compounds from grape extract that inhibit CT. Additional studies determined the mechanism of inhibition for a subset of the compounds: two inhibited CT binding to the cell surface and even stripped CT from the plasma membrane of a target cell; two inhibited the enzymatic activity of CTA1; and four blocked cytosolic toxin activity without directly affecting the enzymatic function of CTA1. Individual polyphenolic compounds from grape extract could also generate cellular resistance to diphtheria toxin, exotoxin A, and ricin. We have thus identified individual toxin inhibitors from grape extract and some of their mechanisms of inhibition against CT.

Modulation of Cholera Toxin Structure/Function by Hsp90

Cholera toxin (CT) is released into the extracellular environment, but the catalytic CTA1 subunit attacks its G protein target within the cytosol of an intoxicated cell. To access the cytosol, CT moves by vesicle carriers from the cell surface to the endoplasmic reticulum (ER). CTA1 then dissociates from the rest of the toxin and shifts to a disordered conformation that facilitates its passage into the cytosol through a pore in the ER membrane. We have found that CTA1 export to the cytosol requires the host cytosolic chaperone Hsp90. Loss of Hsp90 function trapped CTA1 in the ER, and Hsp90 was sufficient for in vitro export of CTA1 from the ER. Structural studies demonstrated Hsp90 will refold disordered CTA1. ATP hydrolysis by Hsp90 was required for both CTA1 refolding and CTA1 extraction from the ER, which suggests a ratchet mechanism for the chaperone-driven movement of CTA1 to the cytosol: the refolding of CTA1 as it emerges at the cytosolic face of the ER membrane would prevent the toxin from sliding back into the translocon pore and would thereby ensure the unidirectional movement of CTA1 from the ER to the cytosol. Hsp90 bound to the N-terminus of CTA1 and did not release CTA1 after refolding the toxin. The continued association of Hsp90 with CTA1 allowed the toxin to maintain an active conformation at 37 °C. Hsp90 thus plays two key roles CT intoxication: it couples toxin refolding with toxin extraction from the ER, and it maintains the cytosolic toxin in a functional conformation.