e., misclassification does not depend on cohort), the study results for the measure of nonvertebral sites and for vertebral sites are likely more attenuated by misclassification than results at the hip. In conclusion, for this large

observational study of more than 200,000 bisphosphonate patients, the apparent differences in the baseline incidence of hip fractures among the alendronate, risedronate, and ibandronate cohorts likely reflect differences in the risk profile of patients prescribed each bisphosphonate. Statistical adjustments could not account for these differences and therefore the design of epidemiological studies should be see more given careful consideration to account for these differences. Relative to the baseline fracture incidence, the longitudinal analyses indicated that alendronate and risedronate decreased nonvertebral and hip fractures over time, whereas ibandronate did not. All three bisphosphonates decreased vertebral fractures. The reductions selleck chemicals llc observed in fracture incidence over time within each cohort suggest that the effectiveness

of each bisphosphonate in clinical practice has been consistent with their efficacies demonstrated in randomized controlled trials. Acknowledgement Funding by The Alliance for Better Bone Health (Procter & Gamble Pharmaceuticals and sanofi-aventis). Conflicts of interest Dr. Abelson reports receiving consulting fees from NU7026 price sanofi-aventis, Procter & Gamble, Novartis; serving on speaker’s bureaus for Amgen, Procter & Gamble, Roche, Novartis, and sanofi-aventis. Dr. Gold reports receiving consulting or advisory committee fees from Amgen, Eli Lilly, GlaxoSmithKline, Merck, Procter & Gamble, Roche, sanofi-aventis; serving on

Tenoxicam speaker’s bureaus for Amgen, Eli Lilly, GlaxoSmithKline, Procter & Gamble, Roche, and sanofi-aventis. Dr. Thomas reports receiving consulting or advisory committee fees from Amgen, Daïchi-Sankyo, Ipsen, Lilly, MSD, Novartis, Procter & Gamble, Roche/GlaxoSmithKline, sanofi-aventis, and Servier; grant support from Lilly, MSD, Nicomed, Novartis, Procter & Gamble, sanofi-aventis, and Servier. Dr. Lange is an employee of Procter & Gamble. Open Access This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. References 1. Avorn J (2007) In defense of pharmacoepidemiology—embracing the yin and yang of drug research. N Engl J Med 357:2219–2221CrossRefPubMed 2. Perreault S, Dragomir A, Blais L et al (2008) Population-based study of the effectiveness of bone-specific drugs in reducing the risk of osteoporotic fracture. Pharmacoepidemiol Drug Saf 17:248–259CrossRefPubMed 3. Langsetmo LA, Morin S, Richards JB et al (2009) Effectiveness of antiresorptives for the prevention of nonvertebral low-trauma fractures in a population-based cohort of women. Osteoporos Int 20:283–290CrossRefPubMed 4.

This could indicate a problem with compliance. However, participants took 100,000 IU under supervision, and exactly the same pattern is observed in the 800 IU group and the sunlight group. This may indicate that supplementation was inadequate. A dose-finding study in nursing home residents SB431542 concentration studied with the same 25(OH)D assays showed that serum 25(OH)D was higher than

50 nmol/l with vitamin D 600 IU/day in 90% of the participants [33]. This fact and the decrease in serum 25(OH)D between 3 and 6 months (Fig. 2, Table 2) indicate a compliance problem. Another point of concern is the interaction of the increase of serum 25(OH)D after supplementation with BMI, mainly in the 100,000 IU group. Although this analysis should be considered exploratory, SB202190 it may indicate that overweight and obese persons will need higher supplementation doses. The negative relationship between body fat percentage and serum 25(OH)D has been reported in the Longitudinal Aging Study Amsterdam [34]. It is striking that PTH concentrations decreased most in the100,000 IU group, although serum 25(OH)D concentrations increased most in the 800 IU group. This might be due to a higher peak concentration of serum PTH in the 100,000 IU group. The mean serum alkaline Go6983 datasheet phosphatase decreased in all groups by about 20%. The high

alkaline phosphatase is a sign of high bone turnover or disturbed mineralization due to vitamin of D deficiency. Besides serum 25(OH)D and PTH concentrations, several clinical outcomes were studied. An improvement in physical performance was not observed. Difficulties with daily life activities decreased significantly, but no differences were observed between the interventions. This may indicate that only a small improvement in vitamin D status is needed to improve functional limitations. Reported pain was not consistent over time or between interventions: number of days with headache episodes decreased

