scholarly journals Genomic Approach for Analysis of Surface Proteins in Chlamydia pneumoniae

2002 ◽  
Vol 70 (1) ◽  
pp. 368-379 ◽  
Author(s):  
Silvia Montigiani ◽  
Fabiana Falugi ◽  
Maria Scarselli ◽  
Oretta Finco ◽  
Roberto Petracca ◽  
...  
Keyword(s):  
Chlamydia Pneumoniae ◽  
Genetic Manipulation ◽  
Respiratory Infections ◽  
Surface Protein ◽  
Surface Proteins ◽  
Mass Spectrometry Analysis ◽  
Western Blots ◽  
Spectrometry Analysis ◽  
Proteomic Approach ◽  
Definition Of

ABSTRACT Chlamydia pneumoniae, a human pathogen causing respiratory infections and probably contributing to the development of atherosclerosis and heart disease, is an obligate intracellular parasite which for replication needs to productively interact with and enter human cells. Because of the intrinsic difficulty in working with C. pneumoniae and in the absence of reliable tools for its genetic manipulation, the molecular definition of the chlamydial cell surface is still limited, thus leaving the mechanisms of chlamydial entry largely unknown. In an effort to define the surface protein organization of C. pneumoniae, we have adopted a combined genomic-proteomic approach based on (i) in silico prediction from the available genome sequences of peripherally located proteins, (ii) heterologous expression and purification of selected proteins, (iii) production of mouse immune sera against the recombinant proteins to be used in Western blotting and fluorescence-activated cell sorter (FACS) analyses for the identification of surface antigens, and (iv) mass spectrometry analysis of two-dimensional electrophoresis (2DE) maps of chlamydial protein extracts to confirm the presence of the FACS-positive antigens in the chlamydial cell. Of the 53 FACS-positive sera, 41 recognized a protein species with the expected size on Western blots, and 28 of the 53 antigens shown to be surface-exposed by FACS were identified on 2DE maps of elementary-body extracts. This work represents the first systematic attempt to define surface protein organization in C. pneumoniae.

scholarly journals Serum-Based Proteomics Profiling in Adult Patients with Cystic Fibrosis

2020 ◽  
Vol 21 (19) ◽  
pp. 7415
Author(s):  
Hicham Benabdelkamel ◽  
Hanadi Alamri ◽  
Meshail Okla ◽  
Afshan Masood ◽  
Mai Abdel Jabar ◽  
...  
Keyword(s):  
Cystic Fibrosis ◽  
Multiple Reaction Monitoring ◽  
Autosomal Recessive Disorder ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Serum Proteomics ◽  
Proteomic Approach ◽  
Significant Difference ◽  
Canonical Pathways ◽  
Cf Transmembrane Conductance Regulator

Cystic fibrosis (CF), the most common lethal autosomal recessive disorder among Caucasians, is caused by mutations in the CF transmembrane conductance regulator (CFTR) chloride channel gene. Despite significant advances in the management of CF patients, novel disease-related biomarkers and therapies must be identified. We performed serum proteomics profiling in CF patients (n = 28) and healthy subjects (n = 10) using the 2D-DIGE MALDI-TOF proteomic approach. Out of a total of 198 proteins identified, 134 showed a statistically significant difference in abundance and a 1.5-fold change (ANOVA, p < 0.05), including 80 proteins with increased abundance and 54 proteins with decreased abundance in CF patients. A multiple reaction monitoring-mass spectrometry analysis of six differentially expressed proteins identified by a proteomic approach (DIGE-MALD-MS) showed a significant increase in C3 and CP proteins and a decrease in APOA1, Complement C1, Hp, and RBP4proteins compared with healthy controls. Fifteen proteins were identified as potential biomarkers for CF diagnosis. An ingenuity pathway analysis of the differentially regulated proteins indicates that the central nodes dysregulated in CF subjects involve pro-inflammatory cytokines, ERK1/2, and P38 MAPK, which are primarily involved in catalytic activities and metabolic processes. The involved canonical pathways include those related to FXR/RXR, LXR/RXR, acute phase response, IL12, nitric oxide, and reactive oxygen species in macrophages. Our data support the current efforts toward augmenting protease inhibitors in patients with CF. Perturbations in lipid and vitamin metabolism frequently observed in CF patients may be partly due to abnormalities in their transport mechanism.

