Are Underweight Shelter Dogs More Likely to Display Food Aggression toward Humans?

It is commonly believed that underweight or emaciated dogs are predisposed to food aggression toward humans. Each year, the American Society for the Prevention of Cruelty to Animals (ASPCA) receives hundreds of dogs from criminal cruelty cases. The dogs range from emaciated to overweight. We analyzed existing data from 900 such dogs to examine the relationship between body condition score and food and chew item aggression toward humans. Across all types of cruelty cases, 9.2% of dogs were aggressive over the food, chew, or both, which is a lower prevalence than that previously reported among shelter dogs. Dogs from cruelty cases originating in New York City were more likely to show aggression over food (z = 3.91, p < 0.001) and chew items (z = 2.61, p = 0.01) than dogs from large-scale cruelty cases, although it is unclear why. Female dogs were less likely to show food (z = -3.75, p < 0.001) and chew item (z = -2.25, p = 0.02) aggression compared to males. Underweight dogs were not more likely to display food aggression, but when they did, the aggression was no more severe than that of normal-weight dogs (Fisher's exact tests = 0.41 and 0.15 for the Food Bowl and Chew Item scenarios, respectively). Breed type was not a significant predictor of aggression. Canine food aggression does not appear to be an aberrant behavior caused by a history of food scarcity but may be related to biological factors such as sex. These findings could prove useful for animal behavior subject matter experts testifying in court or consulting on cruelty cases, as they could speak with scientific validity to the question of whether there is a link between previous food scarcity and the likelihood of food aggression in dogs.

Crystal Structure of d-Ornithine/d-Lysine Decarboxylase, a Stereoinverting Decarboxylase: Implications for Substrate Specificity and Stereospecificity of Fold III Decarboxylases.

A newly discovered Fold III pyridoxal 5'-phosphate (PLP)-dependent decarboxylase, d-ornithine/lysine decarboxylase (DOKDC), catalyzes decarboxylation of d-lysine and d-ornithine with inversion of stereochemistry. The X-ray crystal structure of DOKDC has been determined to 1.72 Å. DOKDC has a low level of sequence identity (<30%) with meso-diaminopimelate decarboxylase (DAPDC) and l-lysine/ornithine decarboxylase (LODC), but its three-dimensional structure is very similar. The distal binding site of DAPDC contains a conserved arginine that forms an ion pair with the l-carboxylate end of DAP. In both LODC and DOKDC, this distal site is modified by replacement of the arginine with aspartate, changing the substrate specificity. l-Ornithine decarboxylase (ODC) and LODC have a conserved phenylalanine on the re-face of the PLP complex that has been found to play a key role in the decarboxylation mechanism. We have found that both DAPDC and DOKDC have tyrosine instead of phenylalanine at this position, which precludes the binding of l-amino acids. Because the PLP-binding lysine in ODC, LODC, DAPDC, and DOKDC is located on the re-face of the PLP, we propose that this is the acid group responsible for protonation of the product, thus resulting in the observed retention of configuration for decarboxylation of l-amino acids and inversion for decarboxylation of d-amino acids. The reactions of DAPDC and DOKDC are likely accelerated by positive electrostatics on the re-face by the lysine ε-ammonium ion and on the si-face by closure of the lid over the active site, resulting in desolvation and destabilization of the d-amino acid carboxylate.

Properties and mechanism of d-glucosaminate-6-phosphate ammonia-lyase: An aminotransferase family enzyme with d-amino acid specificity.

Salmonella enterica serovar Typhimurium utilizes a wide range of growth substrates, some of which are relatively novel. One of these unusual substrates is d-glucosaminate, which is metabolized by the enzymes encoded in the dga operon. d-Glucosaminate is transported and converted to d-glucosaminate-6-phosphate (G6P) by a phosphotransferase system, composed of DgaABCD. The protein product of dgaE, d-glucosaminate-6-phosphate ammonia lyase (DGL), converts G6P to 2-keto-3-deoxygluconate-6-phosphate, which undergoes a retroaldol reaction catalyzed by the DgaF protein to give d-glyceraldehyde-3-phosphate and pyruvate. We have now developed an improved synthesis of G6P which gives a higher yield. The DGL reaction is of mechanistic interest because it is one of only a few enzymes in the pyridoxal-5'-phosphate (PLP) dependent aminotransferase superfamily known to catalyze reaction of a d-amino acid substrate. The pH dependence of DGL shows an optimum at 7.5-8.5, suggesting a requirement for a catalytic base. α-Glycerophosphate and inorganic phosphate are weak competitive inhibitors, with Ki values near 30mM, and d-serine is neither a substrate nor an inhibitor. We have found in rapid-scanning stopped-flow experiments that DGL reacts rapidly with its substrate to form a quinonoid intermediate with λmax=480nm, within the dead time (ca. 2msec), which then rapidly decays (k=279s-1) to an intermediate with absorption between 330 and 350nm, probably an aminoacrylate complex. We suggest a mechanism for DGL and propose that the unusual stereochemistry of the DGL reaction requires a catalytic base poised on the opposite face of the PLP-substrate complex from the other members of the aminotransferase superfamily.

