Transporter proteins, two component systems, and cell division associated proteins (MAP1906c, MAP0448 and MAP2997c) were also upregulated by the C strain (Table 1 and Additional file GSK1210151A supplier 1, Table S8). The sheep strain also upregulated transporter proteins, fatty acid biosynthesis, DNA replication protein (MAP3433), and stress response proteins (MAP3831c, MAP2764) (Table 2, Additional file 1, Table S9 and {Selleck Anti-diabetic Compound Library|Selleck Antidiabetic Compound Library|Selleck Anti-diabetic Compound Library|Selleck Antidiabetic Compound Library|Selleckchem Anti-diabetic Compound Library|Selleckchem Antidiabetic Compound Library|Selleckchem Anti-diabetic Compound Library|Selleckchem Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|Anti-diabetic Compound Library|Antidiabetic Compound Library|buy Anti-diabetic Compound Library|Anti-diabetic Compound Library ic50|Anti-diabetic Compound Library price|Anti-diabetic Compound Library cost|Anti-diabetic Compound Library solubility dmso|Anti-diabetic Compound Library purchase|Anti-diabetic Compound Library manufacturer|Anti-diabetic Compound Library research buy|Anti-diabetic Compound Library order|Anti-diabetic Compound Library mouse|Anti-diabetic Compound Library chemical structure|Anti-diabetic Compound Library mw|Anti-diabetic Compound Library molecular weight|Anti-diabetic Compound Library datasheet|Anti-diabetic Compound Library supplier|Anti-diabetic Compound Library in vitro|Anti-diabetic Compound Library cell line|Anti-diabetic Compound Library concentration|Anti-diabetic Compound Library nmr|Anti-diabetic Compound Library in vivo|Anti-diabetic Compound Library clinical trial|Anti-diabetic Compound Library cell assay|Anti-diabetic Compound Library screening|Anti-diabetic Compound Library high throughput|buy Antidiabetic Compound Library|Antidiabetic Compound Library ic50|Antidiabetic Compound Library price|Antidiabetic Compound Library cost|Antidiabetic Compound Library solubility dmso|Antidiabetic Compound Library purchase|Antidiabetic Compound Library manufacturer|Antidiabetic Compound Library research buy|Antidiabetic Compound Library order|Antidiabetic Compound Library chemical structure|Antidiabetic Compound Library datasheet|Antidiabetic Compound Library supplier|Antidiabetic Compound Library in vitro|Antidiabetic Compound Library cell line|Antidiabetic Compound Library concentration|Antidiabetic Compound Library clinical trial|Antidiabetic Compound Library cell assay|Antidiabetic Compound Library screening|Antidiabetic Compound Library high throughput|Anti-diabetic Compound high throughput screening| Figure S3). The iron-sparing response to iron starvation

occurs when non-essential iron utilization proteins such as aconitase and succinate dehydrogenases are repressed and intracellular iron is used to maintain essential cellular functions [34, 35]. Interestingly, during iron limitation, the cattle strain but not sheep MAP downregulated expression of aconitase (MAP1201c) and succinate dehydrogenases (MAP3697c, MAP3698c) (Figure 2). Repression of aconitase in response to iron starvation is post-transcriptionally mediated via small RNAs [36]. Consistent with this finding, our results reveal an upregulation of aconitase transcripts (both by microarray and Q-RT PCR) with a concomitant downregulation at the protein level in the C MAP alone under iron-limiting conditions. Figure

2 Repression of non-essential iron using proteins under iron-limiting conditions by cattle MAP strain: Reporter ion regions Selleckchem BIX 1294 (114 – 117 m/z) of peptide tandem mass spectrum from iTRAQ labeled peptides from MAP3698c, MAP3697c and MAP1201c are shown. Quantitation of peptides many and inferred proteins are made from relative peak areas of reporter ions. Peptides obtained from cattle MAP cultures grown in iron-replete and iron-limiting medium were labeled with 114 and 115 reporter ions, respectively.. Peptides obtained from sheep MAP cultures grown in iron-replete and iron-limiting medium were labeled with 116

and 117 reporter ions, respectively. The peptide sequences and shown in the parenthesis and the red dashed line illustrates the reporter ion relative peak intensities. Cattle strain of MAP shows an iron sparing response by downregulating expression of iron using proteins. Protein expression under iron-replete conditions The sheep strain upregulated as many as 13 unique peptides (>95% confidence) that were mapped to MAP2121c. A representative peptide map is shown in Figure 3A. Interestingly, none of these were differentially regulated in response to iron by C strain of MAP. MAP2121c was originally described as 35-kDa antigen and is an immune-dominant protein involved in MAP entry into bovine epithelial cells [37, 38].