PMC

(A) Admixture predictions by three computational algorithms. TreeMix three_pop analysis (green arrow) identified Fonni’s Dog contribution to the Portuguese Water Dog/Cane Paratore clade at 17.43% with P = 0.00723. ANGSD (red dashed line) calculated significant values of D(O, Fonni’s Dog; Komondor, Cane Corso) = 0.039, Z = 4.366; D(O, Komondor; Fonni’s Dog, Cane Corso) = 0.031, Z = 3.920; D(O, Fonni’s Dog; Saluki, Cane Corso) = 0.033, Z = 3.893; D(O, Saluki; Fonni’s Dog, Cane Corso) = 0.040, Z = 5.075. AdmixTools (blue dashed line) supports the findings of TreeMix with significant D-statistic values for Fonni’s Dog and Portuguese Water Dog of D(O, Portuguese Water Dog; Fonni’s Dog, X) = −0.0139 to −0.1287, Z = −3.737 to −25.274; D(O, Fonni’s Dog; Portuguese Water Dog, X) = −0.0127 to −0.1309, Z = −3.078 to −25.797; D(O, Fonni’s Dog; X, Portuguese Water Dog) = 0.0100–0.0767, Z = 3.016–22.189; Cane Paratore of D(O, Cane Paratore; Fonni’s Dog, X) = −0.0104 to −0.1317, Z = −3.108 to −26.025; D(O, Fonni’s Dog; Cane Paratore, X) = −0.0096 to −0.1289, Z = −3.055 to −25.805; D(O, Fonni’s Dog; X, Cane Paratore) = 0.0104–0.0811, Z = 3.643–22.974; Komondor of D(O, Fonni’s Dog; Komondor, X) = −0.0116 to −0.1123; D(O, Fonni’s Dog; X, Komondor) = 0.0116–0.1280, Z = 3.142–25.720; and Saluki of D(Saluki, X; Fonni’s Dog, Y) = 0.007–0.131, Z = 3.047–29.352. TreeMix predicted phylogenies with (B) 1 or(C) 25 allowed introgression events, and corresponding standard error residuals for (D) 1 and (E) 25 introgressions.

Current dog owners show increased levels of sIgE to Can f 3 and Can f 5. Venn diagram of the sIgE positivity for lipocalins, albumin and prostatic kallikrein among non‐current dog owners (A); among current dog owners (B). Comparison of median sIgE levels to each dog allergen component by current dog ownership (current dog owners n = 46, non‐current dog owners, n = 267) in all study group (C). Comparison of median sIgE levels to each dog allergen component by current dog ownership (current dog owners n = 35, non‐current dog owners, n = 183) among subjects sensitized to at least one dog allergen component (D). %, percentage of those sensitized to respective allergen components within each group. D, current dog ownership; e5, dog dander immunoglobulin E; sIgE, specific immunoglobulin E. In (C,D) data are presented as median, and whiskers indicate the minimum and maximum values. *Of note, one person can be sensitized to several dog allergen components and thus, the same person can be included in several of the groups.

Ratings are displayed separately for participants with experience of living in the same household with a dog (with dog experience) or without such experiences (no dog experience). Value 0 means that participants have answered incorrectly when asked what kind of emotion there is in the image and value 1 that they have answered correctly. Statistically significant differences between the participant groups are represented by asterisks (**p<0.01 and *p<0.05).

Table (a) demonstrates Genesping GX.11 fold change from microarray and p value for mRNA intensity value of NR4A1 and ATF3 in normal, I/R and non-I/R vehicle- and CI-treated dog LV. Panel b demonstrates real-time RT-PCR validation of NR4A1 (left) and ATF3 (right) mRNA in normal, I/R and non-I/R vehicle- (Veh-nIR) and CI-treated dog LV. Normal dog, n = 5; Veh dog, n = 6; CI dog, n = 6.

A. The results of dog allergic children’s sera compared to the normal human serum (NHS) of the first B cell epitope (P1). B. The results of dog allergic children’s sera compared to NHS of P2. C. The results of dog allergic children’s sera compared to NHS of P3. D. The results of dog allergic children’s sera compared to NHS of P4. E. The results of dog allergic children’s sera compared to NHS of P5. F. The results of dog allergic children’s sera compared to NHS of an unrelevant control peptide (P6) from the Can f 6 sequence.