significantly among participants in the 800-IU intervention and reported pain in upper legs improved significantly in the 100,000-IU intervention compared to the advised sunlight intervention, but no improvement was observed in shoulder pain. The inconsistent clinical results can be explained by the methodological restrictions of this study. There was no placebo-control group as this was judged unethical in this vitamin D-deficient population. Handgrip strength is known to be positively correlated with both lower-extremity and upper-body strength, and it appears to be a reliable test [35, 36]. The chair stand test is reliable and related to vitamin D status [14], but both relationships have been established in older populations. The impact of vitamin D deficiency on muscle strength could be less in younger persons than in older persons. In addition, the tests could not be sufficiently discriminative in a younger population.

Acknowledgements This study was supported by the Glacier Water Company, LLC, Auburn,

WA 98001.”
“Background A randomized, double-blind, placebo-controlled study was performed to evaluate the effect of adding protein (PRO) to buy BAY 80-6946 a recovery mixture on exogenous and Anlotinib ic50 endogenous substrate oxidation during post-recovery exercise. Many studies have shown that carbohydrates (CHO) effectively restore glycogen post-exercise [1]. Some have also suggested that the addition of PRO to a CHO drink may produce further improvements [2]. CHO and PRO ingestion during recovery may result in higher CHO oxidation during subsequent exercise, which may be more beneficial to endurance performance because of preservation of endogenous substrates [3]. Methods With institutional ethics approval six well-conditioned men [age: 34.0 yrs ± 8.2; body mass (BM): 75.6 kg ± 7.1; max: 62.5 ml•kg BM-1•min-1 ± 6.5] completed a depletion protocol, followed DihydrotestosteroneDHT cell line by a 4-hour recovery period, and a subsequent 60 min cycle at 65% max on 3 occasions. During recovery subjects ingested either a placebo (PL), MD+13C-GAL+PRO (highly naturally enriched maltodextrin, 13C-labelled galactose, whey protein hydrolysate, L-leucine, L-phenylalanine; 0.5 +0.3 +0.2 +0.1 +0.1 g•kg BM-1•h-1) or MD+13C-GAL (0.9

+0.3g•kg BM-1•h-1) drink. O2 consumption (L/min) and CO2 production (L/min) were analyzed using breath-by-breath methodology (Metalyzer 3B, Cortex, Leipzig, Germany). Samples of expired air for determination of the 13C enrichment were collected every 15 min of the post-ingestion

exercise. Data expressed as means ± s. Statistical significance set at p ≤ 0.05. Results The mean rate of exogenous CHO oxidation (g·min-1) after MD+13C-GAL vs. MD+13C-GAL+PRO was: 1.80 ± 0.26 GNA12 vs. 1.60 ± 0.18 (at 15 min), 1.85 ± 0.17 vs. 1.61 ± 0.17 (at 30 min), 1.88 ± 0.13 vs. 1.59 ± 0.20 (at 45 min), and 1.81 ± 0.12 vs. 1.47 ± 0.22 (at 60 min), respectively. The mean rate of endogenous CHO oxidation (g·min-1) after MD+13C-GAL vs. MD+13C-GAL+PRO was: 1.33 ± 0.21 vs. 1.66 ± 0.31 (at 15 min), 0.95 ± 0.31 vs. 1.27 ± 0.40 (at 30 min), 0.72 ± 0.25 vs. 1.47 ± 0.20 (at 45 min), and 0.78 ± 0.26 vs. 1.64 ± 0.22 (at 60 min), respectively. Differences between conditions were statistically significant at 45 and 60 min (p < 0.02). 38.8% of the total ingested CHO dose was oxidized after MD+13C-GAL+PRO, which was 8.5% higher than in the MD+13C-GAL trial (30.3%). The contribution of exogenous CHO, endogenous CHO and fat towards the total energy expenditure was: 0, 38.6, 61.4% (PL), 40.7, 20.7, 38.6% (MD+13C-GAL), 34.2, 33.1, 32.7% (MD+13C-GAL+PRO), respectively. Conclusion These results suggest that the inclusion of PRO in the mixture results in a higher amount of total CHO oxidized. However, at the same time adding PRO to the drink seems to increase endogenous CHO oxidation and decrease exogenous CHO and fat oxidation.