scholarly journals A straightforward gel-free proteomics pipeline assisted by liquid isoelectric focusing (OFFGEL) and mass spectrometry analysis to study bovine meat proteome

2020 ◽  
pp. 108201322092914
Author(s):  
Enrique Sentandreu ◽  
Claudia Fuente-García ◽  
José L Navarro ◽  
Miguel A Sentandreu
Keyword(s):  
Mass Spectrometry ◽  
Isoelectric Focusing ◽  
Quantitative Data ◽  
Ion Trap ◽  
Three Dimensional ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Protein Fractionation ◽  
Spectrometry Analysis ◽  
Proteomic Approach

Bovine sarcoplasmic sub-proteome was studied through a straightforward gel-free pipeline supported by liquid isoelectric focusing (OFFGEL) protein fractionation coupled to liquid chromatography-mass spectrometry (LC-MS) analysis. Full-MS and data-dependent MS/MS analyses were simultaneously performed by a conventional three-dimensional ion-trap addressing targeted quantitative and untargeted qualitative research, respectively. There were unambiguously identified 47 proteins distributed along 12 OFFGEL fractions assayed. Regarding intermediate- and high-abundant peptides, bulky quantitative data processing performed by MZmine 2 freeware yielded a satisfactory linearity and coefficient of variation with r2 in the 0.95–0.99 range and about 25%, respectively. Up to 41 peptides from 20 identified proteins were relatively quantified throughout OFFGEL fractions. This reliable, flexible and affordable gel-free proteomic approach could be readily implemented by industry to improve quality assessment of protein-based food products.

scholarly journals The Oligopeptide Transport System Is Essential for the Development of Natural Competence in Streptococcus thermophilus Strain LMD-9

2009 ◽  
Vol 191 (14) ◽  
pp. 4647-4655 ◽  
Author(s):  
Rozenn Gardan ◽  
Colette Besset ◽  
Alain Guillot ◽  
Christophe Gitton ◽  
Véronique Monnet
Keyword(s):  
Quorum Sensing ◽  
Streptococcus Thermophilus ◽  
Defined Medium ◽  
Mass Spectrometry Analysis ◽  
Transport Systems ◽  
Label Free ◽  
Spectrometry Analysis ◽  
Proteomic Approach ◽  
Liquid Chromatography Tandem Mass ◽  
Oligopeptide Transport

ABSTRACT In gram-positive bacteria, oligopeptide transport systems, called Opp or Ami, play a role in nutrition but are also involved in the internalization of signaling peptides that take part in the functioning of quorum-sensing pathways. Our objective was to reveal functions that are controlled by Ami via quorum-sensing mechanisms in Streptococcus thermophilus, a nonpathogenic bacterium widely used in dairy technology in association with other bacteria. Using a label-free proteomic approach combining one-dimensional electrophoresis with liquid chromatography-tandem mass spectrometry analysis, we compared the proteome of the S. thermophilus LMD-9 to that of a mutant deleted for the subunits C, D, and E of the ami operon. Both strains were grown in a chemically defined medium (CDM) without peptides. We focused our attention on proteins that were no more detected in the ami deletion mutant. In addition to the three subunits of the Ami transporter, 17 proteins fulfilled this criterion and, among them, 7 were similar to proteins that have been identified as essential for transformation in S. pneumoniae. These results led us to find a condition of growth, the early exponential state in CDM, that allows natural transformation in S. thermophilus LMD-9 to turn on spontaneously. Cells were not competent in M17 rich medium. Furthermore, we demonstrated that the Ami transporter controls the triggering of the competence state through the control of the transcription of comX, itself controlling the transcription of late competence genes. We also showed that one of the two oligopeptide-binding proteins of strain LMD-9 plays the predominant role in the control of competence.

scholarly journals Proteomic Analysis of Liver from Human Lipoprotein(a) Transgenic Mice Shows an Oxidative Stress and Lipid Export Response

