The worldwide SARS-CoV-2 outbreak poses a serious challenge to human societies and economies. SARS-CoV-2 proteins orchestrate complex pathogenic mechanisms that underlie COVID-19 disease. Thus, understanding how viral polypeptides rewire host protein networks enables better-founded therapeutic research. In complement to existing proteomic studies, in this study we define the first proximal interaction network of SARS-CoV-2 proteins, at the whole proteome level in human cells. Applying a proximity-dependent biotinylation (BioID)-based approach greatly expanded the current knowledge by detecting interactions within poorly soluble compartments, transient, and/or of weak affinity in living cells. Our BioID study was complemented by a stringent filtering and uncovered 2,128 unique cellular targets (1,717 not previously associated with SARS-CoV-1 or 2 proteins) connected to the N- and C-ter BioID-tagged 28 SARS-CoV-2 proteins by a total of 5,415 (5,236 new) proximal interactions. In order to facilitate data exploitation, an innovative interactive 3D web interface was developed to allow customized analysis and exploration of the landscape of interactions (accessible at http://www.sars-cov-2-interactome.org/). Interestingly, 342 membrane proteins including interferon and interleukin pathways factors, were associated with specific viral proteins. We uncovered ORF7a and ORF7b protein proximal partners that could be related to anosmia and ageusia symptoms. Moreover, comparing proximal interactomes in basal and infection-mimicking conditions (poly(I:C) treatment) allowed us to detect novel links with major antiviral response pathway components, such as ORF9b with MAVS and ISG20; N with PKR and TARB2; NSP2 with RIG-I and STAT1; NSP16 with PARP9-DTX3L. Altogether, our study provides an unprecedented comprehensive resource for understanding how SARS-CoV-2 proteins orchestrate host proteome remodeling and innate immune response evasion, which can inform development of targeted therapeutic strategies.

We compute the one-loop QCD amplitudes for the processes HqqQQ and Hqqgg, the latter restricted to the case of opposite-helicity gluons. Analytic expressions are presented for the color-and helicity-decomposed amplitudes. The coupling of the Higgs boson to gluons is treated by an effective interaction in the limit of large top quark mass. The Higgs field is split into a complex field φ and its complex conjugate φ † . The split is useful because amplitudes involving φ have different analytic structure from those involving φ † . We compute the cut-containing pieces of the amplitudes using generalized unitarity. The remaining rational parts are obtained by on-shell recursion. Our results for HqqQQ agree with previous semi-numerical computations. We also show how to convert existing semi-numerical results for the production of a scalar Higgs boson into analogous results for a pseudoscalar Higgs boson.

We study the effect of interference between the standard model Higgs boson resonance and the continuum background in the process ! H ! b " b at a photon collider. Taking into account virtual gluon exchange between the final-state quarks, we calculate the leading corrections to the height of the resonance for the case of a light (m H < 160 GeV) Higgs boson. We find that the interference is destructive and around 0.1%-0.2% of the peak height, depending on the mass of the Higgs and the scattering angle. This suppression is smaller by an order of magnitude than the anticipated experimental accuracy at a photon collider. However, the fractional suppression can be significantly larger if the Higgs coupling to b quarks is increased by physics beyond the standard model. The standard model of particle physics (SM) has been very successful in describing a wide range of elementary particle phenomena to high accuracy. A key ingredient of the model is the scalar Higgs field, responsible for electroweak symmetry breaking and for generating the masses of essentially all massive elementary particles [1-3]. Similar fields exist in extensions of the SM, such as the minimal supersymmetric standard model (MSSM). In the SM, the Higgs boson is the only particle that remains undiscovered, and its properties are determined by its mass. It is a main goal of current and future high energy physics experiments to identify the Higgs boson and explore the details of the Higgs sector. In particular, the discovery of the Higgs boson could take place at run II of the Tevatron at Fermilab; if not there, then at the Large Hadron Collider (LHC) at CERN. Precise measurements of its properties will be one of the tasks of the proposed International Linear Collider (ILC). There is an option to use the ILC as a photon collider, by backscattering laser light off of the high energy electron beams. The high energy, highly polarized photons produced in this way can be used to study the various Higgs couplings to very high accuracy [4][5][6][7][8][9].The mass of the Higgs boson in the SM and MSSM has already been constrained by experiment to a range well within the reach of the aforementioned designed machines. Precision electroweak measurements have put an upper bound on the allowed values for its mass, m H & 170 GeV at 95% confidence level in the SM [10,11]. In the MSSM the Higgs boson mass obeys the bound m H m Z at tree level; radiative corrections increase this limit to about 135 GeV [12][13][14]. The mass of the Higgs boson has also been bounded from below via the Higgs-strahlung process e þ e À ! HZ at LEP2, with m H * 114:1 GeV in the SM and m H * 91:0 GeV in the MSSM [15][16][17][18][19][20].At a photon collider, among the two possible modes, and e, the former is especially useful for Higgs physics. For m H < 140 GeV, the most important channel involves Higgs production via photon fusion, ! H, followed by the decay H ! b " b [21,22]. The advantage of this channel is that the amplitude for the continuum ! b " b background to the Higgs signal is suppr...

Towards a three-dimensional mapping of virus-host proximal protein interactions The SARS-CoV-2 proximal interactome project sets out to build a comprehensive, three-dimensional map of protein virus-host protein interactions inside living human cells. It aims to shed light on unknown mechanisms of infection. It is made possible by a combination of advanced interactomics techniques coupled with algorithms for the 3D visualisation of networks.