Under laboratory conditions, the mosquitoes were reared in hygienic and controlled conditions whereas, reverse is true for the field conditions. Hence, the larvae in field are more exposed to the microbial flora of the open water than their counterparts in the laboratory. Larvae being filter feeders ingest the water in immediate vicinity irrespective of their preference. Similarly, adult mosquitoes feed on uncontrolled natural diet, while laboratory-reared mosquitoes were fed with sterile glucose solution and resins. Even the blood offered to female mosquitoes in laboratory is from infection-free rabbit; on the other hand, the blood meal in field is good

source of various infections. Thus, field-collected mosquitoes have more chances of having diverse gut flora as was observed. Mosquitoes are known to elicit specific immune responses against parasites [3, 4, www.selleckchem.com/products/etomoxir-na-salt.html 42]. Some of these immune responsive genes are expressed in response to bacteria and this raises the possibility that the presence of specific bacteria in the gut may have an effect on the efficacy at which a pathogen is transmitted by a vector selleck kinase inhibitor mosquito [9]. In previous studies Selleck EPZ015666 of lab-reared A. stephensi adults, it was demonstrated that great number of S. marcescens were found in the midgut of the insects, but was not found in larvae and pupae [10]. In another study, it was observed that Plasmodium vivax load in A. albimanus

mosquitoes co-infected with E. cloacae and S. marcensces were lower (17 and 210 times respectively) than control aseptic A. albimanus mosquitoes with Plasmodium vivax infection (without E. cloacae and

S. marcensce). In our study, we also observed that a relatively high number of S. marcescens (35 isolates from lab-reared male/female and 48 clones from field-collected female/larvae) were identified from lab and field- populations of A. stephensi. However, none S. marcescens species were identified from field- collected male A. stephensi. At this point it is premature to draw correlation between the occurrences Carnitine palmitoyltransferase II of S. marcensce and pathogeneCity or vector load. However, previous reports suggest that mortality in S. marcensces-infected A. albimanus mosquitoes was 13 times higher compared with the controls [12]. The present study assumes importance in the light of earlier studies which suggested that the composition of midgut microbiota has a significant effect on the survival of dengue (DEN) viruses in the gut lumen [43]. The overall susceptibility of Aedes aegypti mosquitoes to dengue viruses increased more than two-folds, with the incorporation of bacterium Aeromonas culicicola. However, the increase in susceptibility was not observed when the antibiotic-treated A. aegypti mosquitoes were used, indicating that A. aegypti mosquito midgut bacterial flora plays a role in determining their capaCity to carry viral load to the virus [43].

The animals were pair-fed (15 to 20 g/day) AIN-93 M powdered diet, as recommended [30], and received distilled water ad libitum. The principles of laboratory animal care (NIH publication No. 86-23, revised 1985) were followed, as well as the specific MK 8931 concentration national laws (n° 9.605/1998). All procedures were approved by the Ethics Committee of the

Federal University of Viçosa, Brazil. Creatine and caffeine supplementation Every day, the animals from the groups SCr and ECr were supplemented with creatine, while those from the groups SCrCaf and ECrCaf received creatine plus caffeine. Creatine was given using a two-stage procedure: loading and maintenance. During the loading stage (7 days), in the first week, a dosage of 0.430 g of powdered creatine monohydrate (Sigma) per kg of body weight per day was added to 15 g of the diet (AIN-93 M powdered diet) and given to the groups SCr, ECr, SCrCaf and ECrCaf. The maintenance stage lasted 5 weeks, MEK inhibitor starting from the second week, and a dosage of 0.143 g of creatine/kg body weight/day was added to 15 g of the diet and given to the groups SCr, SCrCaf, ECr and ECrCaf. LY3009104 From the second to the sixth week, a dosage of 10 mg of powdered

caffeine (Sigma) per kg body weight per day was given to animals from the groups SCaf, SCrCaf, ECaf and ECrCaf. Animals from the groups SPl and EPl received diet only. From the fourth week on, all animals received 20 g of the diet every day. Exercise training protocol During the first week, the