The phenotypic variation of Jindo dog. (A). Male Jindo dog with height 35.5 cm, length 38.5 cm, LHR 114.1, (B). Female Jindo dog with height 35 cm, length 40 cm, LHR 114.3, (C). Female Jindo dog with height 42 cm, length 43 cm, LHR 102.4, (D). Female Jindo dog with height 47 cm, length 48 cm, LHR 102.1, (E). Female Jindo dog with height 50 cm, length 54 cm, LHR 108, (F). Female Jindo dog with height 51.5 cm, length 54.4 cm, LHR 105.6, (G). Female Jindo dog with height 49 cm, length 52 cm, LHR 106.1, (H). Male Jindo dog with height 52.0 cm, length 55.5 cm, LHR 106.7.

A) View of the interior of a communal Waiwai house in Konashen, Guyana circa 1955, showing a dog leashed on a dog shelf on the left. Scanned black and white negative. Interior with hammocks, three people and a dog. Negative of slide 2. Object no: ARC/GUP/004/003 Horniman Museum and Gardens. B) Dog house in Masakenari Village, Guyana in 2019.

A, Western blots of membrane proteins prepared from dog atrium (lane 1, DA1) and isolated dog atrial myocytes (lane 2, DA2) probed with a Kv3.1 antibody. Lane 3, dog atrial membrane preparation after pre-incubation of antibody with Kv3.1 peptide (Pre-inc). B, Western blots with Kv1.5 antibody obtained with human atrial (HA) and dog atrial (DA) tissues.

AP dog, CV dog, and UF dog SDS-PAGE. SDS-PAGE = sodium dodecyl-sulfate polyacrylamide gel electrophoresis; AP = acetone precipitated dog hair and dander extract; CV = conventional dog hair and dander extract; UP = ultrafiltered dog hair and dander extract; MW = molecular weight.

Phylogenetic tree constructed upon the complete nucleotide sequences of the H genes of representative CDVs and the selected Hungarian strains. The code, accession number and provenience for the sequences used in the present study are as follow: Dog 98-002 Jpn (AB025270, Japan), Dog KDK1 Jpn (AB025271, Japan), Dog 26D Jpn (AB040766, Japan), Dog Hm3 Jpn (AB040767, Japan), Dog Hm6 Jpn (AB040768, Japan), Dog 00Lm Jpn (AB212730, Japan), Dog P945 Jpn (AB212964, Japan), Dog S124C Jpn (AB212965, Japan), Dog A75/17 USA (AF164967, USA), Dog Chn (AF172411, China), Giant Panda Chn (AF178038, China), Lesser Panda Chn (AF178039, China), Snyder Hill (AF259552, Germany), Onderstepoort (AF378705, South Africa), Dog DK91 Dnk (AF478544, Denmark), Dog Trk (AY093674, Turkey), Dog 5804 Ger (AY386315, Germany), Dog TN Chn (AY390347, China), Racoon 00-2601 USA (AY438597, USA), Racoon 01-2676 USA (AY498692, USA), Racoon 01-2641 USA (AY526496, USA), Racoon 01-2689 USA (AY649446, USA), Dog 18133 USA (AY964108, USA), Dog 19876 USA (AY964110, USA), Dog 25259 USA (AY964114, USA), Dog NTU 1 Jpn (DQ191175, Japan), Dog NTU Jpn (DQ191765, Japan), Dog 324-03 Ita (DQ494317, Italy), Dog 265 Ita (DQ494318, Italy), Ferret Ger (X84999, Germany), Convac (Z35493, Denmark), Mink Dnk (Z47759, Denmark), Dog Dnk (Z47761, Denmark), Black Leopard USA (Z47763, USA), Javelina USA (Z47764, USA), Chinese Leopard USA (Z54156, USA), Dog 404 Ger (Z77671, Germany), Dog Grn (Z47760, Greenland), Seal PDV2 Rus (X84998, Russia), Dog 179-94 Ita (DQ226087, Italy), Dog Yanaka Jpn (D85755, Japan), Dog Hamamatsu Jpn (D85754, Japan).

