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"Ross, James F."
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The adsorption of fungal ice-nucleating proteins on mineral dusts: a terrestrial reservoir of atmospheric ice-nucleating particles
The occurrence of ice-nucleating particles (INPs) in our atmosphere has a profound impact on the properties and lifetime of supercooled clouds. To date, the identities, sources and abundances of particles capable of nucleating ice at relatively low supercoolings (T > −15 °C) remain enigmatic. While biomolecules such as proteins and carbohydrates have been implicated as important high-temperature INPs, the lack of knowledge on the environmental fates of these species makes it difficult to assess their potential atmospheric impacts. Here we show that such nanoscale ice-nucleating proteins from a common soil-borne fungus (Fusarium avenaceum) preferentially bind to and confer their ice-nucleating properties to kaolinite. The ice-nucleating activity of the proteinaceous INPs is unaffected by adsorption to the clay, and once bound the proteins do not readily desorb, retaining much of the activity even after multiple washings with pure water. The atmospheric implications of the finding that biological residues can confer their ice-nucleating ability to dust particles are discussed.
Journal Article
The Mutagenic Plasticity of the Cholera Toxin B-Subunit Surface Residues: Stability and Affinity
Mastering selective molecule trafficking across human cell membranes poses a formidable challenge in healthcare biotechnology while offering the prospect of breakthroughs in drug delivery, gene therapy, and diagnostic imaging. The cholera toxin B-subunit (CTB) has the potential to be a useful cargo transporter for these applications. CTB is a robust protein that is amenable to reengineering for diverse applications; however, protein redesign has mostly focused on modifications of the N- and C-termini of the protein. Exploiting the full power of rational redesign requires a detailed understanding of the contributions of the surface residues to protein stability and binding activity. Here, we employed Rosetta-based computational saturation scans on 58 surface residues of CTB, including the GM1 binding site, to analyze both ligand-bound and ligand-free structures to decipher mutational effects on protein stability and GM1 affinity. Complimentary experimental results from differential scanning fluorimetry and isothermal titration calorimetry provided melting temperatures and GM1 binding affinities for 40 alanine mutants among these positions. The results showed that CTB can accommodate diverse mutations while maintaining its stability and ligand binding affinity. These mutations could potentially allow modification of the oligosaccharide binding specificity to change its cellular targeting, alter the B-subunit intracellular routing, or impact its shelf-life and in vivo half-life through changes to protein stability. We anticipate that the mutational space maps presented here will serve as a cornerstone for future CTB redesigns, paving the way for the development of innovative biotechnological tools.
Journal Article
Sortase-Modified Cholera Toxoids Show Specific Golgi Localization
Cholera toxoid is an established tool for use in cellular tracing in neuroscience and cell biology. We use a sortase labeling approach to generate site-specific N-terminally modified variants of both the A2-B5 heterohexamer and B5 pentamer forms of the toxoid. Both forms of the toxoid are endocytosed by GM1-positive mammalian cells, and while the heterohexameric toxoid was principally localized in the ER, the B5 pentamer showed an unexpectedly specific localization in the medial/trans-Golgi. This study suggests a future role for specifically labeled cholera toxoids in live-cell imaging beyond their current applications in neuronal tracing and labeling of lipid rafts in fixed cells.
Journal Article
Thought and World
James F. Ross is a creative and independent thinker in
contemporary metaphysics and philosophy of mind. In this concise
metaphysical essay, he argues clearly and analytically that
meaning, truth, impossibility, natural necessity, and our
intelligent perception of nature fit together into a distinctly
realist account of thought and world. Ross articulates a moderate
realism about repeatable natural structures and our abstractive
ability to discern them that poses a challenge to many of the
common assumptions and claims of contemporary analytic philosophy.
He develops a broadly Aristotelian metaphysics that recognizes the
\"hidden necessities\" of things, which are disclosed through the
sciences, which ground his account of real impossibility as a kind
of vacuity, and which require the immateriality of the human
ability to understand. Those ideas are supported by a novel account
of false judgment. Ross aims to offer an analytically and
historically respectable alternative to the prevailing positions of
many British-American philosophers.
eBook
Rational Reliance
Ross discusses the features of rational reliance, willing commitment and the cognitive functions of feeling to indicate that religious commitment is not some deformity of rational belief, but rather follows a general process for knowing.
Journal Article
ON CHRISTIAN PHILOSOPHY: UNA VERA PHILOSOPHIA?
The notion of a Christian philosophy is examined. The reality of God is accessible to rational inquiry and can be proved by various considerations.
Journal Article
The Crash of Modal Metaphysics
Quantified modal logic is discussed. A change in propositional truth-values does not generate all the ways things might have been.
Journal Article