animals from the groups EPl, ECr, ECaf and ECrCaf swam for 30 min/day Reverse transcriptase in a tank (60 cm wide, 75 cm long, 80 cm deep) filled with water at 32 ± 1°C to adapt to the environment. The exercise training regime comprised vertical jumps from the bottom of the tank to the surface water. To augment the exercise intensity, an external load (% of body weight) was added to the animal by using plumber spheres in a lycra vest. The deepness of water was determined by an average percentage of the animals’ length (i.e. distance between the end of the posterior members and the nostril) (Table 1). The training program was conducted from the second to the sixth week of the experiment and the animals performed 4 sets of 10 jumps with 1 minute recovery time between sets, 5 days/week (Table 1). This exercise training regime and the working apparatus are currently used in our laboratory and elsewhere [31]. During the last training session, concentrations of blood lactate of the exercised animals were monitored in three moments.

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Right sided tears are significantly less likely than left sided tears because of the protective effect of the liver [2, 16, 27]. This could also be explained by better visualisation of the left diaphragm, on diagnostic laparoscopy, but restricted visualisation of the right diaphragm [28]. The systematic review of literature

has confirmed 27 cases of left sided rupture [4, 8, 11, 13, 16–19, 21, 22, 24, 26, 29, 30] and 13 cases of right sided selleck products rupture were reported [2–4, 7, 15, 24, 31–33]. The rarely reported sites include 1 check details central diaphragmatic hernia [20], 2 bilateral [12, 24] and 1 trans-diaphragmatic intercostal hernia [34] The systematic review of literature also confirmed intra abdominal and retroperitoneal contents in the hernial sac, which are summarised in the table below (Table 1) [35–37]. Table 1 Type of visceral herniation Sac Contents YH25448 mw No of cases References Strangulated Transverse Colon 1 [13] Perforated Transverse Colon 3 [16, 19, 21] Splenic flexure 2 [12, 18] Splenic flexure cancer 1 [4] Intrathoracic Splenosis 2 [8, 35] Spleen 2 [12, 22] Right hepatic lobe 6 [2, 7, 15, 31–33]

Small Bowel 1 [31] Stomach/Perforated gastric ulcer 6 [8, 12, 17, 26, 29, 30] Intra-thoracic gastric volvulus 2 [36, 37] Kidney, Ureter and Renal Vein 1 [7] Part of Ascending and Transverse Colon 1 [7] Gall Bladder

1 [7] Omentum/Mesentery 2 [20, 34] Investigations The studies published before 1996 have quoted that 12–69% of diaphragmatic ruptures are missed at the pre operative phase [38–40]. CT scan was not widely used investigation when Non-specific serine/threonine protein kinase these papers were published. However, with the introduction of reformatting of images the sensitivity of the CT scan in picking up the diaphragmatic rupture has significantly increased[41]. While audible bowel sounds on the chest auscultation suggests displaced bowel loops, a chest x ray is the first line of investigation, repeated imaging increases sensitivity[8]. Insertion of a naso-gastric tube can decompress the intra-thoracic stomach to delineate a chest x ray interpretation [8, 29] and increase the diagnostic sensitivity to approximately 75%[8]. The sensitivity of chest radiographs is 46% for left sided ruptures and 17% for right sided ruptures [42]. Helical CT with axial, sagittal and coronal reconstruction increases the sensitivity to 73% and the specificity to 90%[12]. A diagnostic laparoscopy and/or diagnostic thoracoscopy could be performed as a semi-elective procedure, the timing planned in accordance with the heamodynamic and respiratory status of the patient [27, 28]. Meticulous inspection and palpation of the diaphragm should be performed during laparotomy in patients with trauma [12].