2018 ◽  
Vol 2018 ◽  
pp. 1-11
Author(s):  
Euan J. Rodger ◽  
Carolyn M. Porteous ◽  
Gregory T. Jones ◽  
Michael Legge ◽  
Torsten Kleffmann ◽  
...  
Keyword(s):  
Human Liver ◽  
Density Lipoprotein ◽  
Bioinformatic Analysis ◽  
Liver Cells ◽  
Mass Spectrometry Analysis ◽  
Two Dimensional Gel Electrophoresis ◽  
Lipoprotein A ◽  
Spectrometry Analysis ◽  
Human Liver Cells ◽  
Proteomic Approach

Background. Mouse models of hypercholesterolaemia have been used to identify arterial proteins involved in atherosclerosis. As the liver is extremely sensitive to dyslipidemia, one might expect major changes in the abundance of liver proteins in these models even before atherosclerosis develops. Methods. Lipid levels were measured and a proteomic approach was used to quantify proteins in the livers of mice with an elevated low-density lipoprotein (LDL) and the presence of lipoprotein(a) [Lp(a)] but no atherosclerosis. Results. The livers of Lp(a) mice showed an increased triglyceride but reduced phospholipid and oxidised lipid content. Two-dimensional gel electrophoresis and mass spectrometry analysis identified 24 liver proteins with significantly increased abundance in Lp(a) mice (P<0.05). A bioinformatic analysis of the 24 proteins showed the major effect was that of an enhanced antioxidant and lipid efflux response with significant increases in antioxidant (Park7, Gpx1, Prdx6, and Sod1) and lipid metabolism proteins (Fabp4, Acaa2, apoA4, and ApoA1). Interestingly, human liver cells treated with Lp(a) showed significant increases in Gpx1 and Prdx6 but not Sod1 or Park7. Conclusions. The presence of human LDL and Lp(a) in mice promotes an enhanced flux of lipids into the liver which elicits an antioxidant and lipid export response before the onset of atherosclerosis. The antioxidant response can be reproduced in human liver cells treated with Lp(a).

scholarly journals Targeting the endothelial progenitor cell surface proteome to identify novel mechanisms that mediate angiogenic efficacy in a rodent model of vascular disease

2013 ◽  
Vol 45 (21) ◽  
pp. 999-1011 ◽  
Author(s):  
Catherine C. Kaczorowski ◽  
Timothy J. Stodola ◽  
Brian R. Hoffmann ◽  
Anthony R. Prisco ◽  
Pengyuan Y. Liu ◽  
...  
Keyword(s):  
Cell Surface ◽  
Vascular Disease ◽  
Rodent Model ◽  
Surface Proteins ◽  
Mass Spectrometry Analysis ◽  
Major Advance ◽  
Endothelial Progenitor ◽  
Angiogenic Potential ◽  
Spectrometry Analysis

Endothelial progenitor cells (EPCs) promote angiogenesis, and clinical trials suggest autologous EPC-based therapy may be effective in treatment of vascular diseases. Albeit promising, variability in the efficacy of EPCs associated with underlying disease states has hindered the realization of EPC-based therapy. Here we first identify and characterize EPC dysfunction in a rodent model of vascular disease (SS/Mcwi rat) that exhibits impaired angiogenesis. To identify molecular candidates that mediate the angiogenic potential of these cells, we performed a broad analysis of cell surface protein expression using chemical labeling combined with mass spectrometry. Analysis revealed EPCs derived from SS/Mcwi rats express significantly more type 2 low-affinity immunoglobulin Fc-gamma (FCGR2) and natural killer 2B4 (CD244) receptors compared with controls. Genome-wide sequencing (RNA-seq) and qt-PCR confirmed isoforms of CD244 and FCGR2a transcripts were increased in SS/Mcwi EPCs. EPCs with elevated expression of FCGR2a and CD244 receptors are predicted to increase the probability of SS/Mcwi EPCs being targeted for death, providing a mechanistic explanation for their reduced angiogenic efficacy in vivo. Pathway analysis supported this contention, as “key” molecules annotated to cell death paths were differentially expressed in the SS/Mcwi EPCs. We speculate that screening and neutralization of cell surface proteins that “tag” and impair EPC function may provide an alternative approach to utilizing incompetent EPCs in greater numbers, as circulating EPCs are depleted in patients with vascular disease. Overall, novel methods to identify putative targets for repair of EPCs using discovery-based technologies will likely provide a major advance in the field of regenerative medicine.