H-gene 70% majority rule parsimony consensus tree. Arrows or boxes demarcate locations of viruses from this study. GenBank accession numbers are: (1) CDV 00-2601 (Illinois raccoon, Table 3); (2) Chinese leopard (Z54156); (3) 01-2641 (Illinois raccoon, Table 3); (4) black leopard (Z47763); (5) black panther (Z54166); (6 – 8, Illinois raccoons, Table 3); (9) raccoon (Z47765); (10) A75/17 (AF164967); (11) dog (USA) (Z47762); (12) javelina (Z47764); (13) raccoon dog Tanu (AB016776); (14) dog (Taiwan) (AY378091); (15) dog Hamam (D85754); (16) dog KDK1 (AB025271); (17) dog Ueno (D85753); (18) dog Yanaka (D85755); (19) giant panda (AF178038); (20) dog 5804 (AY386315); (21) dog Denmark (Z47761); (22) dog 91A (AF478544); (23) dog isolate A (AF478543); (24) dog 91B (AF478546); (25) dog 91C (AF478548); (26) dog 91D (AF478550); (27) dog isolate C (AF478547); (28) dog isolate B (AF478545); (29) dog isolate D (AF478549); (30) dog isolate 2544 (Z77672); (31) dog isolate 404 (Z77671); (32) dog isolate 4513 (Z77673); (33) dog (Turkey) (AY093674); (34) ferret (X84999); (35) mink (Z47759); (36) lesser panda (AF178039); (37) Siberian seal (X84998); (38) dog (China) (AF172411); (39) dog (Greenland) (Z47760); (40) dog 26D (AB040766); (41) dog 5B (AY297453); (42) dog 5VD (AY297454); (43) dog 98-002 (AB025270); (44) dog HM-3 (AB040767); (45) dog HM-6 (AB040768); (46 – 54, Illinois raccoons, Table 3), (55) Snyder Hill (AF259552); (56) Onderstepoort (AF378705); (57) PDV-1 (AF479274).

Serine 123 phosphorylation is required for expression of the phosphorylated p21 isoform. A, sequence similarity between human and dog p21. Shaded areas indicate the regions for replacing dog p21 with that of human p21 and vice versa. B, schematic representation of various dog and human p21 mutants. C, region, from amino acid 117 to 126, in dog p21, required for expression of two dog p21 isoforms. Three micrograms of pcDNA3 vectors that express HA-tagged wild-type dog p21, dog p21(Hu 38–74), dog p21(Hu 74–83), dog p21(Hu 84–93), dog p21(Hu 107–116), dog p21(Hu 117–126), and dog p21(Hu 127–136) was transfected into Cf2Th cells for 24 h followed by Western blot analysis to determine the levels of p21 proteins, actin, and GAPDH. D, 3 μg of pCDNA3 vectors that express HA-tagged wild-type dog p21, wild-type human p21, human p21(Dog 117–136), human p21(Dog 117–126), human p21(R122H), and human p21(G124P) transfected into 293T cells for 24 h, followed by Western blot analysis to determine the levels of p21 proteins, actin, and GAPDH. E, Cf2Th cells transiently transfected with pcDNA3 vectors expressing human p21(Dog 117–136), human p21(Dog 117–126), human p21(R122H), and human p21(G124P) for 24 h. The cell lysates were treated with or without λ phosphatase (300 units) for 30 min, followed by Western blot analysis to determine the level of p21 proteins, actin, and GAPDH. F, proline at 124 requirement for expression of two dog p21 isoforms. Three micrograms of pcDNA3 vectors that express HA-tagged wild-type dog p21, dog p21(Hu 117–126), dog p21(L120V), dog p21(H122R), dog p21(P124G), and dog p21(R126Q) was transfected into Cf2Th cells for 24 h followed by Western blot analysis to determine the levels of p21 proteins, actin, and GAPDH. G, serine 123 phosphorylation responsibility for expression of two dog p21 isoforms. Three micrograms of pcDNA3 vectors that express HA-tagged wild-type dog p21, dog p21(Hu 117–126), dog p21(S123A), and dog p21(S123D) was transfected into Cf2Th cells for 24 h followed by Western blot analysis to determine the levels of p21 proteins, actin, and GAPDH.

