The Grizzly, May 3, 2001

Xenadrine Evidence Points Towards Addictive Nature • Class of 2004 Offers Words of Wisdom to Class of 2005 • Public Radio Personality Ira Glass Hosts Lecture at Ursinus • Fountain Expected to be Completed Soon • Saying Goodbye: Grizzly Editor Signoffs • Opinions: National Missile Defense Still a Bad Idea; Greek Week Unites Local Organizations; Awards Ceremony an Enriching Experience • Stalin\u27s Daughter Steals the Stage • Annual Student Art Show Arrives at Berman • Women\u27s Lacrosse Wins CC Title; Looks Ahead to NCAA\u27s • Girls Rugby Finishes Spring Season • Tennis Teams Lose in First Round at CCC • A Weekend of CCC Playoffs and Tournaments Sees Success for Few • Final Exams Schedulehttps://digitalcommons.ursinus.edu/grizzlynews/1490/thumbnail.jp

Fermenting Feminism

"Fermenting Feminism brings together artists whose work responds to what it means to bring fermentation and feminism into the same critical space. These are works that approach fermentation through intersectional and trans-inclusive feminist frameworks, and works that approach feminisms through the metaphor and material practice of fermentation. As both a metaphor and a physical process, fermentation embodies bioavailability and accessibility, preservation and transformation, inter-species symbiosis and coevolution, biodiversity and futurity, harm reduction and care." -- p. [1]

Sandor Katz and the Possibilities of a Queer Fermentive Praxis

Fermentation, when embedded in queer politics, offers a conceptual and material challenge to the ideology of purism that structures dominant understandings of health in the North American context. Through a close reading of Sandor Katz’s book Wild Fermentation and the author’s experiences at a 2014 summer residency at Katz’s Foundation for Fermentation Fervor, this article contributes to food studies scholarship exploring the transformative potential of fermentation. In his teaching and writing, Katz challenges the ideology of purism through a queer fermentive praxis that advocates for improvisation, microbial inspiration, and interdependent nourishment. This praxis demonstrates an imperfect, do-it-yourself (DIY) ethos of fermentation that empowers folks to experiment with found and foraged materials. Katz’s theorization of fermentation as social change heralds the queer shape-shifting of microorganisms as inspiration for human action. And, in the context of the queer rural community where he makes his home, Katz’s fermentive praxis cultivates interdependent, inter-species nourishment. This queer fermentive praxis activates the political potential of fermentation by refusing the dominant view of human beings as individuals engaged in purity projects of control and subordination. Instead, it imagines humans as co-constituted, deeply dependent subjects who are responsible to, and in service of creating conditions for flourishing of all kinds of life.La fermentation, lorsque partie intégrante des activités d’une communauté non-hétéronormative, présente un défi d’ordre conceptuel et matériel face à l’idéologie puriste qui sous-tend la perception généralisée de la santé en Amérique du Nord. Grâce à une lecture attentive du livre de Sandor Katz, Wild Fermentation, qu’a effectuée l’auteure, ainsi qu’à ses expériences vécues lors de son séjour estival à la Katz’s Foundation for Fermentation Fervor (Fondation des adeptes de la fermentation, notre traduction) en 2014, cet article apporte une contribution intéressante aux travaux académiques sur les aliments qui explorent le potentiel transformateur de la fermentation. Autant dans la formation qu’il donne que dans ses écrits, Katz met au défi les idées puristes en préconisant des pratiques de fermentation qui encouragent l’improvisation, l’inspiration microbienne, et une alimentation basée sur des ingrédients interdépendants. Cette pratique démontre une philosophie en matière de fermentation qui fait appel à l’improvisation et à la créativité, en permettant aux gens d’expérimenter avec des ingrédients cueillis dans la nature. La théorisation de la fermentation comme agent de changement social avancée par Katz est annonciatrice de l’inspiration qu’offre la métamorphose des microorganismes en matière d’intervention sociale. Qui plus est, dans le contexte de la communauté altersexuelle où il s’est établi, les pratiques de Katz en matière de fermentation nourrissent le concept d’une alimentation basée sur des ingrédients interdépendants et interspécifiques. Ces pratiques qui sortent des sentiers battus encouragent le pouvoir politique potentiel de la fermentation en refusant les idéologies populaires qui considèrent les êtres humains comme des personnes impliquées dans des projets de contrôle et de subordination purificatoires. Au lieu de cela, sa vision privilégie les êtres humains comme étant des individus qui cohabitent et dépendent fortement les uns des autres, et qui s’efforcent, et se rendent responsables, de créer des conditions propices à l’épanouissement de toutes les espèces vivantes

Structure-function analyses of metal-binding sites of HypA reveal residues important for hydrogenase maturation in Helicobacter pylori.

The nickel-containing enzymes of Helicobacter pylori, urease and hydrogenase, are essential for efficient colonization in the human stomach. The insertion of nickel into urease and hydrogenase is mediated by the accessory protein HypA. HypA contains an N-terminal nickel-binding site and a dynamic structural zinc-binding site. The coordination of nickel and zinc within HypA is known to be critical for urease maturation and activity. Herein, we test the hydrogenase activity of a panel of H. pylori mutant strains containing point mutations within the nickel- and zinc-binding sites. We found that the residues that are important for hydrogenase activity are those that were similarly vital for urease activity. Thus, the zinc and metal coordination sites of HypA play similar roles in urease and hydrogenase maturation. In other pathogenic bacteria, deletion of hydrogenase leads to a loss in acid resistance. Thus, the acid resistance of two strains of H. pylori containing a hydrogenase deletion was also tested. These mutant strains demonstrated wild-type levels of acid resistance, suggesting that in H. pylori, hydrogenase does not play a role in acid resistance

Strains, plasmids, and primers used in this study.

