1–1 mg/ml 0.01–1 mg/ml [81] KPL-1 Selleckchem EPZ015666 Iscador Qu, M, A Iscador P ML I IC50 0.1–0.3 mg/ml

1.94 mg/ml 141 ng/ml [22]   Iscador M, Qu, Abnobaviscum Fr Inhibition of proliferation 1 mg/ml 0,1–1 mg/ml [81]   Iscucin® A, M, P, C, Po, T, Qu, S Cytotoxicity 0.1 mg/ml [82]   Iscador M ML I No stimulation of cell proliferation 0.05–5 ng ML/ml 0.01–5 ng/ml [83] MCF-7 Iscador Qu, M, A Iscador P ML I IC50 0.09–0.12 mg/ml SBI-0206965 1.61 mg/ml 410 ng/ml [22]   Lektinol IC50 >10 ng ML I/ml [84]   Iscador Qu, M, P (max. 1 or 1.5 mg/ml) Inhibition of S-phase progression Induction of apoptosis   [85–87]   Iscador M Iscador P ML I Iscador Qu IC50 No influence 185 μg/ml no activity 0.003 μg/ml 0.0015–15 μg/ml [88, 89]   Viscotoxin isoforms (A1, A2, A3, B, 1-PS) Viscotoxin isoform U-PS GI50 LC50 0.02–0.8 μg/ml 0.6 to >1 μg/ml no activity [90]   ML I A chain Inhibition of proliferation 0.5

μg/ml [91]   ML I, ML II, ML III Inhibition of proliferation 1–10 ng/ml [91]   TNF & ML I (100 ng/ml) Potentiation of TNF-cytotoxicity   [92]   Lektinol IC50 0.003 μg/ml [93]   Helixor P ML I IC50 > 150 μg/ml 0.086 μg/ml [94]   Iscucin M, P, C, Po, T, Qu, S Iscucin A, Pi Cytotoxicity 0.1 mg/ml no activity [82] MCF-7/ADR Lektinol IC50 (SRB assay) 0.3 E-4 μg/ml [93] MAXF 401NL Helixor P ML I IC50 0.66 μg/ml 0.003 μg/ml [94]   Iscador M Iscador P ML I Iscador Ferroptosis inhibitor Qu IC50 >70% growth inhibition < 3 μg/ml no activity 0.353 E-4 μg/ml 10 μg/ml [88, 89] MAXF 401 Lektinol IC50 < 0.1 E-4 μg/ml [93] MAXF 1162 Lektinol IC50 < 0.1 E-4 μg/ml [93] MAXF 449 Lektinol IC50 0.2 E-4 μg/ml [93] MAXF MX1 Lektinol IC50 < 0.1 E-4 μg/ml [93] MDA-MB-231 Lektinol IC50 0.7 E-4 μg/ml [93]   Helixor P ML I IC50 135 μg/ml 0.041 μg/ml [94] MDA-MB-468 Helixor P ML 1 IC50 47

μg/ml Rucaparib 0.006 μg/ml [94] MDA-MB-486-HER2 Iscador M Inhibition of epidermal growth factor-induced proliferation 0.5 μg/ml [95] Colo-824 Iscador M ML I No stimulation of cell proliferation 0.05–5 ng ML/ml 0.01–5 ng/ml [83] HCC-1937 Iscador Qu, M, A Iscador P ML I IC50 0.1 to 0.3 mg/ml 2.14 mg/ml 320 ng/ml [22]   Iscucin A, M, P, C, Po, T, Qu, S Cytotoxicity 0.1 mg/ml [82] BT474 Helixor M, A Cytotoxicity (WST-1) Maximum (80 and 100%) with 25 mg/ml [96] Primary breast cancer Iscador M, Qu Abnobaviscum Fr Mitochondrial activity (MTT) 50–80% with 0.1–0.001 mg/ml [81]   Abnobaviscum M Inhibition of proliferation 0.5–50 μg/ml [97]   ML I Inhibition of proliferation 1–50 ng/ml [20, 98] T47D ML I, II, III IC50 > 0.1 – 1 ng/ml [99]   ML I A-chain Inhibition of proliferation 10 ng/ml [91] BT549 ML I A-chain Inhibition of proliferation 500 ng/ml [91] HBL100 ML I A-chain Inhibition of proliferation 100 ng/ml [91] Breast cancer cells ML II, ML III, viscotoxins Cytotoxicity   [100] Ovarian cancer OVXF 1619L Helixor P ML I IC50 119 μg/ml 0.100 E-3 μg/ml [94] OVXF 899L Helixor P ML I IC50 >150 μg/ml 0.229 μg/ml [94] SKOV-3 (HER-2 expression) Recombinant ML I IC50 Induction of apoptosis 0.033 ng/ml [101] OVCAR3 Iscador Qu, M (max.

