Proteomes

13 pages, 1785 KiB

Open AccessReview

Proteome Discoverer—A Community Enhanced Data Processing Suite for Protein Informatics

by Benjamin C. Orsburn

Proteomes 2021, 9(1), 15; https://doi.org/10.3390/proteomes9010015 - 23 Mar 2021

Cited by 128 | Viewed by 10797

Proteomics researchers today face an interesting challenge: how to choose among the dozens of data processing and analysis pipelines available for converting tandem mass spectrometry files to protein identifications. Due to the dominance of Orbitrap technology in proteomics in recent history, many researchers [...] Read more.

Proteomics researchers today face an interesting challenge: how to choose among the dozens of data processing and analysis pipelines available for converting tandem mass spectrometry files to protein identifications. Due to the dominance of Orbitrap technology in proteomics in recent history, many researchers have defaulted to the vendor software Proteome Discoverer. Over the fourteen years since the initial release of the software, it has evolved in parallel with the increasingly complex demands faced by proteomics researchers. Today, Proteome Discoverer exists in two distinct forms with both powerful commercial versions and fully functional free versions in use in many labs today. Throughout the 11 main versions released to date, a central theme of the software has always been the ability to easily view and verify the spectra from which identifications are made. This ability is, even today, a key differentiator from other data analysis solutions. In this review I will attempt to summarize the history and evolution of Proteome Discoverer from its first launch to the versions in use today. Full article

(This article belongs to the Special Issue Feature Review Papers in Proteomes)

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16 pages, 1588 KiB

Open AccessArticle

Corynebacterium diphtheriae Proteome Adaptation to Cell Culture Medium and Serum

by Jens Möller, Fatemeh Nosratabadi, Luca Musella, Jörg Hofmann and Andreas Burkovski

Proteomes 2021, 9(1), 14; https://doi.org/10.3390/proteomes9010014 - 13 Mar 2021

Cited by 3 | Viewed by 4589

Abstract

Host-pathogen interactions are often studied in vitro using primary or immortal cell lines. This set-up avoids ethical problems of animal testing and has the additional advantage of lower costs. However, the influence of cell culture media on bacterial growth and metabolism is not [...] Read more.

Host-pathogen interactions are often studied in vitro using primary or immortal cell lines. This set-up avoids ethical problems of animal testing and has the additional advantage of lower costs. However, the influence of cell culture media on bacterial growth and metabolism is not considered or investigated in most cases. To address this question growth and proteome adaptation of Corynebacterium diphtheriae strain ISS3319 were investigated in this study. Bacteria were cultured in standard growth medium, cell culture medium, and fetal calf serum. Mass spectrometric analyses and label-free protein quantification hint at an increased bacterial pathogenicity when grown in cell culture medium as well as an influence of the growth medium on the cell envelope. Full article

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18 pages, 2206 KiB

Open AccessReview

Proteomics Landscape of Alzheimer’s Disease

by Ankit P. Jain and Gajanan Sathe

Proteomes 2021, 9(1), 13; https://doi.org/10.3390/proteomes9010013 - 10 Mar 2021

Cited by 8 | Viewed by 6711

Abstract

Alzheimer’s disease (AD) is the most prevalent form of dementia, and the numbers of AD patients are expected to increase as human life expectancy improves. Deposition of β-amyloid protein (Aβ) in the extracellular matrix and intracellular neurofibrillary tangles are molecular hallmarks of the [...] Read more.

Alzheimer’s disease (AD) is the most prevalent form of dementia, and the numbers of AD patients are expected to increase as human life expectancy improves. Deposition of β-amyloid protein (Aβ) in the extracellular matrix and intracellular neurofibrillary tangles are molecular hallmarks of the disease. Since the precise pathophysiology of AD has not been elucidated yet, effective treatment is not available. Thus, understanding the disease pathology, as well as identification and development of valid biomarkers, is imperative for early diagnosis as well as for monitoring disease progression and therapeutic responses. Keeping this goal in mind several studies using quantitative proteomics platform have been carried out on both clinical specimens including the brain, cerebrospinal fluid (CSF), plasma and on animal models of AD. In this review, we summarize the mass spectrometry (MS)-based proteomics studies on AD and discuss the discovery as well as validation stages in brief to identify candidate biomarkers. Full article