<p>Strains, plasmids, and primers used in this study.</p

The Δ<i>hydABCDE</i> strain of <i>H</i>. <i>pylori</i> 26695 is not attenuated for acid survival.

<p>The wild-type (WT) strain, urease mutant strain (Δ<i>ureAB</i>), and hydrogenase mutant strain (Δ<i>hydABCDE</i>) were incubated for 1 hr in PBS adjusted to pH 6.0 (A and B) or to pH 2.3 (C and D), in the absence (A and C) or presence (B and D) of 5 mM urea. The number of colony-forming units (CFU) was measured at 0 min (T₀) and at 60 min (T₆₀), and percent survival was calculated as CFU at T₆₀ divided by CFU at T₀. Data from individual biological replicates are shown as points, with the bar plotted at the mean. Open symbols indicate that no bacteria were recovered and thus, the CFU are plotted as a function of the limit of detection (1000 CFU/mL). Three biological replicates were performed. For panels A-C, a one-way ANOVA followed by Dunnett’s test for multiple comparisons was performed; the comparison was made only to WT. In panel D, the same statistical tests were performed on the log-transformed data. **** = p < 0.0001.</p

The Δ<i>hydB</i> strain of <i>H</i>. <i>pylori</i> G27 is not attenuated for acid survival.

<p>The wild-type (WT) strain, urease mutant strain (Δ<i>ureB</i>), and hydrogenase mutant strain (Δ<i>hydB</i>) were incubated for 1 hr in PBS adjusted to pH 6.0 (A and B) or to pH 2.3 (C and D), in the absence (A and C) or presence (B and D) of 5 mM urea. The number of colony-forming units (CFU) was measured at 0 min (T₀) and at 60 min (T₆₀), and percent survival was calculated as CFU at T₆₀ divided by CFU at T₀. Data from individual biological replicates are shown as points, with the bar plotted at the mean. Open symbols indicate that no bacteria were recovered and thus, the CFU are plotted as a function of the limit of detection (100 CFU/mL). Three biological replicates were performed. For panels A-C, a one-way ANOVA followed by Dunnett’s test for multiple comparisons was performed; the comparison was made only to WT. In panel D, the same statistical tests were performed on the log-transformed data. **** = p < 0.0001.</p

The structure of HypA and its role in urease and hydrogenase maturation.

<p>(A) Representation of the NMR structure of <i>H</i>. <i>pylori</i> HypA (PDB: 2KDX) [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0183260#pone.0183260.ref025" target="_blank">25</a>] with the main chain colored in light grey and the metal binding sites in color to highlight the location of residues involved in metal coordination. Residues comprising the nickel-binding site (M1, H2, E3, and D40) are shown in green. Residues of the zinc-binding site (C74, C77, H79, C91, C94, and H95) are shown in cyan. The metal-binding oxygen (red), nitrogen (blue), and sulfur (yellow) atoms are shown as small spheres. The nickel atom representation in this figure (dotted green circle) was not resolved in the 2KDX structure, and the resolved zinc atom is shown as a dark grey sphere. The zinc-binding site adopts two pH-dependent conformations, as illustrated: Zn(Cys)₂(His)₂ at acidic pH, and Zn(Cys)₄ at neutral pH. (B) HypA contributes to the maturation of hydrogenase and urease through delivery of nickel (green circles). Urease requires nickel for activity, of which one of the downstream effects is acid resistance. In the absence of HypA, maturation of urease can still be accomplished through the addition of excess nickel (dashed line). Hydrogenase requires nickel for activity, but herein is shown not to contribute to <i>in vitro</i> acid resistance (red X). In the absence of HypA, maturation of hydrogenase cannot be accomplished through the addition of excess nickel.</p

Mutation of the metal coordination sites of HypA results in decreased hydrogenase activity.

<p>Cell lysates from the indicated <i>hypA</i> mutant strains, in addition to wild-type (WT) strain, urease mutant strain (Δ<i>ureB</i>), <i>hypA</i> mutant strain (<i>hypA</i>::<i>kan-sacB</i>), and <i>hypA</i> restorant (<i>hypA</i>-R) were utilized to determine hydrogenase activity using a methyl viologen assay. The rate at which H₂ was oxidized (in μmol/min) was obtained using the slope of absorbance at A_{578 nm}, which was normalized to the amount of total protein in the cell lysate (in μg), and normalized against the activity of the WT strain to obtain percent hydrogenase activity. The hydrogenase activities of <i>hypA</i> mutant strains with mutations found within the nickel-binding site (A) and within the zinc-binding site (B) are shown. Two biological replicates were tested in A, and three biological replicates were tested in B. The mean is graphed, with range (A) or standard deviation (B).</p

Hydrogenase activity, urease activity, survival at pH 2.3 with urea, and dissociation constants.^a

<p>Hydrogenase activity, urease activity, survival at pH 2.3 with urea, and dissociation constants.<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0183260#t002fn001" target="_blank">^a</a></p