This, together with the small thickness of the film, explains the low intensity of the Raman signal in our case. Thus, based on the data of all three characterization methods, we can state that in the sample of type

II, the SiO2 film is covered with approximately 1-nm-thick film consisting of sp 2 carbon-based highly disordered amorphous phase click here with some number of three-layer defective graphene inclusions. Possible reasons for greater disordering and the number of defects of the in the type II sample deposited carbon film as compared to the type I one can be the greater distance between the source and substrate as well as a lot more gases of air in the sandwich during the type II sample preparation. Substantial changes in the silicon oxide film indicate the significant impact of the atmosphere taking place during the fabrication of the type II sample. First, its thickness increased, and its refractive index decreased. Second, attention should be given to the silicon oxide film growth rate during the graphite sublimation process: the oxide thickness increase was 13.4 nm

in type II sample, but only 4.0 nm in the control Si-SiO2 sample placed in the oven near the quartz box. Such difference in the silicon oxidation rate can be explained by increase in the ‘source-substrate’ sandwich temperature. The increase in local temperature inside the sandwich is possible because the heating of graphite to 850°C in air should cause exothermic oxidation reactions with

oxygen and water molecules [23]. Authors [24] showed that exposure of a few layer graphene films LY3039478 ic50 in air at T ≥ 600°C leads to the formation of defects. The defects are initially sp 3 type and become vacancy-like at higher temperature [24]. Thus, the abovementioned facts make it possible to think that more defective structure of carbon deposit in the type II sample is to great extent caused by the greater amount of the active air gases (oxygen, water vapor) as well as the higher local temperature in the sandwich. All of this is the consequence of greater distance between the graphite plate and the substrate. Conclusions The possibility Idoxuridine of graphene fabrication using the simple and low-cost modified method of close space sublimation at the atmospheric pressure has been demonstrated. When carrying out carbon deposition under the same conditions, the thickness of several-layer graphene film decreases and its defectiveness selleck chemicals increases with increase in the distance between the source and the substrate. This motivates further in-depth study of the mechanism of the film formation in order to develop the technological regimes that would allow fabrication of the better graphene films. First of all, it would be necessary to determine the influence of the atmosphere on the graphene film deposition process. References 1. Castro Neto AH, Guinea F, Peres NMR, Novoselov KS, Geim AK: The electronic properties of graphene.

Conclusions 2-D PAGE studies might be extremely powerful for comparison of protein expression in different mycoplasma isolates, especially when considering that lipoproteins can be selectively

detected with this method, and that size and phase variations can be easily spotted through the application of powerful differential comparison approaches as the 2D DIGE. However, these need to be integrated with traditional Western immunoblotting and GeLC-MS/MS buy Belnacasan for a deeper coverage and characterization of other mycoplasmal surface immunogens to be used as tools for vaccination, diagnosis, and therapy. This combined approach allowed the identification and characterization of 194 M. agalactiae proteins putatively localized on the membrane or associated to it, providing useful insights on its composition. In the future, alternative approaches such as blue native electrophoresis and chemical crosslinking of surface proteins will also enable to elucidate functional and structural aspects of membrane proteins that cannot be accounted for by the traditional gel-based proteomic approaches. Methods Bacterial strains and culture conditions At least three replicate cultures of Mycoplasma agalactiae PG2T and two Sardinian field buy Luminespib isolates (named Bortigali and Nurri), were grown in PPLO medium supplemented learn more with 20% heat inactivated horse