A hypothetical protein (MAP0860c) upregulated in the presence of iron in the cattle strain of MAP has been described as a part of MAP-specific large sequence polymorphism (LSP4) [22]. Table 3 Transcript and protein expression in cattle MAP under iron-replete (HI) conditions   MAP ORF ID Predicted function aFold change       Protein Transcript Metabolism   MAP0150c FadE25_2 (acyl-coA dehydrogenase) 1.72 ± 0.1 1.88 ± 0.2   MAP0789 acetyl-CoA acetyltransferase 1.73 ±

0.3 1.56 ± 0.1   MAP1846c ATP phosphoribosyltransferase 1.69 ± 0.2 3.68 ± 0.3   MAP2332c Fas (fatty acid synthase) 1.61 ± 0.5 2.28 ± 0.4   MAP3404 AccA3 (acetyl-/propionyl-coenzyme A) 1.45 ± 0.1 2.18 ± 0.2   MAP3698c succinate dehydrogenase 1.89 ± 0.3 4.57 ± 0.5 Cellular processes   MAP1339 iron regulated conserved protein 1.62 GF120918 supplier ± 0.2 0.78 ± 0.3   MAP1653 thiol peroxidase 1.79 ± 0.5 2.29 ± 0.2 Information storage and processing   MAP2907c translation initiation factor IF-2 1.57 ± 0.2 1.89 ± 0.2   MAP2945c ribosome releasing factor 1.66 ± 0.3 2.11 ± 0.5   MAP4113 50S ribosomal

protein L1 1.61 ± 0.1 1.57 ± 0.2   MAP4125 rplJ 50S ribosomal protein L10 1.52 ± 0.1 1.66 ± 0.5   MAP4142 fusA elongation factor G 2.13 ± 0.4 3.05 ± 0.3   MAP4160 rpsJ 30S ribosomal protein S10 1.68 ± 0.3 2.87 ± 0.4   MAP4181 rpsH 30S ribosomal protein S8 1.79 ± 0.5 2.42 ± 0.1   click here MAP4233 rpoA DNA-directed RNA polymerase 1.56 ± 0.1 1.65 ± 0.4 Poorly characterized pathways   MAP0216 FbpA antigen 85-A 1.87 ± 0.2 2.16 ± 0.3   MAP1122 mycobacterial ACP-196 integration host factor 1.73 ± 0.3 2.00 ± 0.5 a MAP oligoarray was used to measure gene expression whereas iTRAQ was used to quantitate protein expression in the cultures of cattle MAP strain grown in iron-replete (HI) or iron-limiting (LI) medium. Fold change for each target

was calculated and represented as a log2 ratio of HI/LI. Shown are the MAP genes that demonstrated the presence of 1.5 times or more of transcripts and proteins in HI compared to LI. Genes are annotated based on the motif searches in KEGG database. In contrast, we did not document any upregulation (at a log2 fold change of Decitabine 1.5) in the S MAP under iron-replete conditions. The directionality of transcripts as identified by microarrays under iron-replete conditions by S MAP strain was confirmed by real time RT-PCR (Additional file 1, Table S4). Proteome The following criteria were used for protein identification in each treatment – (1) peptides identified by mass spectrometry were searched against the non-redundant (nr) protein database deposited in NCBI); and (2) MAP specific peptides reported with >95% confidence were used to quantify the relative abundance (iron-replete v/s iron-limitation) of each protein. A peptide with no hits on the MAP genome but with identities with other mycobacterial proteins was considered as unannotated MAP protein.

In

our study, we precisely characterized the composition of quinoa chromosomes by exposing only 1 ms of dwell time to avoid the radiation damage. Here we have shown for the first time the advantages of utilizing atomic force microscopy (AFM) and scanning electron microscopy (SEM) for the morphological characterization (at the atomic and nanoscale level) and STXM for the compositional characterization (at the nanoscale level) of chromosomes. The morphology and the biochemical properties inside a single quinoa chromosome were determined by utilizing nanoscale imaging tools such as STXM, AFM, SEM, and confocal laser scanning microscopy (CLSM). Methods Root tip preparation Chromosomes were isolated from the meristematic tissue of quinoa root tips. Seeds of Chenopodium quinoa were germinated on moist Ilomastat solubility dmso filter papers in petri dishes at room temperature in

EPZ015938 manufacturer the dark over 48 h. For cytogenetic CBL0137 mouse analysis, primary root tips were pretreated with 2 mM 8-hydroxyquinoline for 4 h at room temperature, followed by incubation in ice-cold water overnight, fixed in methanol-glacial acetic acid (3:1 ratio), and stored at -4°C for further use. Cell suspension About 2-mm meristematic tips from each root were removed followed by dissection into the smallest possible sections. The root tip sections were macerated in a 200-μL enzyme reaction mixture for 4 h at 37°C. After the incubation time, the solution was filtered through a 50-μm gauze twice.

