Nat Genet 2006, 38:873–875.PubMedCrossRef 35. Schrauder M, Frank S, Strissel PL, Lux MP, Bani MR, Rauh C, Sieber CC, Heusinger K, Hartmann A, Schulz-Wendtland R, Strick R, Beckmann MW, Fasching PA: Single nucleotide polymorphism D1853N of the ATM gene may alter the risk for breast cancer. J Cancer Res Clin Oncol 2008, 134:873–882.PubMedCrossRef 36. Tommiska J, Jansen L, Kilpivaara O, Edvardsen H, Kristensen V, Tamminen A, Aittomaki K, Blomqvist AMN-107 C, Borresen-Dale AL, Nevanlinna H:

ATM variants and cancer risk in breast cancer patients from Southern Finland. BMC Cancer 2006, 6:209.PubMedCrossRef selleck kinase inhibitor Competing interests The authors declare that they have no competing interests. Authors’ contributions GLB, PXM, and Zhang

L designed the study, and wrote the manuscript; SH, WX, and RL performed data acquisition; LLJ performed quality control of data; LWB, LML, and YWZ performed statistical analysis and interpretation. All authors read and approved the final manuscript.”
“Introduction P505-15 Skin tumors have become one of the most common cancers in many countries, with rapid increasing incidence during the last half century. Nonmelanoma skin cancers including basal cell carcinoma (BCC) and squamous cell carcinoma (SCC) now make up more than one third of all cancers in the United States [1]. A large number of studies regarding the role of oncogenes and hormones, as well as environmental and predisposing factors, have been reported. Oncogenes, especially Src family kinases (SFKs), which are activated in colon and breast cancers, are drawing

attention for Methane monooxygenase their involvement in malignant melanoma (MM) [2]. SFKs are non-receptor tyrosine kinases that participate in variable cellular signal transduction pathways, with the capacity to trigger cancer with its continuous activation. SFKs are composed of 9 members, c-Src, c-Yes, Fyn, Lyn, Lck, Hck, Blk, Rgr, and Yrk. SFKs play integral roles in cancer development to include proliferation, survival, motility, invasiveness, metastasis, and angiogenesis. Most SFKs are primarily expressed from a hematopoietic cell origin, but c-Src, c-Yes, and Fyn are expressed at high levels by platelets, neurons, and some epithelial tissues [3]. c-Src and c-Yes in particular are over-expressed or hyper-activated in many human epithelial cancers. The role and process of these two oncogenes in colon and breast cancer are well studied, but not in other human cancers. The role of SFKs in melanoma have been investigated with conflicting reports, but their overall role in nonmelanoma skin tumors has yet to be elucidated. Tyrosine kinases are known to be activated in many human MM, SCC, and BCC epithelial cancers. Therefore, we studied the expression of c-Src and c-Yes to uncover its involvement in malignant skin cancer development.

MST analysis was completed within four working days. Analysis of the sequence combinations determined three new genetic profiles, including profile ST43, which characterized the three isolates derived from patients A, D, and E; profile ST44, which characterized the two isolates derived from patient B and the index patient C; and profile ST45, which was discovered

in the isolate derived from patient F (Figure 1). These new profiles resulted from a novel combination of the following spacer alleles: the ST43 profile combined alleles 1/MST1, 1/MST2, 1/MST3, 2/MST4, 1/MST8, 3/MST11, 4/MST12, and allele 4/MST13; the ST44 profile combined alleles 1/MST1, 1/MST2, 2/MST3, 2/MST4, 1/MST8, 3/MST11, 4/MST12, and allele 4/MST13; and the ST45 profile combined alleles 1/MST1, 1/MST2, 1/MST3, selleck products 1/MST4, 3/MST8, 3/MST11, 4/MST12, and allele 4/MST13. The profiles for ST43, ST44, and ST45 have been added to our free and accessible MST database http://​ifr48.​timone.​univ-mrs.​fr/​MST_​Mtuberculosis/​mst. MST this website genotyping data were assumed to be authentic based on the observations see more that the PCR-negative controls remained negative, coupled with the observation that all PCR products were of the predicted size. Moreover, analysis of the spacer sequences edited in this work identified three new profiles, clearly

indicating that amplicons did not result from laboratory contamination as a consequence of previous experiments. The MST genotyping data provided evidence to support epidemiological and clinical data

