Pets may contract foodborne pathogens, including Salmonella, Listeria monocytogenes, and Shiga toxin-producing Escherichia coli (STEC), from their diet, environment, and infected humans and animals. 17,18,20 A 2014 study reported Salmonella, L. monocytogenes, and STEC in 7.7%, 16.3%, and 4.1%, respectively, of 196 samples of commercial raw pet foods tested. 18 In addition, a 2017 multi-laboratory study of Salmonella prevalence in pets demonstrated that dogs testing positive for Salmonella were more likely to have consumed raw food than cooked food. 20 The U.S. Food and Drug Administration (FDA; https://www.fda.gov/ForConsumers/ConsumerUpdates/ucm403350.htm) and the Centers for Disease Control and Prevention (https://www.cdc.gov/ salmonella/schwarzengrund_faq.html) have issued statements to consumers that feeding raw meat diets to pets may pose a public health risk. Despite the public health risk, previous surveys on pet feeding practices in the United States, Canada, and Australia indicate that 16-30% of dogs and 9.6% of cats may receive raw diets or bones. 5,14 Infected animals, however, may not show clinical signs, complicating the diagnosis of pet foodborne illness. 20 Because of the potential for human exposure, identifying and diagnosing pet foodborne illness is crucial to protecting animal and human health. 18 We report the results of 2 case investigations involving 3 breeders, each with pet illness associated with consumption of raw pet food. For each case investigation, FDA received consumer complaints either through the FDA Safety Reporting Portal (https://www.safetyreporting.hhs.gov/) or through a FDA District Office. The FDA Center for Veterinary Medicine evaluated the complaints (https://www.fda.gov/Safety/ ReportaProblem/QuestionsandAnswersProblemReporting/ ucm056069.htm), and the FDA Veterinary Laboratory Investigation and Response Network (Vet-LIRN; https://www.fda. gov/AnimalVeterinary/ScienceResearch/ucm247334.htm) requested medical records and conducted dietary and environmental exposure interviews to obtain signalment and significant clinical histories from both case investigations (Table 1). Clinical samples, leftover open products, and closed unopened products were tested for foodborne pathogens, primarily Salmonella and Listeria in case 1, with the addition of E. coli in case 2. In both cases, product pathogen testing was 823046V DIXXX10.1177/1040638718823046Whole genome sequencing to confirm pet foodborne illnessJones et al.

Within the genus Mycoplasma are species whose cells have terminal organelles, polarized structures associated with cytadherence and gliding motility. Mycoplasma penetrans , found mostly in HIV-infected patients, and Mycoplasma iowae , an economically significant poultry pathogen, are members of the Mycoplasma muris phylogenetic cluster. Both species have terminal organelles that interact with host cells, yet the structures in these species, or any in the M. muris cluster, remain uncharacterized. Time-lapse microcinematography of two strains of M. penetrans , GTU-54-6A1 and HF-2, and two serovars of M. iowae , K and N, show that the terminal organelles of both species play a role in gliding motility, with differences in speed within and between the two species. The strains and serovars also differed in their hemadsorption abilities that positively correlated with differences in motility speeds. No morphological differences were observed between M. penetrans and M. iowae by scanning electron microscopy (SEM). SEM and light microscopy of M. penetrans and M. iowae showed the presence of membranous filaments connecting pairs of dividing cells. Breaking of this filament during cell division was observed for M. penetrans by microcinematography, and this suggests a role for motility during division. The Triton X-100-insoluble fractions of M. penetrans and M. iowae consisted of similar structures that were unique compared to those identified in other mycoplasma species. Like other polarized mycoplasmas, M. penetrans and M. iowae have terminal organelles with cytadherence and gliding functions. The difference in function and morphology of the terminal organelles suggests that mycoplasmas have evolved terminal organelles independently of one another.

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Although mycoplasmas have small genomes, many of them, including the HIV-associated opportunist Mycoplasma penetrans, construct a polar attachment organelle (AO) that is used for both adherence to host cells and gliding motility. However, the irregular phylogenetic distribution of similar structures within the mycoplasmas, as well as compositional and ultrastructural differences among these AOs, suggests that AOs have arisen several times through convergent evolution. We investigated the ultrastructure and protein composition of the cytoskeleton-like material of the M. penetrans AO with several forms of microscopy and biochemical analysis, to determine whether the M. penetrans AO was constructed at the molecular level on principles similar to those of other mycoplasmas, such as Mycoplasma pneumoniae and Mycoplasma mobile. We found that the M. penetrans AO interior was generally dissimilar from that of other mycoplasmas, in that it exhibited considerable heterogeneity in size and shape, suggesting a gel-like nature. In contrast, several of the 12 potential protein components identified by mass spectrometry of M. penetrans detergent-insoluble proteins shared certain distinctive biochemical characteristics with M. pneumoniae AO proteins, although not with M. mobile proteins. We conclude that convergence between M. penetrans and M. pneumoniae AOs extends to the molecular level, leading to the possibility that the less organized material in both M. pneumoniae and M. penetrans is the substance principally responsible for the organization and function of the AO.IMPORTANCE Mycoplasma penetrans is a bacterium that infects HIV-positive patients and may contribute to the progression of AIDS. It attaches to host cells through a structure called an AO, but it is not clear how it builds this structure. Our research is significant not only because it identifies the novel protein components that make up the material within the AO that give it its structure but also because we find that the M. penetrans AO is organized unlike AOs from other mycoplasmas, suggesting that similar structures have evolved multiple times. From this work, we derive some basic principles by which mycoplasmas, and potentially all organisms, build structures at the subcellular level.KEYWORDS Mycoplasma, cytoskeleton, electron microscopy, evolution, fractionation, mass spectrometry, transcriptomics

Genomic data and biomedical imaging data are undergoing exponential growth. However, our understanding of the phenotype–genotype connection linking the two types of data is lagging behind. While there are many types of software that enable the manipulation and analysis of image data and genomic data as separate entities, there is no framework established for linking the two. We present a generic set of software tools, BioDIG, that allows linking of image data to genomic data. BioDIG tools can be applied to a wide range of research problems that require linking images to genomes. BioDIG features the following: rapid construction of web-based workbenches, community-based annotation, user management and web services. By using BioDIG to create websites, researchers and curators can rapidly annotate a large number of images with genomic information. Here we present the BioDIG software tools that include an image module, a genome module and a user management module. We also introduce a BioDIG-based website, MyDIG, which is being used to annotate images of mycoplasmas.Database URL: BioDIG website: http://biodig.orgBioDIG source code repository: http://github.com/FriedbergLab/BioDIGThe MyDIG database: http://mydig.biodig.org/