From Pato to Parlor.: Domesticity, Masculinity, Religious Space, and Alternative Archives in 20th-Century Ghana

Vom pato zur Wohnstube. Häuslichkeit, männlichkeit, religiöser Raum und alternative Archive im Ghana des 20. Jahrhunderts Die Missionare, die vor 150 Jahren im heutigen Südwest-Ghana ankamen, fanden eine Form häuslicher Architektur vor, die weitgehend von Gender-Prinzipien geprägt war. Jeder, der es sich leisten konnte, baute in seinem Gehöft einen auf drei Seiten geschlossenen Plattform (pato), wo er Besucher empfangen konnte. Ebenfalls wichtig war der Raum, in dem die sakralen Hocker der matrilinearen Ahnen aufbewahrt wurden. Mit der Ausbreitung des Christentums im frühen 20. Jahrhundert entstand eine neue Klasse gebildeter Männer, die zwar im Einklang mit den Forderungen der Missionare zusammen mit der Ehefrau und den Kindern in einem Haus wohnten, aber innerhalb davon eine Stube hatten, die einen männlichen Raum darstellte. Sie übernahm sowohl die Funktion des sakralen Hockerraums (sie war mit christlicher Ikonographie geschmückt und diente unter anderem als Gebetsraum) als auch die des Besucherraums. Dieser Wandel in der Architektur widerspiegelte den Übergang zu einem neuen Männertypu

Intravenous immunoglobulin contains a broad repertoire of anticarbohydrate antibodies that is not restricted to the IgG2 subclass

BACKGROUND: Specificities for carbohydrate IgG antibodies, thought to be predominantly of the IgG2 subclass, have never been broadly examined in healthy human subjects. OBJECTIVE: To examine commercial intravenous immunoglobulin (IVIG) preparations for their ability to recognize a wide range of glycans and to determine the contribution of IgG2 to the binding pattern observed. METHODS: We used a glycan microarray to evaluate IVIG preparations and a control mix of similar proportions of human myeloma IgG1 and IgG2 for binding to 377 glycans, courtesy of the Consortium for Functional Glycomics Core H. Glycans recognized were categorized using public databases for their likely cellular sources. IgG2 was depleted from IVIG by using immunoaffinity chromatography, and depletion was confirmed by using nephelometry and surface plasmon resonance. RESULTS: Nearly half of the glycans bound IgG. Some of the glycans with the greatest antibody binding can be found in structures of human pathogenic bacteria (eg, Streptococcus pneumoniae, Mycobacterium tuberculosis, Vibrio cholera) and nonpathogenic bacteria, including LPS and lipoteichoic acid, capsular polysaccharides, and exopolysaccharides. Surprisingly, depletion of IgG2 had only a modest effect on anticarbohydrate recognition patterns compared with the starting IVIG preparation. Little to no binding activity was detected to human endogenous glycans, including tumor-associated antigens. CONCLUSIONS: This novel, comprehensive analysis provides evidence that IVIG contains a much wider range than previously appreciated of anticarbohydrate IgG antibodies, including those recognizing both pathogenic and non-pathogen-associated prokaryotic glycans

The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites.

Despite the paradigm that carbohydrates are T cell-independent antigens, isotype-switched glycan-specific immunoglobulin G (IgG) antibodies and polysaccharide-specific T cells are found in humans. We used a systems-level approach combined with glycan array technology to decipher the repertoire of carbohydrate-specific IgG antibodies in intravenous and subcutaneous immunoglobulin preparations. A strikingly universal architecture of this repertoire with modular organization among different donor populations revealed an association between immunogenicity or tolerance and particular structural features of glycans. Antibodies were identified with specificity not only for microbial antigens but also for a broad spectrum of host glycans that serve as attachment sites for viral and bacterial pathogens and/or exotoxins. Tumor-associated carbohydrate antigens were differentially detected by IgG antibodies, whereas non-IgG2 reactivity was predominantly absent. Our study highlights the power of systems biology approaches to analyze immune responses and reveals potential glycan antigen determinants that are relevant to vaccine design, diagnostic assays, and antibody-based therapies