Endonuclease that confirmed laboratory cross-contamination. Specifically, one profile (ST43) comprised three isolates recovered from epidemiologically-linked patients, whereas a different profile (ST45) characterized only one isolate from a specimen collected from an unrelated patient F. The profile ST44 was discovered for two M. tuberculosis isolates obtained from the index patient C and one unrelated patient B. Microscopic examination of a respiratory tract specimen collected from patient B indicated the presence of acid-fast bacilli, while the same analysis performed for a specimen from the respiratory tract of the index patient C showed no indication of acid-fast bacilli. Both of the latter two specimens were handled in the same laboratory, on the same day, and within the same batch of sample preparations, which explains the observation that the specimen recovered from the index patient (patient C) was contaminated by the specimen collected from patient B. Such a situation has been previously observed in cases of laboratory cross-contamination [19, 20]. Interestingly, the frequency of false-positive cultures has been shown to be higher for laboratories that do not process high numbers of specimens [6], as was the case in the present report.

This is consistent with the presence of proteins accumulating non-synonymous substitutions. Some proteins can also be exported across the inner and outer membranes via typical gram-negative secretion systems (reviewed in [38]) encoded exclusively in the M. endobia genome. As other endosymbionts with similarly reduced genomes, selleck kinase inhibitor M. endobia has retained a fully functional Sec translocation

complex [16]. It also encodes Ffh, which together with 4.5S RNA forms the signal recognition particle (SRP), needed to bind the signal sequence of the proteins targeted for secretion through this system and to drive them to FtsY, the SRP receptor. Although in other endosymbionts there is an alternative system to assist proteins in their secretion, in which the proteins are recognized by the SecB chaperone after translation, this system cannot be functional in this consortium, because secB appears to be a pseudogene [16]. Intermediate metabolism T. princeps has almost null metabolic capacities, except for the production of essential amino acids, as described elsewhere [16]. Only M. endobia encodes a phosphotransferase system (PTS) for the uptake of hexose as carbon source, Selleckchem Blasticidin S and it is predicted to perform glycolysis, transform pyruvate into acetate, and use it to feed the pathway for fatty acids biosynthesis, similarly to that described for B. aphidicola BCc, with highly reduced metabolic capabilities [39]. However, the pentose phosphate

pathway appears to be incomplete, since only zwf, pgl and tkt have been preserved, while talA appears to be a pseudogene. Interestingly, T. princeps has retained a transaldolase Glutamate dehydrogenase TalB, which along with transketolase (Tkt) creates a reversible link between the pentose phosphate pathway and glycolysis, revealing another possible

case of metabolic complementation between both bacteria. Regarding the tricarboxylic acid (TCA) cycle, only mdh (encoding malate dehydrogenase) has been preserved in T. princeps, while M. endobia has retained only the genes that encode succinyl-CoA synthetase. This is the only step that has been maintained in S. symbiotica SCc [5], where the authors indicate that it must have been retained because it is necessary for lysine biosynthesis. Nevertheless, this cannot be the case in this consortium, since lysine biosynthesis cannot be accomplished. As in other endosymbionts, NAD+ can be regenerated by the action of the NADH-quinone oxidoreductase encoded by the nuo operon. But, in the absence of ATP synthase buy MK-2206 coupled to the electron transport chain, the whole consortium relies on substrate-level phosphorylation as a source of ATP. Acetyl-CoA can also be a source of ATP thanks to the presence of the genes ackA and pta. The consortium also shares with other endosymbiotic bacteria with reduced genomes the incapability to synthesize nucleotides de novo. T. princeps has completely lost all genes involved in this function, while M.

Methylation analysis showed the presence of this website derivatives of terminal Galp, terminal Manp, 2-substituted Manp, 3-substituted Manp, 6-substituted www.selleckchem.com/products/gdc-0994.html Manp, and 2,6-substituted Manp. The spectrum was recorded in D2O at 25°C, relative to the HOD signal at 4.78 ppm. Chemical shifts were assigned utilizing DQF-COSY, TOCSY, ROESY, HSQC, and HMBC experiments (Table 2). Anomeric configurations