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16 pages, 1577 KiB

Open AccessReview

C1q Complement/Tumor Necrosis Factor-Associated Proteins in Cardiovascular Disease and COVID-19

by Yaoli Xie, Zhijun Meng, Jia Gao, Caihong Liu, Jing Wang, Rui Guo, Jianli Zhao, Bernard Lopez, Theodore Christopher, Daniel Lee, Xinliang Ma and Yajing Wang

Proteomes 2021, 9(1), 12; https://doi.org/10.3390/proteomes9010012 - 1 Mar 2021

Cited by 8 | Viewed by 4568

Abstract

With continually improving treatment strategies and patient care, the overall mortality of cardiovascular disease (CVD) has been significantly reduced. However, this success is a double-edged sword, as many patients who survive cardiovascular complications will progress towards a chronic disorder over time. A family [...] Read more.

With continually improving treatment strategies and patient care, the overall mortality of cardiovascular disease (CVD) has been significantly reduced. However, this success is a double-edged sword, as many patients who survive cardiovascular complications will progress towards a chronic disorder over time. A family of adiponectin paralogs designated as C1q complement/tumor necrosis factor (TNF)-associated proteins (CTRPs) has been found to play a role in the development of CVD. CTRPs, which are comprised of 15 members, CTRP1 to CTRP15, are secreted from different organs/tissues and exhibit diverse functions, have attracted increasing attention because of their roles in maintaining inner homeostasis by regulating metabolism, inflammation, and immune surveillance. In particular, studies indicate that CTRPs participate in the progression of CVD, influencing its prognosis. This review aims to improve understanding of the role of CTRPs in the cardiovascular system by analyzing current knowledge. In particular, we examine the association of CTRPs with endothelial cell dysfunction, inflammation, and diabetes, which are the basis for development of CVD. Additionally, the recently emerged novel coronavirus (COVID-19), officially known as severe acute respiratory syndrome-coronavirus-2 (SARS-CoV-2), has been found to trigger severe cardiovascular injury in some patients, and evidence indicates that the mortality of COVID-19 is much higher in patients with CVD than without CVD. Understanding the relationship of CTRPs and the SARS-CoV-2-related damage to the cardiovascular system, as well as the potential mechanisms, will achieve a profound insight into a therapeutic strategy to effectively control CVD and reduce the mortality rate. Full article

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14 pages, 3071 KiB

Open AccessReview

Regenerative Potential of Enamel Matrix Protein Derivative and Acellular Dermal Matrix for Gingival Recession: A Systematic Review and Meta-Analysis

by Muhammad Saad Shaikh, Mohid Abrar Lone, Hesham Matabdin, Muneeb Ahmed Lone, Azeem Hussain Soomro and Muhammad Sohail Zafar

Proteomes 2021, 9(1), 11; https://doi.org/10.3390/proteomes9010011 - 25 Feb 2021

Cited by 14 | Viewed by 3867

Abstract

Objective: The purpose of this study was to assess the clinical effectiveness of using a combination of enamel matrix protein derivative and acellular dermal matrix in comparison to acellular dermal matrix alone for treating gingival recessions. Methods: The Cochrane Library (Wiley), PubMed by [...] Read more.

Objective: The purpose of this study was to assess the clinical effectiveness of using a combination of enamel matrix protein derivative and acellular dermal matrix in comparison to acellular dermal matrix alone for treating gingival recessions. Methods: The Cochrane Library (Wiley), PubMed by Medline (NLM), Medline (EBSCO), and Embase (Ovid) databases were searched for entries up to April 2020. Only clinical trials were included. Primary outcomes were root coverage (%), changes in keratinized tissue width and recession (mm). Meta-analysis was conducted for root coverage, changes in keratinized tissue width, recession, clinical attachment level and probing depth. Results: Four studies were selected for the analysis. In primary outcomes, root coverage, change in keratinized tissue width and recession analysis showed a mean difference of 4.99% (p = 0.11), 0.20 mm (p = 0.14) and 0.13 mm (p = 0.23) respectively between the two groups. Secondary outcomes analysis also exhibited a statistically insignificant difference between the test and control group with mean difference of 0.11 mm (p = 0.32) in clinical attachment level gain and -0.03 mm (p = 0.29) in probing depth reduction analysis. Conclusions: Within the limits of this study, enamel matrix protein derivative combined with acellular dermal matrix used for treating gingival recession defects resulted in no beneficial effect clinically than acellular dermal matrix only. Full article

