The question concerning human rights and human rightlessness: disposability and struggle in the Bhopal gas disaster

In the midst of concerns about diminishing political support for human rights, individuals and groups across the globe continue to invoke them in their diverse struggles against oppression and injustice. Yet both those concerned with the future of human rights and those who champion rights activism as essential to resistance, assume that human rights – as law, discourse and practices of rights claiming – can ameliorate rightlessness. In questioning this assumption, this article seeks also to reconceptualise rightlessness by engaging with contemporary discussions of disposability and social abandonment in an attempt to be attentive to forms of rightlessness co-emergent with the operations of global capital. Developing a heuristic analytics of rightlessness, it evaluates the relatively recent attempts to mobilise human rights as a frame for analysis and action in the campaigns for justice following the 3 December 1984 gas leak from Union Carbide Corporation’s (UCC) pesticide manufacturing plant in Bhopal, India. Informed by the complex effects of human rights in the amelioration of rightlessness, the article calls for reconstituting human rights as an optics of rightlessness

Blood group antigen recognition via the group a streptococcal m protein mediates host colonization

Streptococcus pyogenes (group A streptococcus [GAS]) is responsible for over 500,000 deaths worldwide each year. The highly virulent M1T1 GAS clone is one of the most frequently isolated serotypes from streptococcal pharyngitis and invasive disease. The oral epithelial tract is a niche highly abundant in glycosylated structures, particularly those of the ABO(H) blood group antigen family. Using a high-throughput approach, we determined that a strain representative of the globally disseminated M1T1 GAS clone 5448 interacts with numerous, structurally diverse glycans. Preeminent among GAS virulence factors is the surface-expressed M protein. M1 protein showed high affinity for several terminal galactose blood group antigen structures. Deletion mutagenesis shows that M1 protein mediates glycan binding via its B repeat domains. Association of M1T1 GAS with oral epithelial cells varied significantly as a result of phenotypic differences in blood group antigen expression, with significantly higher adherence to those cells expressing H antigen structures compared to cells expressing A, B, or AB antigen structures. These data suggest a novel mechanism for GAS attachment to host cells and propose a link between host blood group antigen expression and M1T1 GAS colonization. IMPORTANCE: There has been a resurgence in group A streptococcal (GAS) invasive disease, which has been paralleled by the emergence of the highly virulent M1T1 GAS clone. Intensive research has focused on mechanisms that contribute to the invasive nature of this serotype, while the mechanisms that contribute to host susceptibility to disease and bacterial colonization and persistence are still poorly understood. The M1T1 GAS clone is frequently isolated from the throat, an environment highly abundant in blood group antigen structures. This work examined the interaction of the M1 protein, the preeminent GAS surface protein, against a wide range of host-expressed glycan structures. Our data suggest that susceptibility to infection by GAS in the oral tract may correlate with phenotypic differences in host blood group antigen expression. Thus, variations in host blood group antigen expression may serve as a selective pressure contributing to the dissemination and overrepresentation of M1T1 GAS.12 page(s