scholarly journals Identification of Novel Surface Proteins of Anaplasma phagocytophilum by Affinity Purification and Proteomics

2007 ◽  
Vol 189 (21) ◽  
pp. 7819-7828 ◽  
Author(s):  
Yan Ge ◽  
Yasuko Rikihisa
Keyword(s):  
Anaplasma Phagocytophilum ◽  
Affinity Purification ◽  
The United States ◽  
Capillary Liquid Chromatography ◽  
Etiologic Agent ◽  
Surface Proteins ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis ◽  
Major Surface

ABSTRACT Anaplasma phagocytophilum is the etiologic agent of human granulocytic anaplasmosis (HGA), one of the major tick-borne zoonoses in the United States. The surface of A. phagocytophilum plays a crucial role in subverting the hostile host cell environment. However, except for the P44/Msp2 outer membrane protein family, the surface components of A. phagocytophilum are largely unknown. To identify the major surface proteins of A. phagocytophilum, a membrane-impermeable, cleavable biotin reagent, sulfosuccinimidyl-2-[biotinamido]ethyl-1,3-dithiopropionate (Sulfo-NHS-SS-Biotin), was used to label intact bacteria. The biotinylated bacterial surface proteins were isolated by streptavidin agarose affinity purification and then separated by electrophoresis, followed by capillary liquid chromatography-nanospray tandem mass spectrometry analysis. Among the major proteins captured by affinity purification were five A. phagocytophilum proteins, Omp85, hypothetical proteins APH_0404 (designated Asp62) and APH_0405 (designated Asp55), P44 family proteins, and Omp-1A. The surface exposure of Asp62 and Asp55 was verified by immunofluorescence microscopy. Recombinant Asp62 and Asp55 proteins were recognized by an HGA patient serum. Anti-Asp62 and anti-Asp55 peptide sera partially neutralized A. phagocytophilum infection of HL-60 cells in vitro. We found that the Asp62 and Asp55 genes were cotranscribed and conserved among members of the family Anaplasmataceae. With the exception of P44-18, all of the proteins were newly revealed major surface-exposed proteins whose study should facilitate understanding the interaction between A. phagocytophilum and the host. These proteins may serve as targets for development of chemotherapy, diagnostics, and vaccines.

scholarly journals Specific Roles of the iroBCDEN Genes in Virulence of an Avian Pathogenic Escherichia coli O78 Strain and in Production of Salmochelins

2008 ◽  
Vol 76 (8) ◽  
pp. 3539-3549 ◽  
Author(s):  
Mélissa Caza ◽  
François Lépine ◽  
Sylvain Milot ◽  
Charles M. Dozois
Keyword(s):  
Escherichia Coli ◽  
Respiratory Infections ◽  
Mass Spectrometry Analysis ◽  
Liquid Chromatography Mass Spectrometry ◽  
Avian Pathogenic Escherichia Coli ◽  
Prevalence Studies ◽  
Spectrometry Analysis ◽  
E Coli ◽  
Pathogenic Escherichia Coli ◽  
Negative Mutant

ABSTRACT Avian pathogenic Escherichia coli (APEC) strains are a subset of extraintestinal pathogenic E. coli (ExPEC) strains associated with respiratory infections and septicemia in poultry. The iroBCDEN genes encode the salmochelin siderophore system present in Salmonella enterica and some ExPEC strains. Roles of the iro genes for virulence in chickens and production of salmochelins were assessed by introducing plasmids carrying different combinations of iro genes into an attenuated salmochelin- and aerobactin-negative mutant of O78 strain χ7122. Complementation with the iroBCDEN genes resulted in a regaining of virulence, whereas the absence of iroC, iroDE, or iroN abrogated restoration of virulence. The iroE gene was not required for virulence, since introduction of iroBCDN restored the capacity to cause lesions and colonize extraintestinal tissues. Prevalence studies indicated that iro sequences were associated with virulent APEC strains. Liquid chromatography-mass spectrometry analysis of supernatants of APEC χ7122 and the complemented mutants indicated that (i) for χ7122, salmochelins comprised 14 to 27% of the siderophores present in iron-limited medium or infected tissues; (ii) complementation of the mutant with the iro locus increased levels of glucosylated dimers (S1 and S5) and monomer (SX) compared to APEC strain χ7122; (iii) the iroDE genes were important for generation of S1, S5, and SX; (iv) iroC was required for export of salmochelin trimers and dimers; and (v) iroB was required for generation of salmochelins. Overall, efficient glucosylation (IroB), transport (IroC and IroN), and processing (IroD and IroE) of salmochelins are required for APEC virulence, although IroE appears to serve an ancillary role.

