Historicising the Birangona: Interrogating the Politics of Commemorating the Wartime Rape of 1971 in the context of the 50th Anniversary of Bangladesh

Two decades ago, ‘1971’ was deemed to not have a market within Indian publishing houses and media outlets. Yet, one is struck by the contemporary Indian focus on the iconic figure of the Birangona – brave women, a title given by the State of Bangladesh to women raped by the Pakistani army and their Bengali and non-Bengali collaborators during the Bangladesh war of 1971. It is important to engage with the public memory of wartime sexual violence of 1971 beyond the horrific constructions of the Birangona and the potential for propaganda and geopolitical calculations that the narrative engenders for India

Graphic Ethnography and Generative Resilience of Sexual Violence in Conflict of the Birangonas (War-heroines) in Bangladesh

The use of rape was common during the 1971 war in Bangladesh. Six days after the war ended, the new government publicly declared that any woman raped in the war was a birangona or ‘war heroine’. There exists a public memory of wartime rape through various literary, visual and testimonial forms, ensuring that the raped woman endures as an iconic figure. However, women’s experiences of wartime sexual violence are often explained through the limited lenses of silence, voice, shame, honour, gender, patriarchy, stigma, trauma and ostracisation, which help to create the figure of the horrific raped woman – meaning that birangonas are often assumed to have a horrific life trajectory. This can undermine the very resilience that characterises many of the women who were raped. In contrast, this chapter focuses on generative resilience, as offering a different narrative of sexual violence that emphasises women’s abilities to continue to live with and pass on the experiences of sexual violence in ways that are uniquely relational. It is this contextualised and social ecological understanding of resilience that needs to inform adaptive peacebuilding, in order to foster a nuanced understanding of the effects of rape as a weapon of war

Complexity of Strong Implementability

We consider the question of implementability of a social choice function in a classical setting where the preferences of finitely many selfish individuals with private information have to be aggregated towards a social choice. This is one of the central questions in mechanism design. If the concept of weak implementation is considered, the Revelation Principle states that one can restrict attention to truthful implementations and direct revelation mechanisms, which implies that implementability of a social choice function is easy to check. For the concept of strong implementation, however, the Revelation Principle becomes invalid, and the complexity of deciding whether a given social choice function is strongly implementable has been open so far. In this paper, we show by using methods from polyhedral theory that strong implementability of a social choice function can be decided in polynomial space and that each of the payments needed for strong implementation can always be chosen to be of polynomial encoding length. Moreover, we show that strong implementability of a social choice function involving only a single selfish individual can be decided in polynomial time via linear programming

Side Chain Hydrophobicity Modulates Therapeutic Activity and Membrane Selectivity of Antimicrobial Peptide Mastoparan-X

The discovery of new anti-infective compounds is stagnating and multi-resistant bacteria continue to emerge, threatening to end the "antibiotic era". Antimicrobial peptides (AMPs) and lipo-peptides such as daptomycin offer themselves as a new potential class of antibiotics; however, further optimization is needed if AMPs are to find broad use as antibiotics. In the present work, eight analogues of mastoparan-X (MPX) were investigated, having side chain modifications in position 1, 8 and 14 to modulate peptide hydrophobicity. The self-association properties of the peptides were characterized, and the peptide-membrane interactions in model membranes were compared with the bactericidal and haemolytic properties. Alanine substitution at position 1 and 14 resulted in higher target selectivity (red blood cells versus bacteria), but also decreased bactericidal potency. For these analogues, the gain in target selectivity correlated to biophysical parameters showing an increased effective charge and reduction in the partitioning coefficient for membrane insertion. Introduction of an unnatural amino acid, with an octyl side chain by amino acid substitution, at positions 1, 8 and 14 resulted in increased bactericidal potency at the expense of radically reduced membrane target selectivity. Overall, optimized membrane selectivity or bactericidal potency was achieved by changes in side chain hydrophobicity of MPX. However, enhanced potency was achieved at the expense of selectivity and vice versa in all cases

A Family of Helminth Molecules that Modulate Innate Cell Responses via Molecular Mimicry of Host Antimicrobial Peptides

Over the last decade a significant number of studies have highlighted the central role of host antimicrobial (or defence) peptides in modulating the response of innate immune cells to pathogen-associated ligands. In humans, the most widely studied antimicrobial peptide is LL-37, a 37-residue peptide containing an amphipathic helix that is released via proteolytic cleavage of the precursor protein CAP18. Owing to its ability to protect against lethal endotoxaemia and clinically-relevant bacterial infections, LL-37 and its derivatives are seen as attractive candidates for anti-sepsis therapies. We have identified a novel family of molecules secreted by parasitic helminths (helminth defence molecules; HDMs) that exhibit similar biochemical and functional characteristics to human defence peptides, particularly CAP18. The HDM secreted by Fasciola hepatica (FhHDM-1) adopts a predominantly α-helical structure in solution. Processing of FhHDM-1 by F. hepatica cathepsin L1 releases a 34-residue C-terminal fragment containing a conserved amphipathic helix. This is analogous to the proteolytic processing of CAP18 to release LL-37, which modulates innate cell activation by classical toll-like receptor (TLR) ligands such as lipopolysaccharide (LPS). We show that full-length recombinant FhHDM-1 and a peptide analogue of the amphipathic C-terminus bind directly to LPS in a concentration-dependent manner, reducing its interaction with both LPS-binding protein (LBP) and the surface of macrophages. Furthermore, FhHDM-1 and the amphipathic C-terminal peptide protect mice against LPS-induced inflammation by significantly reducing the release of inflammatory mediators from macrophages. We propose that HDMs, by mimicking the function of host defence peptides, represent a novel family of innate cell modulators with therapeutic potential in anti-sepsis treatments and prevention of inflammation