serum and 500 μg/mL ampicillin, at 37°C with constant agitation. Mycoplasmas were collected by centrifugation (10 min at 10,000 × g at 4°C), and washed three times with PBS. At least three mycoplasma pellets were obtained from each bacterial culture replicate, and used for genetic and proteomic analyses. Total DNA was extracted from a set of pellets with DNeasy Blood & Tissue Kit (Qiagen), and subjected to FS1-FS2 PCR for species confirmation [51]. Total protein extracts and Triton X-114 fractionation

For total protein extracts, bacterial pellets were resuspended in 1% hot SDS, incubated for 3 minutes at 95°C, chilled, and diluted with lysis buffer (7 M urea, 2 M thiourea, 2.5% CHAPS, 2% ASB-14, 40 mM Tris-HCl pH 8.8, 1% IPG-buffer, protease inhibitors), and insoluble materials were discarded by centrifugation (10 min at 10,000 × g at 4°C) [52]. Hydrophilic and hydrophobic protein fractions were obtained Rucaparib manufacturer by Triton X-114 fractionation [29, 30] and ProteoPrep® Membrane Extraction Kit (Sigma-Aldrich). Proteins samples were quantified as described [52]. SDS-PAGE and 2-D PAGE SDS-PAGE was performed on 8% polyacrylamide gels on a Protean Tetra Cell (Bio-Rad) following the manufacturer instructions, and gels were stained with PageBlue™ Protein Staining Solution (Fermentas). Prior to 2-D PAGE, Triton X-114 fractions were precipitated with methanol-chloroform [35] and resuspended in lysis buffer (8 M urea, 2 M thiourea, 2.5% CHAPS, 2% ASB-14, 40 mM Tris-HCl pH 8.8, 1% IPG-buffer, protease inhibitors).

Furthermore, there was no statistical difference in bacterial loads in this website the ear effusions recovered from the two groups (Figure  3A). Figure 3 Deletion of hfq in H. influenzae strain 86-028NP in the chinchilla model of otitis media. (A) Bacterial titers of 86-028NP (closed circles) and the ∆hfq strain HI2207 (closed squares) in the middle ear effusions collected on days 4, 7, 11 and

14 post infection. (B) Competitive index comparing the input ratios of 86-028NP and HI2207 on day 0 to the output ratios of bacterial titers on the days indicated post infection (**P<0.001). In the fitness assays, five chinchillas were challenged with the wild type and mutant strains and disease progression was assessed on days 4, 7, 11, and 14 post-infection (Figure  3B). Over the duration of the experiment, the wild type strain produced titers normally seen in otitis media in the chinchilla following challenge with this strain [46]. However, the mutant strain was unable to compete with wild type in this environment. The average competitive index [(mutant output/WT output)/(mutant input/WT input)] in the ten ears was approximately 0.01 by day four (P<0.001, one

sample t-test for competitive index = 1.0) and continued to decline until day 11 when all ears were cleared of the mutant strain (Figure  3B). Because in vitro growth rates of mutant and wild type strains were not different in sBHI, the results of the mixed challenge suggest that the mutant’s fitness reduction is specific to the host environment. The nontypeable strain R2866 was compared Ribociclib research buy to the hfq mutant, HI2206, and the ∆hfq complement selleck screening library strain, HI2210, for the ability to establish and maintain bacteremia in the infant rat model of invasive disease. Virulence and fitness models of infection were also used in the infant rats. In the virulence study, two groups of 10 infant rats were infected with the wild type or mutant strain and disease progression was monitored by MK-0457 research buy clinical signs of infection and by bacterial titers in the blood. There was no observed