STM2360 encodes a d-ornithine/d-lysine decarboxylase in Salmonella enterica serovar typhimurium.

STM2360 is a gene located in a small operon of undetermined function in Salmonella enterica serovar Typhimurium LT2. The amino acid sequence of STM2360 shows significant similarity (∼30% identity) to diaminopimelate decarboxylase (DapDC), a Fold III pyridoxal-5'-phosphate (PLP) dependent enzyme involved in l-lysine biosynthesis. We have found that the protein coded by STM2360 has a previously undocumented catalytic activity, d-ornithine/d-lysine decarboxylase (DOKDC). The reaction products, cadaverine and putrescine, respectively, were identified by NMR and mass spectrometry. The substrate specificity of DOKDC is d-Lysine > d-Ornithine. This is the first pyridoxal-5'-phosphate dependent decarboxylase identified to act on d-amino acids. STM2358, located in the same operon, has ornithine racemase activity. This suggests that the physiological substrate of the decarboxylase and the operon is ornithine. Homologs of STM2360 with high sequence identity (>80%) are found in other common enterobacteria, including species of Klebsiella, Citrobacter, Vibrio and Hafnia, as well as Clostridium in the Firmicutes, and Pseudomonas.

Relationship Between Scarring and Dog Aggression in Pit Bull-Type Dogs Involved in Organized Dogfighting.

When pit bull-type dogs are seized in an investigation of organized dogfighting, heavily scarred dogs are often assumed to be highly dog aggressive due to a history of fighting. These dogs may be deemed dangerous and euthanized based on scarring alone. We analyzed our existing data on dogs seized from four dogfighting investigations, examining the relationship between the dogs' scars with aggression towards other dogs. Scar and wound data were tallied in three body zones where dogfighting injuries tend to be concentrated. Dog aggression was assessed using a model dog and a friendly stimulus dog in a standardized behavior evaluation. Scarring and dog aggression were significantly related, more strongly among male (Fisher's Exact p < 0.001) than female dogs (Fisher's Exact p = 0.05). Ten or more scars in the three body zones was a reasonable threshold with which to classify a dog as high risk for dog aggression: 82% of males and 60% of females with such scarring displayed dog aggression. However, because many unscarred dogs were dog aggressive while some highly scarred dogs were not, we recommend collecting behavioral information to supplement scar counts when making disposition decisions about dogs seized in dogfighting investigations.

A Mannose Family Phosphotransferase System Permease and Associated Enzymes Are Required for Utilization of Fructoselysine and Glucoselysine in Salmonella enterica Serovar Typhimurium.

UNLABELLED: Salmonella enteric serovar Typhimurium, a major cause of food-borne illness, is capable of using a variety of carbon and nitrogen sources. Fructoselysine and glucoselysine are Maillard reaction products formed by the reaction of glucose or fructose, respectively, with the ε-amine group of lysine. We report here that S. Typhimurium utilizes fructoselysine and glucoselysine as carbon and nitrogen sources via a mannose family phosphotransferase (PTS) encoded by gfrABCD (glucoselysine/fructoselysine PTS components EIIA, EIIB, EIIC, and EIID; locus numbers STM14_5449 to STM14_5454 in S. Typhimurium 14028s). Genes coding for two predicted deglycases within the gfr operon, gfrE and gfrF, were required for growth with glucoselysine and fructoselysine, respectively. GfrF demonstrated fructoselysine-6-phosphate deglycase activity in a coupled enzyme assay. The biochemical and genetic analyses were consistent with a pathway in which fructoselysine and glucoselysine are phosphorylated at the C-6 position of the sugar by the GfrABCD PTS as they are transported across the membrane. The resulting fructoselysine-6-phosphate and glucoselysine-6-phosphate subsequently are cleaved by GfrF and GfrE to form lysine and glucose-6-phosphate or fructose-6-phosphate. Interestingly, although S. Typhimurium can use lysine derived from fructoselysine or glucoselysine as a sole nitrogen source, it cannot use exogenous lysine as a nitrogen source to support growth. Expression of gfrABCDEF was dependent on the alternative sigma factor RpoN (σ(54)) and an RpoN-dependent LevR-like activator, which we designated GfrR. IMPORTANCE: Salmonella physiology has been studied intensively, but there is much we do not know regarding the repertoire of nutrients these bacteria are able to use for growth. This study shows that a previously uncharacterized PTS and associated enzymes function together to transport and catabolize fructoselysine and glucoselysine. Knowledge of the range of nutrients that Salmonella utilizes is important, as it could lead to the development of new strategies for reducing the load of Salmonella in food animals, thereby mitigating its entry into the human food supply.

A network evaluation of attitudes toward gays and lesbians among U.S. military cadets.

