Spaces of Holomorphic Immersions of Open Riemann Surfaces into the Complex Plane

Let M be an open Riemann surface. A recent result due to Forstneriˇc and L´arusson [8] says that, for a closed conical subvariety A ⇢ Cn such that A \ {0} is an Oka manifold, the weak homotopy type of the space of non-degenerate holomorphic A-immersions of M into Cn is the same as that of the space of holomorphic (or equivalently, continuous) maps from M into A\{0}. In their paper, the authors sketch the proof of this theoremthrough claiming analogy with a related result, and invoking advanced results from complex and di↵erential geometry, including seminal theorems from Oka theory. The work contained in this thesis was motivated by the absence of a self-contained proof for the special case where A = C – as, perhaps, the first geometrically interesting case that one would consider. We remedy the absence by providing a fully detailed, self-contained proof of this case; namely, the parametric h-principle for holomorphic immersions of open Riemann surfaces into C. We outline this more precisely as follows. Take a holomorphic 1-form ✓ on M which vanishes nowhere. We denote by I(M,C) the space of holomorphic immersions of M into C, and denote by O(M,C⇤) the space of nonvanishing holomorphic functions on M. We prove, in all detail, that the continuous map I(M,C)!O(M,C⇤), f 7! df /✓, is a weak homotopy equivalence. This gives a full description of the weak homotopy type of I(M,C), as the target space O(M,C⇤) is known by algebraic topology (Remark 5.2.3).Thesis (MPhil) -- University of Adelaide, School of Mathematical Sciences, 202

The interaction between NS1B protein of influenza B virus and the ubiquitin-like modifier ISG15 : insights into a unique species specific property of the virus

textInfluenza B virus causes a respiratory disease in people with a compromised immune system. The NS1B protein of influenza B virus is essential for virus growth and plays a crucial role in inhibiting the anti-viral responses mounted by the infected host cell. The N terminal 104 amino acids of NS1B bind a cellular protein called ISG15. ISG15 is an interferon induced 'ubiquitin-like' protein, and upon interferon induction, is conjugated to hundreds of targets. It has been found that both ISG15 and its conjugation inhibit many viruses. The focus of the current study was to characterize the interaction between NS1B and ISG15. Study of a recombinant influenza B virus which encoded a mutant NS1B protein that is unable to bind ISG15 revealed that ISG15 is mis-localized in cells infected with wild type but not the mutant influenza B virus. Further, such a mutant virus is attenuated in growth as compared to wild type virus in human cell lines but is not attenuated in canine cell lines. This result led to the discovery of the species specific nature of the interaction between NS1B and ISG15. Specifically, NS1B was found to bind ISG15 homologs from human and old world monkeys like Rhesus macaques and African green monkeys but not those from mouse or canines. These findings were extended by identifying the hinge between the N and C terminal domains of ISG15 as one of the major determinants of species specificity. These results highlight the importance of using human or primate cell culture models to study the effect of ISG15 on influenza B virus, and raises new possibilities on differences in the function of the ISG15 system in different species.Microbiolog

(2005-2006) Assembly Resolution 26: ln support of students at The University of Texas at Austin who are seeking a meeting with the President of The University of Texas at Austin to write a letter to Dow Chemical Company to address its responsibility towards the Bhopal disaster and ask Dow Chemical Company to spend matching funds for the environmental clean-up in Bhopal

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