difference in disease progression between the two groups and there was no significant difference in the bacterial titers (Figure  4A). Figure 4 Comparison of H. influenzae strains R2866, HI2206, and HI2210 to sustain bacteremia in infant rats. (A) Bacteremic titers of rats infected with either R2866 (closed circles) or HI2206 (closed squares) in the virulence model of infection. (B) Competitive index showing the comparison of bacteria input ratios of R2866 and HI2206 on Day 0 compared to the output ratios on subsequent days of the infection. (C) Competitive index comparing the ∆hfq strain HI2206 and the complement HI2210. (D) Comparison of fitness of R2866 and HI2210. Data are representative of two independent experiments. (**P<0.0001; *P<0.01). In the infant rat fitness study, two cohorts of 10 pups were used to compare the fitness of R2866, HI2206, and HI2210.

IprScan predicts InterPro domains based on protein sequences [56]. The

Interpro2go mapping file (http://​www.​ebi.​ac.​uk/​interpro) was used to map GO annotations to genes with the corresponding domain predictions. A domain-based GO prediction was made only if it was not redundant with an existing manually-curated or orthology-based GO term, or one of its parental terms, that was already assigned to an orthologous protein. Finally, descriptions for genes lacking manual or GO-based annotations were constructed from the manual GO terms assigned to MDV3100 manufacturer characterized orthologs. GO annotations were included with the following precedence: BP, followed by MF, and then CC. For genes that lacked experimental characterization and characterized orthologs, but had functionally characterized InterPro domains, descriptions were generated from the domain-based GO annotations. The same precedence rules applied as to the descriptions selleck generated using orthology-based GO information. For genes that

lacked experimental characterization and characterized PR-171 datasheet orthologs, and without functionally characterized InterPro domains, but had uncharacterized orthologs, the descriptions simply list the orthology relationship because no inferred GO information was available. Secondary metabolic gene cluster analysis and annotation The pre-computed results file (smurf_output_precomputed_08.13.08.zip) was downloaded from the SMURF website (http://​jcvi.​org/​smurf/​index.​php). Version 1.2.1 of the antiSMASH program [39] was downloaded from (http://​antismash.​secondarymetabol​ites.​org/​) and run locally on the chromosome and/or contig sequences of A. nidulans FGSC A4, A. fumigatus Af293, A. niger CBS 513.88 and A. oryzae RIB40. Details of the parameters the antiSMASH program uses to predict boundaries are in described in Medema et al. 1998 [39] and those for SMURF are described in Khaldi et al. 2010 [38]. The secondary metabolic gene clusters predicted by

these programs P-type ATPase were manually analyzed and annotated using functional data available for each gene in AspGD. Cluster membership was determined based on physical proximity of candidate genes to cluster backbone genes. Adjacent genes were added to the cluster if they had functional annotations common to known secondary metabolism genes. In cases where backbone genes had Jaccard orthologs in other species (see above), we required orthology between all other cluster members. Confirmation of orthology between clusters was facilitated by use of the Sybil multiple genome browser which can be used to evaluate synteny between species. We visually evaluated synteny by examining whether a gene that was putatively in a cluster had orthologs in the other species – where a gene in the species in which the cluster was identified no longer had orthologs in the other species that were adjacent, we inferred a break in synteny.

capsulatum with a large set of tiling arrays, and combined the results with gene-targeted expression profiling and sequence homology, #E7080 cost randurls[1|1|,|CHEM1|]# yielding a high confidence set of validated gene predictions for G217B with 7,362 gene predictions being validated by at least two of the three methods. In addition, the unbiased approach of the tiling arrays allowed us to detect 264 novel transcripts that are now being incorporated into our oligo expression arrays, directly extending the sensitivity of that platform. Additionally, the results of

this study are available at http://​histo.​ucsf.​edu in an interactive format intended to facilitate expression, insertional mutagenesis, and bioinformatics based studies. Thus, the transcript sets resulting from this study represent an enhancement of the previously available H. capsulatum gene set and a starting point for the experimental and theoretical characterization of the molecular biology of this important intracellular pathogen. Methods RNA Extraction and cDNA synthesis To generate a diverse RNA sample for the tiling experiment, we prepared RNA from yeast-form CP673451 Histoplasma capsulatum strain G217B (ATCC 26032; a kind gift of William