scholarly journals Evidence that Biosynthesis of the Second and Third Sugars of the Archaellin Tetrasaccharide in the Archaeon Methanococcus maripaludis Occurs by the Same Pathway Used by Pseudomonas aeruginosa To Make a Di-N-Acetylated Sugar

2015 ◽  
Vol 197 (9) ◽  
pp. 1668-1680 ◽  
Author(s):  
Sarah Siu ◽  
Anna Robotham ◽  
Susan M. Logan ◽  
John F. Kelly ◽  
Kaoru Uchida ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Mass Spectroscopy ◽  
Specific Antigen ◽  
Mass Spectrometry Analysis ◽  
Methanococcus Maripaludis ◽  
Western Blots ◽  
Bacterial Gene ◽  
Content Type ◽  
Spectrometry Analysis ◽  
Type Iv

ABSTRACTMethanococcus maripaludishas two surface appendages, archaella and type IV pili, which are composed of glycoprotein subunits. Archaellins are modified with an N-linked tetrasaccharide with the structure Sug-1,4-β-ManNAc3NAmA6Thr-1,4-β-GlcNAc3NAcA-1,3-β-GalNAc, where Sug is (5S)-2-acetamido-2,4-dideoxy-5-O-methyl-α-l-erythro-hexos-5-ulo-1,5-pyranose. The pilin glycan has an additional hexose attached to GalNAc. In this study, genes located in two adjacent, divergently transcribed operons (mmp0350-mmp0354andmmp0359-mmp0355) were targeted for study based on annotations suggesting their involvement in biosynthesis of N-glycan sugars. Mutants carrying deletions inmmp0350,mmp0351,mmp0352, ormmp0353were nonarchaellated and synthesized archaellins modified with a 1-sugar glycan, as estimated from Western blots. Mass spectroscopy analysis of pili purified from the Δmmp0352strain confirmed a glycan with only GalNAc, suggestingmmp0350tommp0353were all involved in biosynthesis of the second sugar (GlcNAc3NAcA). The Δmmp0357mutant was archaellated and had archaellins with a 2-sugar glycan, as confirmed by mass spectroscopy of purified archaella, indicating a role for MMP0357 in biosynthesis of the third sugar (ManNAc3NAmA6Thr).M. maripaludismmp0350,mmp0351,mmp0352,mmp0353, andmmp0357are proposed to be functionally equivalent toPseudomonas aeruginosawbpABEDI, involved in converting UDP-N-acetylglucosamine to UDP-2,3-diacetamido-2,3-dideoxy-d-mannuronic acid, an O5-specific antigen sugar. Cross-domain complementation of the final step of theP. aeruginosapathway withmmp0357supports this hypothesis.IMPORTANCEThis work identifies a series of genes in adjacent operons that are shown to encode the enzymes that complete the entire pathway for generation of the second and third sugars of the N-linked tetrasaccharide that modifies archaellins ofMethanococcus maripaludis. This posttranslational modification of archaellins is important, as it is necessary for archaellum assembly. Pilins are modified with a different N-glycan consisting of the archaellin tetrasaccharide but with an additional hexose attached to the linking sugar. Mass spectrometry analysis of the pili of one mutant strain provided insight into how this different glycan might ultimately be assembled. This study includes a rare example of an archaeal gene functionally replacing a bacterial gene in a complex sugar biosynthesis pathway.

scholarly journals Determination of the lipid composition of the GPI anchor

PLoS ONE ◽  
2021 ◽  
Vol 16 (8) ◽  
pp. e0256184
Author(s):  
Auxiliadora Aguilera-Romero ◽  
Susana Sabido-Bozo ◽  
Sergio Lopez ◽  
Alejandro Cortes-Gomez ◽  
Sofia Rodriguez-Gallardo ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Lipid Composition ◽  
Surface Proteins ◽  
Mass Spectrometry Analysis ◽  
Gpi Anchor ◽  
Spectrometry Analysis ◽  
Lipid Structure ◽  
Lipid Moiety ◽  
Protein Lipidation