were assigned on the basis of the chemical shifts of the 3 J H-1, H-2 values, which were determined from the DQF-COSY experiment, and from the shifts of 1 J C-1, H-1 values derived from a coupled 1H,13C-HSQC. Based on the TOCSY MI-503 price spectrum from the H-2 proton signal for all the spin systems, it was possible to assign all of the resonances, and from these, all the 13C resonances from the HSQC spectrum. Table 2 1H and 13C NMR data of the galactomannan fraction from Histophilus somni 2336 Residue 1 2 3 4 5 6 2-Manp 5.28 4.10 3.91 3.72 3.71 3.87, 3.72   101.2 79.3 71.0 67.4 75.4 61.8 3-Manp 5.16 4.21 3.88 3.65 3.76 3.89, 3.74   103.2 71.1 79.1 66.0 75.3 62.0 2,6-Manp 5.13 4.22 3.87 3.60 3.76 3.88, 3.73   99.2 79.1 71.1 66.1 74.6 68.0 2,6-Manp 5.10 4.03 3.93 3.69 3.80 4.00, 3.70   99.2 79.6 71.5 67.8 74.6 67.6 t-Manp 5.03 4.06 3.86 3.66 3.75 3.89, 3.71   103.2 71.0 71.2 67.5 76.4 62.1 t-Manp 5.04 4.20 3.93 3.62 3.86 3.89, 3.71   103.2 70.1 70.7 67.9 76.4 62.1 6-Manp 4.89 3.98 3.82 3.71 3.88 3.91, 3.73   100.6 70.6 71.0 67.3 74.8 66.5 t-Galp 4.52 3.32 3.48 3.87 3.84 3.84,

4.21 In the low field anomeric region several signals were present, all identifiable as mannose spin systems (low 3 J H-1, H-2 Resveratrol and 3 J H-2, H-3 values) experiencing a different magnetic environment. At 5.28 ppm a cluster of signals were present, all indicative of 2-substituted mannose residues. In fact, 13C resonance assignments showed the downfield displacement of a C-2 resonance for the spin system, evidently due to glycosylation. Furthermore, at 5.16 ppm a cluster of signals indicated that a 3-substituted mannose was present, as attested by the downfield shift of C-3 resonance at 79.1 ppm. At 5.13 and 5.10 ppm two very similar spin systems were found. Both residues possessed C-2 and C-6 chemical shifts at low fields owing to glycosylation, and were therefore identified as two distinct clusters of 2,6-di-subtituted mannose residues that experienced a slightly different magnetic environment.

Predisposed risk for retained uterine products includes history of previous curettage, cesarean section, multiple births or endometrial infection or

injury [15]. If the placenta has not been delivered within 15-30 minutes of childbirth or in cases suspicious for retained placental fragments, the placenta must be retrieved [7]. Golan and colleagues, 1983 [15], showed success of medical management by injecting 10 IU of oxytocin directly into the umbilical vein. Providing bleeding cessation in 10 of 10 patients treated for PPH due to delayed (>30 min) expulsion of placenta. If this umbilical vein injection is bypassed, or not successful, adequate regional anesthesia or general anesthesia should be ensured; current hemostatic parameters should be reassessed with cross-matched blood available, broad spectrum antibiotics administered and an oxytocin drip (40 IU oxytocin in 500 mL of 0.9% saline, at 125 Cyclosporin A nmr mL/hr) should be started before attempting to remove retained uterine products. The best way to remove retained products is to approach transvaginally, finding the plane between the placenta and uterine wall then gently separate the placental parts from the uterus sweeping the surgeon’s AZD1480 datasheet fingers in a side-to-side motion. After this has been completed, the uterine cavity should again be checked to ensure it is empty [11].

Injuries to the genital tract may produce severe bleeding, a quantity that may be unexpected to the inexperienced. Optimal repair includes correct positioning of the patient to allow for adequate vision and access of surgical instruments. In order to gain effective control of the bleeding, the injured area should be sutured, starting at the apex of the tear. If the apex cannot be reached, the suture should be started as close to the apex as possible, then, once the remainder of the tear has been approximated, place traction Resveratrol to reach the previously hidden apex. If there is extensive trauma to the vaginal wall, with multiple lacerations, Compound C price bruising and oozing repairs, vaginal packing to provide hemostasis should be placed and maintained for 12-24 hours [11]. Vaginal

packing consists of gauze tape, roller gauze or gauze 4 × 4′s that are tied end to end, placed loosely at first, then more tightly in subsequent layers using a ring or dressing forceps to create a mass the size of a softball. It is important to ensure foley catheter has been placed to allow an outlet for urination in addition to monitoring of urine output [16]. Failure of Hemorrhage Control If postpartum hemorrhage has not been controlled at this point the patient should be emergently moved to the labor and delivery OR suite, notifying the anesthesia provider, the blood bank (of the possibility for massive transfusion protocol) and the following staff, if available: Staff General/Trauma surgeon, senior general surgery residents, the patient’s nurse and any available nurse’s assistants.