Goldman, Washington University, St. Louis, MO) under a variety of conditions (including early, middle, and late logarithmic growth, stationary phase, heat shock (42°C for 30 min), oxidative stress (1 mM menadione for 80 min), sulfhydryl Ketotifen reducing stress (10 mM DTT for 2 hours), and a range of media (HMM[20], 3M[20], YPD[21], and SD complete[21]). Total RNA and polyA RNA were prepared as previously described[8, 9]. Cy5-labeled cDNA was prepared from individual RNA samples as previously described[8], and an equal mass of cDNA was pooled from each sample and hybridized to individual tiling arrays as described below. Whole Genome Tiling Array Design The whole genome tiling arrays were designed based on the GSC Histoplasma capsulatum strain G217B genome assembly as of 11/30/2004. Degenerate sequence and transposable elements were removed from the assembly using RepeatMasker[22] with default parameters and the repeat families determined by the

GSC. The remaining sequence was tiled with 50 mer probes at an average frequency of one probe every 60 base pairs. Probe spacing was adjusted to minimize variation in melting temperature, and a subset of probes were truncated to optimize synthesis, in collaboration with CombiMatrix. The number of arrays used to tile a given contig was minimized, and the location of tiling probes was randomized within a given array. In addition, each array contained a common set of control probes, viz.: quality control (QC) and negative control (NC) probes designed by CombiMatrix (Mukilteo, WA); positive control probes tiling the genomic loci and non-genic flanking sequence of TEF1(P40911)[23], TYR1[9], and CBP1(AF006209)[24]; and probes specific to a spike-in control sequence.

Open Access This article

CBL0137 clinical trial 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. Pando 10.58 S, 69.40 W − I. De la Riva, pc; S. Reichle, pc Tahuamanu, Depto. Pando 11.24 S, 69.10 W − I. De la Riva, pc; S. Reichle, pc Brazil (39 localities, 21 presences) Ajarani check details region, Edo. Roraima 02.0 N, 62.45 W − C. this website Azevedo-Ramos, pc Alto Rio Juruá region, Edo. Amazonas 08.0 S, 72.50 W − C. Azevedo-Ramos, pc Baixo Rio Juruá region, Edo. Amazonas 03.15 S, 66.15 W − C. Azevedo-Ramos, pc Belém region, Edo. Pará 01.29 S, 48.24 W − C. Azevedo-Ramos, pc Boa Vista region, Edo. Roraima 02.49 N, 60.40 W − J.P. Caldwell, pc Caiman region, Edo. Amapá 03.18 N, 52.15 W

+ Lescure, (1981a) Chanpiom region, Edo. Pará 01.20 N, 51.16 W − C. Azevedo-Ramos, pc Carajás region, Edo. Pará 06.02 S, 50.25 W + C. Azevedo-Ramos, pc CEMEX, SE of Santarém, Edo. Pará 03.09 S, 54.51 W + J.P. Caldwell, pc Cruzeiro do Sul, Edo. Acre 07.37 S, 72.35 W − Authors’ pers. observ. Igarapé de Piranha, Edo. Amazonas 05.43 S, 61.16 W + MZUSP Ituxi region, Edo. Amazonas 08.17 S, 65.30 W − C. Azevedo-Ramos, pc Jacareacanga, Edo. Pará 01.32 S, 47.03 W + ZUEC Lago do Castanho, Edo. Amazonas 03.45 S, 60.30 W + ZUEC

