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Embeddings produced by pre-trained deep neural networks (DNNs) are widely used; however, their efficacy for downstream tasks can vary widely. We study the factors influencing transferability and out-of-distribution (OOD) generalization of pre-trained DNN embeddings through the lens of the tunnel effect hypothesis, which is closely related to intermediate neural collapse. This hypothesis suggests that deeper DNN layers compress representations and hinder OOD generalization. Contrary to earlier work, our experiments show this is not a universal phenomenon. We comprehensively investigate the impact of DNN architecture, training data, image resolution, and augmentations on transferability. We identify that training with high-resolution datasets containing many classes greatly reduces representation compression and improves transferability. Our results emphasize the danger of generalizing findings from toy datasets to broader contexts. 

Abstract A contractile sheath and rigid tube assembly is a widespread apparatus used by bacteriophages, tailocins, and the bacterial type VI secretion system to penetrate cell membranes. In this mechanism, contraction of an external sheath powers the motion of an inner tube through the membrane. The structure, energetics, and mechanism of the machinery imply rigidity and straightness. The contractile tail ofAgrobacterium tumefaciensbacteriophage Milano is flexible and bent to varying degrees, which sets it apart from other contractile tail-like systems. Here, we report structures of the Milano tail including the sheath-tube complex, baseplate, and putative receptor-binding proteins. The flexible-to-rigid transformation of the Milano tail upon contraction can be explained by unique electrostatic properties of the tail tube and sheath. All components of the Milano tail, including sheath subunits, are crosslinked by disulfides, some of which must be reduced for contraction to occur. The putative receptor-binding complex of Milano contains a tailspike, a tail fiber, and at least two small proteins that form a garland around the distal ends of the tailspikes and tail fibers. Despite being flagellotropic, Milano lacks thread-like tail filaments that can wrap around the flagellum, and is thus likely to employ a different binding mechanism.