Moulos et al Scientific Data-Data Citation 4

This entry (Data Citation 4) contains multiple files: i) the assembled Bombyx mori genome as described in the ‘Methods’ section, ii) the assembled Bombyx mori transcriptome assembled like the Bombyx mori genome and used for optimizing the short read alignment procedure, iii) the assembled Bombyx mori genes in GFF, GTF and text tab-delimited format, iv) bowtie2 indexes for the Bombyx mori genome, v) bowtie2 indexes for the Bombyx mori transcriptome and vi) custom code used for the analysis

Moulos et al. Scientific Data-Data Citation 5- Proteome Discoverer 1.4 data analysis files

There are 6 Excel files in this entry. Each file contains the raw analysis by Proteome Discoverer 1.4 software of the proteomic data from Day 0 and Day 6 of the 5th instar larvae of Bombyx mori. 3 files are from Day 0 (3 biological replicates) and 3 files are from Day 6 (3 biological replicates) of the 5th instar.<br

2DE and western blot analysis of serospecificity for samples from different dogs suffering from CVL.

<p>(A) Total promastigote cell extracts were separated in the first dimension with a pH gradient of 3–10 (7 cm strips) followed by 12% SDS-PAGE. The separated proteins were electroblotted onto nitrocellulose membranes and probed with different pools of sera from (B) healthy dogs (n = 5; 1:500), (C, E) asymptomatic dogs (n = 5 and n = 4, respectively; 1:500), and (D, F) symptomatic dogs (n = 3 and n = 2, respectively; 1:1,000).</p

Comparison of serospecificities against total promastigote cell extracts of symptomatic (SD) and asymptomatic (AD) dogs suffering from CVL.

<p>(A) Total promastigote cell extracts were separated in the first dimension with a pH gradient of 5–8 (7-cm strips) followed by 12% SDS-PAGE. The separated proteins were electroblotted onto a nitrocellulose membrane and probed with pools of sera from (B) asymptomatic (n = 9; 1:500) and (C) symptomatic dogs (n = 5; 1:1,000). Protein spots recognized by AD sera only are numbered.</p

<i>In silico</i> evaluation of the identified proteins antigenicity.

<p><i>In silico</i> evaluation of the identified proteins antigenicity.</p

Protein antigens recognized by IgG antibodies in asymptomatic dog (AD) sera.

<p>Protein antigens recognized by IgG antibodies in asymptomatic dog (AD) sera.</p

IgG reaction pattern associated with CVL status.

<p>Total <i>Leishmania infantum</i> promastigote cell extracts were separated with 12% SDS-PAGE and electrotransferred to nitrocellulose membranes. The membranes were probed with serum obtained from individual asymptomatic dogs (1:500) or symptomatic dogs (1:1,000) and secondary anti-dog (A) IgG, (B) IgG1 or (C) IgG2 (1:10,000). Representative western blots from each group of dogs are depicted (asymptomatic: n = 5; symptomatic: n = 3). Numbers represent the code numbers of the dogs enrolled in the study. Molecular weight markers are shown on the left-hand side.</p

Proteins selected on the basis of predicted antigenicity and their content on highly scored MHC class I- and MHC class II-restricted epitopes.

<p>Proteins selected on the basis of predicted antigenicity and their content on highly scored MHC class I- and MHC class II-restricted epitopes.</p

Percentage (%) of amino acid sequence coverage of identified <i>L</i>. <i>infantum</i> proteins based on their content in high binding MHC class I and/or II-restricted peptides.

<p>Percentage (%) of amino acid sequence coverage of identified <i>L</i>. <i>infantum</i> proteins based on their content in high binding MHC class I and/or II-restricted peptides.</p

Proteomic Analysis of Human Angiogenin Interactions Reveals Cytoplasmic PCNA as a Putative Binding Partner

Human Angiogenin (hAng) is a member of the ribonuclease A superfamily and a potent inducer of neovascularization. Protein interactions of hAng in the nucleus and cytoplasm of the human umbilical vein cell line EA.hy926 have been investigated by mass spectroscopy. Data are available via ProteomeXchange with identifiers PXD006583 and PXD006584. The first gel-free analysis of hAng immunoprecipitates revealed many statistically significant potential hAng-interacting proteins involved in crucial biological pathways. Surprisingly, proliferating cell nuclear antigen (PCNA), was found to be immunoprecipitated with hAng only in the cytoplasm. The hAng–PCNA interaction and colocalization in the specific cellular compartment was validated with immunoprecipitation, immunoblotting, and immunocytochemistry. The results revealed that PCNA is predominantly localized in the cytoplasm, while hAng is distributed both in the nucleus and in the cytoplasm. hAng and PCNA colocalize in the cytoplasm, suggesting that they may interact in this compartment