Mamirauá region, Edo. Amazonas 03.30 S, 64.35 W − C. Azevedo-Ramos, pc Maués, Edo. Amazonas 03.24 S, 57.42 W + AMNH Monte Cristo, Edo. Pará 04.40 S, 55.38 W + MZUSP Município de Castanho, Edo. Amazonas 03.30 S, 59.54 W − J.P. Caldwell, pc Paragominas region, Edo. Pará 03.45 S, 48.20 W + C. Azevedo-Ramos, pc PN da Serra do Divisor, Edo. Acre 08.20 S, 73.32 W − Authors’ pers. observ. Pojuca, Serra AMP deaminase do Carajás, Edo. Pará 06.10 S, 51.05 W + ZUEC Porto Platon, Edo. Amapá 00.42 N, 51.27 W + MZUSP Porto Grande, Edo. Amapá 00.42 N, 51.24 W + ZUEC Porto Walter, Edo. Acre 08.15 S, 72.47 W − J.P. Caldwell, pc Presidente Figuereido, Edo. Amazonas 02.00 S, 60.00 W − Authors’ pers. observ. Reserva Campina, Edo. Amazonas 03.07 S, 60.03 W + ZUEC Reserva INPA-WWF, Edo. Amazonas 02.25 S, 59.43 W + MZUSP Reserva Pacanari, Edo. Pará 00.52 S, 52.31 W + ZUEC Rio Amaparí, Edo. Amapá 01.15 N, 52.15 W + MZUSP Rio Formoso, Edo. Rondônia 10.19 S, 64.34 W − J.P. Caldwell, pc Rio Ituxi, Edo. Amazonas 08.29 S, 65.43 W − J.P. Caldwell, pc Rio Manjuru, Edo. Amazonas 04.00 S, 57.00 W + AMNH Rio Maú, Edo. Roraima 04.20 N, 59.45 W + MZUSP Serra do Navio, Edo. Amapá 01.55 N, 51.50 W + MZUSP; McDiarmid (1973) Terra Verde Lodge, Edo. Amazonas 03.37 S, 59.86 W − J.P. Caldwell, pc Urucú region, Edo.

Our limited phenotypic screen for attenuated parasite growth confirmed the feasibility of such approaches inP. falciparumby identifying several genes and pathways critical for blood-stage development. One of the most severely affected mutant parasites identified in our screen is a knockout of MAL8P1.104 (clone F3), which is thePlasmodiumorthologue of yeastCaf1(CCR4-associated factor 1) selleck [33]. In yeast, CAF1 is a component of CCR4-NOT complex that is a global regulator of gene expression, controlling chromatin remodelling, transcriptional regulation, mRNA stability and protein degradation [34]. MEK phosphorylation Experimental protein interaction data indicates

a similar functional complex exists inP. falciparum[7] and with a scarcity of known transcription factors or identifiable conserved regulatory elements inPlasmodium, deadenylation may be extremely significant in controlling gene expression through regulating mRNA

abundance by degradation [35]. The significance of protein phosphorylation and dephosphorylation in regulating parasite cellular activities is also clearly ICG-001 demonstrated by the attenuated growth phenotype of our knockout of PFF0770c (clone A5), which encodes one of the 12 type 2C protein phosphatases (PP2C) found inPlasmodium[36]. PP2Cs carry out a wide range of functions in higher eukaryotes including intracellular signalling and providing cell cycle and developmental check points [37–39]. Two PP2Cs, in Non-specific serine/threonine protein kinase the closely related apicomplexanToxoplasma,

were recently shown to be involved in parasite motility and host cell modulation [40,41]. Another mutant clone displaying attenuated growth was a knockout of PF10_0350 (clone E6) that codes for a hypothetical protein unique toPlasmodiumspecies and attests to the theory that such uniquePlasmodiumgenes need to be investigated further as antimalarial targets.piggyBacinsertion in the 5′ UTRs of PFC0271c and PFC0275w, coding for glutaredoxin and glycerol-3 phosphate dehydrogenase, respectively, resulted in increased levels of both transcripts in the mutant clone B7 as seen by quantitative RT-PCR (data not shown), indicating that optimal expression of genes is essential for normal parasite growth. Several other phenotypic screens such as those for virulence, drug resistance, gametocytogenesis and transmissibility of infection to mosquito hosts can now be accomplished inP. falciparumthat will contribute immensely to our current understanding of parasite biology. Apart from its application in whole-genome mutagenesis and phenotype screens,piggyBacis also a powerful tool for stable transgene expression inP. falciparumas any parasite strain or clone of interest can be transformed. We have confirmed the functionality ofpiggyBacsystem in three different strains ofP.