To this filtered solution, 2 ml of 75 mM KCl solution was added. This suspension was centrifuged for 70 min at 20°C at 760 rpm. The supernatant was discarded and the precipitate was re-suspended in 3 ml of the 3:1 fixative (methanol: acetic acid) and again centrifuged for 7 min at 760 rpm/75 g at 20°C. The above process was repeated five times. After discarding the supernatant from the final wash, the resulting pellet was re-suspended in 200 μL of the 3:1 fixative. AFM imaging In an attempt to prepare a full set of chromosomes, the samples were prepared not from the cell Immune system suspension but using the maceration technique reported by Neethirajan et al. [14]. Briefly, the pretreated quinoa root tips were incubated in an enzyme solution of 2% cellulase, 2% pectolyase, and 1.5% macerozyme for 90 min at 37°C, followed by squashing on the glass slides by tapping with the tip of forceps in 30% acetic acid. The squashed specimens were further cleaned using 1X SSC to remove the cellular debris, before being imaged using AFM. The samples were first observed with an inverted phase contrast optical microscope (Nikon Eclipse Ti, Nikon Instruments, Tokyo, Japan) and photographed to determine the location of the chromosomes to be studied by AFM. The glass slides were marked underneath as a possible region of interest for AFM imaging.

In red (⋆), the A. salmonicida subsp. salmonicida cluster; in green (●), the A. salmonicida subsp. achromogenes cluster; in blue (), the A. salmonicida subsp. smithia cluster; in pink (➜), the A. salmonicida subsp. masoucida cluster; and in brown (✪), A. popoffii strains clustering together.

Copy number of the IS630 LY2606368 element and RFLP among other Aeromonas species Other Aeromonas species revealed lower copy numbers of IS630: 5 in A. molluscorum, 5 to 8 in clinical A. sobria strains, 9 in A. veronii, 5 in A. allosaccharophila and A. media. Only one copy was found in A. bivalvium and a clinical strain of A. hydrophila. No signal for IS630 was obtained in A. caviae, A. trota, A. simiae, A. eucrenophila, A. ichthiosmia, A. jandaei, A. culicicola, A. enteropelogenes, I-BET151 concentration A. bestiarum and the type strains of A. hydrophila and A. sobria. Among the 8 strains of A. popoffii we found 6 very distinct patterns. Analysis of IS630 abundance, localization and impact on the genome of Aeromonas species In order to study the origin of IS630 in A. salmonicida, we performed a profound analysis and comparison of published Aeromonas genomes (Additional file 2: Table

S2). The genetic environment of IS630 ZD1839 mouse copies in the A. salmonicida subsp. salmonicida A449 genome is shown in detail in Additional file 1: Table S1. About 148 loci or DNA sequences forming 108 complete or partial IS units were found in the chromosome of A. salmonicida subsp. salmonicida A449 and on the plasmids pASA4/pASA5 [GenBank: CP000644.1, CP000645.1 and CP000646.1]. IS630 (referred to as ISAs4 in the Genbank genome annotation

of A. salmonicida A449 and as ISAs7 in the corresponding manuscript [16]) was found to be present in 38 copies and was the most abundant family representing AZD9291 cost 35% of transposons in A. salmonicida A449 (Figure 3, Additional file 3: Table S3). The different copies are well-conserved and show 98% nucleotide sequences identity. The other 70 IS elements are ISAs7 (13%), ISAs5 (11%), ISAs6 (6%), ISAs11 (6%), ISAs2 (5%), ISAs9 (4%), ISAs8 (4%), and unclassified ISAs (16%) (Figure 3). 90% of the IS630 copies reside in chromosomal regions that are specific to A. salmonicida subsp. salmonicida and were not found in other Aeromonas. Interestingly most of these loci correspond to known genes in bacterial genera other than Aeromonas. This is the case for instance for the hypothetical gene ASA_1385 (homology to VOA_002034 of Vibrio sp. RC586) that is directly linked to IS630 in A. salmonicida subsp. salmonicida and is not found in other Aeromonads (Additional file 2: Table S2). In ISAs families other than IS630, 34 (31%) are directly adjacent to IS630 showing that 66% of A. salmonicida A449 transposons are associated to genomic domains of variability. In comparison to other Aeromonas sp., A.