In eukaryotic cells, a subset of cell surface proteins is attached by the glycolipid glycosylphosphatidylinositol (GPI) to the external leaflet of the plasma membrane where they play important roles as enzymes, receptors, or adhesion molecules. Here we present a protocol for purification and mass spectrometry analysis of the lipid moiety of individual GPI-anchored proteins (GPI-APs) in yeast. The method involves the expression of a specific GPI-AP tagged with GFP, solubilization, immunoprecipitation, separation by electrophoresis, blotting onto PVDF, release and extraction of the GPI-lipid moiety and analysis by mass spectrometry. By using this protocol, we could determine the precise GPI-lipid structure of the GPI-AP Gas1-GFP in a modified yeast strain. This protocol can be used to identify the lipid composition of the GPI anchor of distinct GPI-APs from yeast to mammals and can be adapted to determine other types of protein lipidation.

Software-Supported Selection of Cell Surface Proteins for Cell Stratification and Chimeric Antigen Receptor-Based Therapies

Blood ◽  
2014 ◽  
Vol 124 (21) ◽  
pp. 5116-5116 ◽  
Author(s):  
Christian Simon ◽  
Barnkob Mike ◽  
Lars Rønn Olsen
Keyword(s):  
Cell Surface ◽  
Protein Expression ◽  
Hematopoietic Cells ◽  
Surface Protein ◽  
Surface Proteins ◽  
Surface Molecules ◽  
Surface Protein Expression ◽  
Surface Profiles ◽  
Definition Of ◽  
Selection Of

Abstract Hematopoietic cells and cell surface molecules have both been defined in the hundreds, and the cell-specific profiles arising from the presence of specific proteins on the surface of different cells or biological states (e.g. developmental stages, disease states, etc.) represent data of high combinatorial complexity. The dynamic surface marker profiles of cells have been extensively used for cell sorting and for therapeutics where specific surface markers are used to direct therapeutic agents to diseased cells, using either monoclonal antibodies or cell-based therapies. Immunophenotyping is commonly used to define and sort cells based on the proteins present on their surface. In order to efficiently separate similar cells, a large number of surface proteins are often used. Complete knowledge about unique, cell-specific profiles of surface protein expression are likely to reveal much simpler surface profiles than currently used, as well as the definition of surface profiles where non are currently defined. In cancer immunotherapy, adoptive transfer of chimeric antigen receptor (CAR) engineered T cells show promise as therapy modality. Currently, the main achievements utilizing this technique have been made targeting single malignancy-specific surface molecules, but progress is being made in requiring binding of several ligands before lymphocyte activation, which will increases the specificity of the therapy and thereby decrease off-target effects. Defining surface protein expression profiles for cell stratification and CAR therapy in silicorequires information about expression of a large number of surface proteins on a large number of cells. At present, no high-throughput technique for measuring surface protein expression exists, although efforts to increase throughput using mass spectrometry and computational prediction of protein expression from mRNA expression are being explored. However, surface molecule expression on individual cells has been characterized at low rates using immunohistochemistry or flow cytometry for decades, and vast amounts of cell-specific expression has been measured and published. This represents a rich, but unstructured source of data and information. To facilitate the definition of unique surface molecule profiles, we collected and organized large amounts of these data of human hematopoietic cells and the corresponding quantitative or qualitative presence (depending on availability) of known molecular surface molecules from the primary literature. To do so, we employed text mining techniques for article classification (as either containing information about surface protein expression or not) and subsequently extensive manual curation to assemble the data foundation for defining cell surface profiles for stratification and therapy. To analyze these data, we have developed algorithms for selection of cell surface protein for cell stratification and for target selection for CAR-based therapies. The resulting database contains expression of 305 surface proteins across 206 hematopoietic cells, totaling 6153 data points. We have applied our algorithm to define unique profiles for each of the 206 cells, thus characterizing the surface profiles of the majority of hematopoietic cells to increase efficiency and specificity of cell stratification and therapy targeting. Future efforts will include expanding the database to contain surface protein expression for cells in all human tissues, as well as experimental validation of discovered surface profiles. Disclosures No relevant conflicts of interest to declare.

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