[³H]AS binds directly to dog NPC1L1-K_v1.1. (A) 2D model of dog NPC1L1-K_v1.1. The membrane topology of dog NPC1L1 was predicted with HMMTOP and TMHMM servers available through http://expasy.org/tools/#ptm and manually refined. The pentahelical SSD is highlighted in purple. (B and C) Dog NPC1L1-K_v1.1 is functional. Dog NPC1L1-K_v1.1/MDCKII-Flp (B) or dog NPC1L1/MDCKII-Flp (C) cells were seeded on 96-well plates and incubated with increasing concentrations of [³H]AS for 4 h at 37°C. Specific binding was fit to a single-site saturation model yielding K_d/B_max values of 1.15 nM/3370 cpm for Dog NPC1L1-K_v1.1/MDCKII-Flp cells (●) and 1.28 nM/6436 cpm for dog NPC1L1/MDCKII-Flp cells (▲). (Inset) [³H]cholesterol flux into dog NPC1L1-K_v1.1/MDCKII-Flp cells (●) and dog NPC1L1/MDCKII-Flp cells (▲) was performed as described in the Experimental Procedures in the presence of increasing concentrations of PS. [³H]Ch flux was fit to a single-site inhibition model, yielding IC₅₀ values of 0.21 (B) and 0.24 nM (C) for dog NPC1L1-K_v1.1/MDCKII-Flp cells (●) and dog NPC1L1/MDCKII-Flp cells (▲), respectively. (D) Strategy for affinity purification of dog NPC1L1-K_v1.1. (E and F) Immunoprecipitation of dog NPC1L1-K_v1.1 from membranes and cells. Membranes from dog NPC1L1-K_v1.1/MDCKII-Flp (E) or dog NPC1L1/MDCKII-Flp (F) cells were incubated with 20 nM [³H]AS overnight and solubilized with 1% digitonin/0.03% sodium taurocholate for 30 min at 4°C, as described in Experimental Procedures. Solubilization of 35% or 26% of membrane bound [³H]AS activity from either dog NPC1L1-K_v1.1 or dog NPC1L1 membranes, respectively, was obtained. Solubilized [³H]AS activity (S) was incubated with protein A Sepharose beads coated with an anti-K_v1.1 antibody for 3 h at 4°C. Unbound [³H]AS activity (U) was collected, and the beads were washed three times before determination of [³H]AS bound (P). [³H]AS in U and P has been corrected to account for the dissociation of bound [³H]AS (t_1/2 ≈6 h) during the time of immunoprecipitation. [³H]AS recovered in P of dog NPC1L1/MDCKII-Flp is identical to that obtained in the absence of anti-K_v1.1 antibody. Dog NPC1L1-K_v1.1/MDCKII-Flp (E Inset) or dog NPC1L1/MDCKII-Flp (F Inset) cells were incubated with 20 nM [³H]AS overnight. Free [³H]AS was removed from cells by aspiration as described in Experimental Procedures, and the [³H]AS activity bound to cells was solubilized with 1% digitonin/0.03% sodium taurocholate for 30 min at 4°C. The solubilized [³H]AS activity (S) was immunoprecipitated as indicated in D. Data in E and F are representative of 10 and 8 independent experiments from membranes and cells, respectively. (G) Characterization of affinity-purified dog NPC1L1-K_v1.1. The solubilized (S), unbound (U), and purified (P) material of the immunoprecipitation from dog NPC1L1-K_v1.1/MDCKII-Flp and dog NPC1L1/MDCKII-Flp membranes was resolved by SDS/PAGE, transferred onto a PVDF membrane, and analyzed with an anti-K_v1.1 antibody. Two proteins of M_r 125 and 165 kDa are specifically recognized by the anti-K_v1.1 antibody in the three NPC1L1-K_v1.1 but not NPC1L1 samples. (H) Purified material (P) from G was resolved by SDS/PAGE and visualized by silver staining. Two bands at 125 and 165 kDa (indicated by red arrows) are present in the material purified from dog NPC1L1 K_v1.1 but not dog NPC1L1. (I) Quantification histogram displaying the relative specificities scored by relative peptide queries (rPQ) of affinity-purified proteins identified by LC-MS/MS sequencing of the gel lanes in H. * indicates proteins for which MS/MS spectra are assigned from dog NPC1L1 K_v1.1 but not dog NPC1L1-material. Values were 12 queries for NPC1L1 (gi 148223061) and 2 queries for Trx-related protein (gi 73963782).

Multi-locus sequence typing-distance based phylogenetic tree for extended-spectrum beta-lactamase-producing Escherichia coli isolates. D, dog; C, cat; CD, colonized dog; O, owner; lower case letter, environment; H1, household 1; H2, household 2; D68, dog 10; D5, dog 1; H1O1 t1 SK1, owner household 1; H1O1 t4, owner household 1; H1CD1 t1 SK2 dog household 1; D9, dog 1; D40, dog 5; D10, dog 2; D18, dog 1; C16 SK1, cat 2; D17, dog 2; H1CD1 t2, dog household 1; H1CD1 t1 SK1, dog household 1; H1f1, dog’s sleeping basket (living room); H1c1, water bowl; H1O1 t1 SK2, owner household 1; s7, dog cage; D69 SK2, dog 11; H1m1, carpet; h1y1, kitchen sponge; H1g1, dog’s blanket on terrace; D48, dog 7; H1O1 t2, owner household 1; H1h1, dog’s sleeping basket (bedroom); i11, small cabinet; H1CD1 t3, dog household 1; C17, cat 3; H1CD1 t4 SK2, dog household 1; D26, dog 3; C16 SK2, cat 2; H2O2 t2, owner household 2; H2O2 t1, owner household 2; D58 SK2, dog 9; D72, dog 12; *, whole genome sequencing conducted.