The U.S. military's ban on open homosexuality has become an increasingly salient issue since its implementation in 1993 and its repeal in 2011. The military is an organization with a unique professional and social organization. Evaluating military attitudes from a network perspective may offer insight into the role of formal and informal leadership in engendering attitudinal change and cultural tolerance around homosexuality. This study evaluates the role of network centrality and network exposure across formal (command networks) and informal (friendship and perceived leadership networks) structures on attitudes toward homosexuality in the military. This work analyzes survey data from a single cadet company within the U.S. Military Academy (n = 139) prior to the repeal of Don't Ask, Don't Tell. Results indicate that popular students tend to show tolerance toward homosexuality, whereas those who hold command leadership positions are more likely to have personal and professional opposition to homosexuality. In addition, formal superior-subordinate relationships are somewhat more likely to suggest social contagion compared to informal leadership and friendship relationships. Recommendations offer guidance for training strategies particularly with respect to a military leaders and socialization. Future research should monitor these issues relative to the post-DADT environment.

Salmonella utilizes D-glucosaminate via a mannose family phosphotransferase system permease and associated enzymes.

Salmonella enterica is a globally significant bacterial food-borne pathogen that utilizes a variety of carbon sources. We report here that Salmonella enterica subsp. enterica serovar Typhimurium (S. Typhimurium) uses d-glucosaminate (2-amino-2-deoxy-d-gluconic acid) as a carbon and nitrogen source via a previously uncharacterized mannose family phosphotransferase system (PTS) permease, and we designate the genes encoding the permease dgaABCD (d-glucosaminate PTS permease components EIIA, EIIB, EIIC, and EIID). Two other genes in the dga operon (dgaE and dgaF) were required for wild-type growth of S. Typhimurium with d-glucosaminate. Transcription of dgaABCDEF was dependent on RpoN (σ(54)) and an RpoN-dependent activator gene we designate dgaR. Introduction of a plasmid bearing dgaABCDEF under the control of the lac promoter into Escherichia coli strains DH5α, BL21, and JM101 allowed these strains to grow on minimal medium containing d-glucosaminate as the sole carbon and nitrogen source. Biochemical and genetic data support a catabolic pathway in which d-glucosaminate, as it is transported across the cell membrane, is phosphorylated at the C-6 position by DgaABCD. DgaE converts the resulting d-glucosaminate-6-phosphate to 2-keto-3-deoxygluconate 6-phosphate (KDGP), which is subsequently cleaved by the aldolase DgaF to form glyceraldehyde-3-phosphate and pyruvate. DgaF catalyzes the same reaction as that catalyzed by Eda, a KDGP aldolase in the Entner-Doudoroff pathway, and the two enzymes can substitute for each other in their respective pathways. Examination of the Integrated Microbial Genomes database revealed that orthologs of the dga genes are largely restricted to certain enteric bacteria and a few species in the phylum Firmicutes.

Medication adherence: pharmacist perspective.

OBJECTIVE: To provide pharmacists with a current, comprehensive review of medication adherence challenges and solutions. DATA SOURCES: A computerized search of the PubMed and Medline databases (through July 2008) identified English language review articles on medication adherence using the MeSH terms patient compliance or adherence and medication, drug regimen, or treatment. STUDY SELECTION: By the authors. DATA EXTRACTION: The results were filtered to include those published in pharmacy journals, and 117 publications were selected based on the content of their abstracts. The final version of this review article used 55 of the 117 publications. An additional 15 publications that provided examples of specific adherence issues were included. A vignette from the authors' experience was used as a case study. DATA SYNTHESIS: This article introduces the challenge of patient medication adherence, discusses the various methods by which to monitor medication adherence, describes various treatment- and condition-related barriers to adherence, and discusses the effectiveness of numerous adherence intervention strategies. CONCLUSION: Nonadherence to a medication regimen may have multiple underlying causes, some of which may be easier to address than others. Open discussion between the pharmacist and patient regarding barriers to adequate medication adherence, followed by a multifaceted, personalized intervention to address these barriers, plays a key role in encouraging patients to adhere to the recommendations of the health care team.

A survey of the methods used in shelter and rescue programs to identify feral and frightened pet cats.

Despite the lack of validated methods for differentiating feral from frightened socialized cats upon intake to animal welfare agencies, these organizations must make handling and disposition decisions for millions of cats each year based on their presumed socialization status. We conducted a nationwide survey of feline welfare stakeholders to learn about methods used to evaluate and categorize incoming cats, amount of time cats are held before assessment, disposition options available, and the level of cooperation among welfare agencies to minimize euthanasia of ferals. A wide variety of assessment methods were described and only 15% of 555 respondents had written guidelines. Holding periods of 1-3 days were common, and cats deemed feral were often euthanased. About half the shelters transferred ferals to trap-neuter-return (TNR) programs at least occasionally. Results highlight the need for validated assessment methods to facilitate judicious holding and disposition decisions for unowned cats at time of intake.

Factors relevant to adoption of cats in an animal shelter.

This study performed a multifactor analysis of the effects of the provision of toys, cage location, and cat characteristics (activity level, age, sex, and coat color) on 111 cats available for adoption in a nonhuman animal shelter. The analysis revealed a greater adopter viewing of cats housed at eye level and of those with toys-even though the toys did not affect the cats' behavior. Adopters viewed cats who were active for longer periods of time. The active cats were more likely to be adopted during the 16-week study than cats who were less active.