The isolate Kp10 formed a distinct cluster with Pediococcus acidilactici, supported by a bootstrap value of 100%. Figure 2 Phylogenetic relationship of Kp10 with related species based on partial 16S rDNA gene sequence analysis. The phylogenetic tree was constructed using the neighbour-joining method (CLC Sequence Viewer 6.5.2). The numbers at the nodes are bootstrap confidence levels (percentage) from 1,000 replicates. The scale bar represents 0.120 substitutions per nucleotide find protocol position. Reference sequences were obtained from the GenBank nucleotide sequence database. Physiological and biochemical this website characterization of isolate Kp10 (P. acidilactici) The isolate Kp10 (P. acidilactici) was

selected for further analysis based on its ability to produce high amounts of BLIS (Table 1). This bacterium was a gram-positive, catalase-negative coccus that was arranged in tetrads (Table 4). Kp10 demonstrated the ability to grow in the presence of 2% NaCl and within a temperature range of 30°C to 45°C. Table 4 Characteristics of isolate Kp10 Characteristics R788 Kp10 (Pediococcus acidilactici)

Gram stain reaction Gram-positive cocci Colony morphology     Size >0.1 mm   Shape Circular   Colour Milky white   Elevation Concave   Density Mucoid and glistening Biochemical characteristics     Catalase – Physiological characteristics   Growth in M17 broth:     With 0.5% NaCl +   With 2% NaCl +   With 4% NaCl –   With 6.5% NaCl –   With 10% NaCl –   At 5°C –   At 10°C –   At 30°C +   At 35°C +   At 37°C +   At 45°C +   At 60°C – Positive results (+), negative results (-).

As shown in Table 5, Kp10 (P. acidilactici) was susceptible second to 18 antibiotics (penicillin G, erythromycin, ceftriaxone, amikacin, ciprofloxacin, norfloxacin, chloramphenicol, cefuroxime sodium, tetracycline, nalidixic acid, ampicillin, gentamycin, nitrofurantoin, sulfamethoxazole/trimethoprim, vancomycin, novobiocin, kanamycin, and oxytetracycline), and resistant to five antibiotics (lincomycin, colistin sulphate, bacitracin, polymixin B, and cefamandole). Table 5 Growth inhibition of P. acidilactici Kp10 by disc diffusion method Antibiotic   Inhibition zone diameter   Disc content Size (mm) ≤15 mm (R) 16–20 mm (I) ≥21 mm (S) Penicillin G 2 Units 24 (0)     + Penicillin G 10 Units 26.5 (0.07)     + Erythromycin 15 μg 32 (0)     + Erythromycin 10 μg 30 (0)     + Ceftriaxone 30 μg 33.08 (1.31)     + Lincomycin 10 μg 0 (0) +     Colistin sulphate 10 μg 0 (0) +     Streptomycin 10 μg 18.63 (0.88)   +   Amikacin 30 μg 24.83 (0.25)     + Cloxacillin 5 μg 19 (0)   +   Ciprofloxacin 10 μg 30 (0)     + Norfloxacin 10 μg 24 (0)     + Chloramphenicol 30 μg 32.28 (0.4)     + Cefuroxime sodium 30 μg 34.25 (0.35)     + Tetracycline 30 μg 29.5 (0.07)     + Tetracycline 10 μg 24 (0)     + Nalidixic acid 30 μg 31 (0)     + Ampicillin 25 μg 32 (0)     + Gentamycin 10 μg 22.5 (0.71)     + Gentamycin 30 μg 28 (0)     + Mecillinam 25 μg 19.72 (0.

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