This truncated protein product would include the entire rhodanese-homology domain and approximately half of the chromate-resistance protein domain. One possibility is that the competitive

advantage that the www.selleckchem.com/products/ch5424802.html SMc00911-insertion mutant strains have against the 1021 wild type strain is due to the expression of this truncated protein, rather than simply a loss-of-function of the full-length protein. Even though SMc00911 is annotated as a “SodM-like” protein in the NCBI database [53, 54, 56], there are only two short segments of similarity KU55933 clinical trial (8 amino acids [38% identity] and 11 amino acids [36% identity]) with a protein confirmed to be a SodM from Xanthomonas campestris pv. campestris (accession no. p53654) [57]. Thus, since the N-terminal similarity of SMc00911 to the GlpE sufurtransferase/rhodanese homology domain and the C-terminal similarity to the chromate-resistance protein domain are both greater than the similarity of this protein to SodM, “SodM-like” may not be the most-appropriate annotation for this ORF. There are two sod ORFs in the S. meliloti

1021 genome, sodB (SMc00043) (SMc02597) and a bacteriocuprein-family sodC (SMc02597) [2, 53, 54]. An S. meliloti 1021 sodB loss-of-function mutant forms Ilomastat in vivo a functional symbiosis with host plants [58], while the symbiotic phenotype of a sodC mutant has not been reported. Expression of other αhizobial conserved ORFS Although they are not required for development of a functional symbiosis by S. meliloti 1021, the ORFs SMb20360 and SMc00135 are also

strongly expressed in nodules, while SMc01562, SMc01266, SMc03964 and the SMc01424-22 operon are moderately expressed (Figure 4; Table 3). However, Calpain the expression of SMc00135 is not specific to the nodule (Figure 4 and Additional file 5). SMb20360 is predicted to encode a protein of the Clp-protease superfamily (COG0740), with specific similarity to ClpP [52]. Polar localization of the ClpXP protease complex within S. meliloti cells has been found to be important for S. meliloti bacteroid differentiation [59], and it is possible that ClpP proteases play a role in the bacteroid differentiation process. Interestingly, in another study, a signature-tagged mutant in SMb20360 was found to be highly competitive for survival, in the free-living state, in competition experiments under salt- and detergent-stressed conditions [60]. SMc01562 is predicted to encode a member of the GYD-domain containing protein superfamily (COG4274) [52]. No function has been reported for this protein family [56]. SMc01266 is predicted to encode a member of the Von Willebrand factor type A (vFWA) superfamily (cl00057), however proteins containing a vFWA domain participate in a wide variety of functions [61].

3.2 [74]. The number of clusters K was estimated by calculating the ad hoc statistic ΔK[76]. ΔK was calculated for K = 1 through 10 using 5 Markov chains for each value of K. The simulations of Evanno et al. [76] showed that the highest value for ΔK reliably identified the optimum DNA-PK inhibitor value of K. Chains were run for 500,000 steps following an initial

burn-in of 100,000 steps, using the admixture ancestry and correlated allele frequency models. Once the optimum value of K was identified, strains were assigned to clusters using assignment coefficients (proportion of cluster membership) generated from an additional run utilizing the linkage ancestry and correlated allele frequency models. A study of recombinant bacterial populations showed the linkage model of ancestry to produce the most accurate assignment scores in situations where there are multiple linked loci along contiguous sections of DNA [75]. The model assumes these sections, which could be recombinant, to be discrete units of inheritance. Markov chains were run see more for 2,000,000 steps following an initial burn-in of 500,000 steps. Acknowledgements We would like to thank staff from Cornell

University’s Quality Milk Production Services and Animal Health Diagnostic Centre for their contribution to sample and isolate collection. This study made use of PathogenTracker 2.0 ( http://​www.​microbtracker.​net), developed by Martin Wiedmann. This work was supported by the National Institute of Allergy and Infectious Disease, U.S.