(A) Overall structure of the complex. The chimeric RBD contains the core structure (in cyan) from SARS-CoV-1 RBD and receptor-binding motif (RBM) (in magenta) from SARS-CoV-2 RBD. The chimeric raccoon dog ACE2 contains the core structure (in green) from human ACE2 and three virus-binding motifs (VBMs) (in orange) from raccoon dog ACE2. (B) Structural interface between SARS-CoV-2 RBM and raccoon dog VBMs. Three virus-binding hotspots are highlighted. The key residues that differ between human ACE2 and raccoon dog ACE2 are shown in sticks.

Expression of metalloprotease and cysteine protease genes from Leishmania (L.) infantum in naturally infected dogs. Total RNA from dog's ear edge skin was extracted and reverse transcription polymerase chain reactions (RT-PCR) were performed using specific primers for the β-actin (a), metalloprotease (b), and cysteine protease (c) genes. RT-PCR products were resolved on a 2% agarose gels stained with Nancy-520. A 100 bp DNA ladder (L) was used as a molecular weight marked and revealed single 87 bp, 202 bp, and 227 bp fragments, respectively, in the tested cDNA samples. Asymptomatic (Dog 2, Dog 4, Dog6, Dog 11, Dog 12, Dog 16, and Dog 19), oligosymptomatic (Dog 3, Dog 5, Dog 7, Dog 8, Dog 9, Dog 10, Dog 13, Dog 14, and Dog 20) and polysymptomatic (Dog 1, Dog 15, Dog 17 and Dog 21).

Cases of dog rabies for alternative dog rabies vaccination programs in East Africa: A. Low levels of transmission; B. High levels of transmission^a Footnotes: a. Results for two scenarios for dog rabies vaccination programs in an East African population of 1 million persons (approximately 2/3 urban, 1/3 rural), with approximately 82,000 dogs (). Vaccination programs: Option 1, annual mass dog vaccination, resulting in 50% of the dog population vaccinated, and Option 2, biannual (twice per year) mass dog vaccination, resulting in 20% of the dog population vaccinated for each vaccination program. Rabies transmission risk is defined, in part, by the number of bites per rabid dog to another dog (see ).

Examples of Donggyeong dog-specific non-synonymous SNPs and consequential amino acid variants. Top panel shows gene structure with the direction of transcription (blue arrow). Bottom panel indicates positions of non-synonymous SNPs and comparison of amino acids among different dog breeds and related species. Two different amino acids corresponding to two nucleotide variants in Donggyeong dog are shown together with a slash delimiter. The dash symbol represents a gap in multiple sequene alignment. DG: Donggyeong dog, DQ: Diquing village dog, KM: Kunming dog, YJ: Yingjiang village dog, GS: German shepherd, LJ: Lijiang village dog, TM: Tibetan mastiff. Other dog breeds not shown here contained the same variant as dog breeds with blue color shown in this figure.

Main research questions (RQ1–RQ5). We examined the triadic connection between the dog owner temperament, dog–owner relationship, and the dog social and cognitive behavior (RQ1–3). Also dog physical activity connection with dog–owner relationship and dog behavior was examined (RQ4), and the modulation of the connection between the owner temperament and dog behavior by the dog breed group (herding dogs vs. primitive type breeds, RQ5).

Evaluation of ICT based on rBcMSA1 and rBcSA1. a Cross-reactivity of ICT using rBcMSA1 with closely related parasite-infected canine sera: lane 1, B. rossi-infected dog serum; lane 2, B. vogeli-infected dog serum; lane 3, B. gibsoni-infected dog serum; lane 4, L. infantum-infected dog serum; lane 5, B. canis-infected dog serum; lane 6, a SPF dog serum; b Specific antibody responses to rBcMSA1 in sequential serum samples from a non-splenectomized dog experimentally infected with B. canis; c Cross-reactivity of rBcSA1 with closely related parasite-infected canine sera: lane 1, SPF dog serum; lane 2, B. canis-infected dog serum; lane 3, B. rossi-infected dog serum; lane 4, B. vogeli-infected dog serum; lane 5, B. gibsoni-infected dog serum; lane 6, L. infantum-infected dog serum; d Specific antibody responses to rBcSA1 in sequential serum samples from a non-splenectomized dog experimentally infected with B. canis