National Institutes of Health, under Grant No. AI073368 awarded to M.J.S. Electronic supplementary material Additional file 1: Torin 1 order Streptococcus RefSeq genome summary statistics. (DOC 102 KB) Additional file 2: S. canis annotation. (XLS 540 KB) Additional file 3: Additional Streptococcus genomes. (XLS 30 KB) Additional file 4: Insertion sites of putative integrative plasmid. (DOC 58 KB) Additional file 5: S. canis isolate MLST allele data. (DOC 87 KB) Additional file 6: Ln P(D) scores for Structure analysis. (DOC 206 fantofarone KB) Additional file 7: MLST PCR primer details. (DOC 118 KB) Additional file 8: Putative integrative plasmid PCR primer details. (XLS 24 KB) References 1. Devriese LA, Hommez J, Kilpper-Balz R, Schleifer KH: Streptococcus canis sp. nov.: a species of group G streptococci from animals. Int J Syst Bacteriol 1986,36(3):422–425.CrossRef 2. Vandamme P, Pot B, Falsen E, Kersters K, Devriese LA: Taxonomic study of Lancefield streptococcal groups C, G, and L ( Streptococcus dysgalactiae ) and proposal of S. dysgalactiae subsp. equisimilis subsp. nov. Int J Syst Bacteriol 1996,46(3):774–781.PubMedCrossRef 3. Murase T, Morita T, Sunagawa Y, Sawada M, Shimada A, Sato K, Hikasa Y: Isolation of Streptococcus canis from a Japanese raccoon dog with fibrinous pleuropneumonia. Vet Rec 2003,153(15):471–472.PubMedCrossRef 4.

The lower limit of quantification was 5.00 ng/mL. The between- and within-run precision for quality controls, expressed as CVs, were no greater than 7.40% and 8.16%, respectively, with deviations

from nominal concentrations of no more than 8.0%. The plasma 17-AAG methotrexate concentrations were analyzed by a non-compartmental method, and the following parameters were assessed: Cmax, tmax, t1/2,λz, AUCt, and AUC∞. Statistical Analyses All statistical analyses were conducted using SAS® version 9.1 software (SAS Institute Inc., Cary, NC, USA). For the pharmacokinetic analyses of the four clinical studies, the descriptive statistics analysis included arithmetic NU7441 price means and CVs for Cmax, AUC, t1/2,λz, Ae24h, and CLR24h; the medians and ranges for tmax; and the geometric means and CVs for Rac(AUC) and Frel. Clinical safety was addressed by assessing AEs, physical examinations, laboratory assessments, ECGs, and vital sign results in a descriptive manner. Descriptive statistics and shift tables (according to normal ranges) were calculated for each parameter at every timepoint and in each treatment group. A treatment-emergent AE analysis selleck was performed. The following inferential statistics were performed

for each study, with a statistical significance level of p < 0.0500. Study 1 Dose proportionality was tested on dose-normalized and natural log–transformed GLPG0259 parameters (Cmax normalized to a 1 mg dose [Cmax/dose] and AUC from 0 to 24 hours [AUC24h] normalized to a 1 mg dose [AUC24h/dose]) after single fed dosing by means of mixed-effects analysis of variance (ANOVA) with the cohort and dose as fixed effects and the subject (nested within the cohort) as a random effect. In the case of a significant dose effect being observed on the parameters listed above, comparison between doses was performed using Tukey’s test. The tmax, being a discrete variable, was analyzed using a non–parametric Kruskal-Wallis test to assess the dose proportionality. For part 2, a mixed-effects ANOVA was performed on natural log–transformed SB-3CT GLPG0259 parameters (Cmax/dose, AUC24h/dose, t1/2,λz, Ae24h, and CLR24h) with the day, dose, and

day-by-dose interaction as fixed effects and the subject as a random effect. Dose proportionality for Rac(AUC) was evaluated from the adapted mixed-effects ANOVA of AUC24h/dose. A Wilcoxon–Mann-Whitney non-parametric test was used to assess the dose proportionality of tmax. The time to reach steady state was assessed by visual inspection of the trough plasma drug concentrations as well as by means of a mixed-effects ANOVA on Ln-transformed GLPG0259 trough plasma drug concentrations. Comparison between days was performed using Tukey’s test. The food effect was assessed using geometric mean ratios of the observed pharmacokinetic parameters (Cmax, AUC24h, AUC∞, and t1/2,λz) for GLPG0259, with and without food, and the corresponding 90% confidence intervals (CIs) for the ratios.

The post-exercise period is often considered the most critical part of nutrient timing. An intense resistance training workout results in the depletion of a significant proportion of stored fuels (including glycogen and amino acids) as well as causing damage to muscle fibers. Theoretically, consuming the proper ratio of nutrients during this time not only initiates the rebuilding of damaged tissue and restoration of energy reserves, but it does so in a supercompensated fashion that enhances both body composition and exercise performance. Several researchers have made reference check details to an “anabolic

window of opportunity” whereby a limited time exists after training to optimize training-related muscular adaptations [3–5]. However, the importance – and even the existence – of a post-exercise ‘window’ can vary according to a number of factors. Not only is nutrient timing research open to question in terms of applicability, but recent evidence has directly challenged the classical view of the relevance of post-exercise nutritional intake on anabolism. Therefore, the purpose of this paper will be twofold: 1) to review the existing literature on the effects of nutrient

timing with respect to post-exercise muscular adaptations, and; 2) to draw relevant conclusions that allow evidence-based nutritional recommendations to be made for maximizing the anabolic response to exercise. Glycogen repletion A primary goal of traditional post-workout Selleck HDAC inhibitor PD184352 (CI-1040) nutrient timing recommendations is to replenish glycogen stores. Glycogen is considered essential to optimal resistance training performance, with as much as 80% of ATP production during such training derived from glycolysis [6]. MacDougall et al. [7] demonstrated that a single set of elbow flexion at 80% of 1 repetition maximum (RM) performed to muscular failure caused a 12% reduction in mixed-muscle glycogen concentration, while three sets at this intensity resulted in a 24% decrease. Similarly, Robergs et al. [8] reported that 3 sets of 12 RM performed to muscular

failure resulted in a 26.1% reduction of glycogen stores in the vastus lateralis while six sets at this intensity led to a 38% decrease, primarily resulting from glycogen depletion in type II PARP activation fibers compared to type I fibers. It therefore stands to reason that typical high volume bodybuilding-style workouts involving multiple exercises and sets for the same muscle group would deplete the majority of local glycogen stores. In addition, there is evidence that glycogen serves to mediate intracellular signaling. This appears to be due, at least in part, to its negative regulatory effects on AMP-activated protein kinase (AMPK). Muscle anabolism and catabolism are regulated by a complex cascade of signaling pathways.

These connected components were then counted to determine the size of the core proteome. It is important to note that the size of the core proteome was defined in terms of the HSP targets number of orthologous groups, not in terms of the total number of individual proteins (from one specific

organism) in those www.selleckchem.com/products/GSK1904529A.html groups. For example, suppose that we were finding the size of the core proteome for a genus with eight isolates, and that there were 500 orthologous groups containing proteins from all eight of those isolates. Further, suppose that each of these groups actually contained ten individual proteins (say, with six isolates having one protein each, and two isolates having two each). Then the size of the core proteome would be reported as 500, not as 500 × 10 = 5000. Unique proteomes were found BKM120 supplier in a similar manner–by counting the number of connected components that contained proteins from all members of a particular group, but in no members of a second group. Finally, the number of singlets in a particular genus was found by performing orthologue detection on the proteins from that genus (only), and identifying the number of connected components containing

just a single protein. Most comparisons done in this study involved a fairly small number of isolates (and therefore proteins). For example, finding the core proteome of a particular genus involved performing orthologue detection for the isolates of that genus (between 4 and 31 isolates, depending on the genus), each

of which had a proteome containing around 1000 to 9000 proteins. However, one type of comparison–finding the proteins unique to each genus–required finding orthologues among all proteins in the proteomes of all isolates used in this study. Due to memory constraints, this could not be done using a single orthologue detection comparison. Instead, comparisons were performed between all possible pairs of genera. Lenvatinib molecular weight For example, in finding the proteins unique to genus A, we first determined the list of proteins in all isolates of genus A, but no isolates of genus B; we then determined the list of proteins found in all isolates of A, but no isolates of C, and so on. Once all lists had been calculated, the proteins that were present in every list were the proteins unique to genus A. Comparison of proteomic similarity with 16S rRNA gene similarity To determine 16S rRNA gene percent identities, the 16S rRNA gene was obtained from each sequenced genome used in this study and the RDP10 tool [49] was used to align sequences based on known conserved and variable regions according to the rRNA’s secondary structure. The percent identity of the 16S rRNA gene between pairs of isolates from the same genus was calculated to the nearest 0.01%.