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14 pages, 4336 KiB

Open AccessArticle

Exoproteome Perspective on the Bile Stress Response of Lactobacillus johnsonii

by Bernadette B. Bagon, Valerie Diane V. Valeriano, Ju Kyoung Oh, Edward Alain B. Pajarillo, Ji Yoon Lee and Dae-Kyung Kang

Proteomes 2021, 9(1), 10; https://doi.org/10.3390/proteomes9010010 - 10 Feb 2021

Cited by 10 | Viewed by 3039

Abstract

Probiotics must not only exert a health-promoting effect but also be capable of adapting to the harsh environment of the gastrointestinal (GI) tract. Probiotics in the GI tract must survive the cell wall-disrupting effect of bile acids. We investigated the exoproteome of Lactobacillus [...] Read more.

Probiotics must not only exert a health-promoting effect but also be capable of adapting to the harsh environment of the gastrointestinal (GI) tract. Probiotics in the GI tract must survive the cell wall-disrupting effect of bile acids. We investigated the exoproteome of Lactobacillus johnsonii PF01 and C1-10 under bile stress. A comparative analysis revealed the similarities between the two L. johnsonii exoproteomes, as well as their different responses to bile. The large number of metabolic proteins in L. johnsonii revealed its metabolic adaptation to meet protein synthesis requirements under bile stress. In addition, cell wall modifications occurred in response to bile. Furthermore, some extracellular proteins of L. johnsonii may have moonlighting function in the presence of bile. Enolase, L-lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase, triosephosphate isomerase, 50s ribosomal protein L7/L12, and cellobiose-specific phosphotransferase system (PTS) sugar transporter were significantly upregulated under bile stress, suggesting a leading role in the collective bile stress response of L. johnsonii from its exoproteome perspective. Full article

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20 pages, 4606 KiB

Open AccessReview

The Dystrophin Node as Integrator of Cytoskeletal Organization, Lateral Force Transmission, Fiber Stability and Cellular Signaling in Skeletal Muscle

by Paul Dowling, Stephen Gargan, Sandra Murphy, Margit Zweyer, Hemmen Sabir, Dieter Swandulla and Kay Ohlendieck

Proteomes 2021, 9(1), 9; https://doi.org/10.3390/proteomes9010009 - 2 Feb 2021

Cited by 28 | Viewed by 9418

Abstract

The systematic bioanalytical characterization of the protein product of the DMD gene, which is defective in the pediatric disorder Duchenne muscular dystrophy, led to the discovery of the membrane cytoskeletal protein dystrophin. Its full-length muscle isoform Dp427-M is tightly linked to a sarcolemma-associated [...] Read more.

The systematic bioanalytical characterization of the protein product of the DMD gene, which is defective in the pediatric disorder Duchenne muscular dystrophy, led to the discovery of the membrane cytoskeletal protein dystrophin. Its full-length muscle isoform Dp427-M is tightly linked to a sarcolemma-associated complex consisting of dystroglycans, sarcoglyans, sarcospan, dystrobrevins and syntrophins. Besides these core members of the dystrophin–glycoprotein complex, the wider dystrophin-associated network includes key proteins belonging to the intracellular cytoskeleton and microtubular assembly, the basal lamina and extracellular matrix, various plasma membrane proteins and cytosolic components. Here, we review the central role of the dystrophin complex as a master node in muscle fibers that integrates cytoskeletal organization and cellular signaling at the muscle periphery, as well as providing sarcolemmal stabilization and contractile force transmission to the extracellular region. The combination of optimized tissue extraction, subcellular fractionation, advanced protein co-purification strategies, immunoprecipitation, liquid chromatography and two-dimensional gel electrophoresis with modern mass spectrometry-based proteomics has confirmed the composition of the core dystrophin complex at the sarcolemma membrane. Importantly, these biochemical and mass spectrometric surveys have identified additional members of the wider dystrophin network including biglycan, cavin, synemin, desmoglein, tubulin, plakoglobin, cytokeratin and a variety of signaling proteins and ion channels. Full article

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29 pages, 1869 KiB

Open AccessReview

Exosome-Derived Mediators as Potential Biomarkers for Cardiovascular Diseases: A Network Approach

by Liliana Moreira-Costa, António S. Barros, André P. Lourenço, Adelino F. Leite-Moreira, Rita Nogueira-Ferreira, Visith Thongboonkerd and Rui Vitorino

Proteomes 2021, 9(1), 8; https://doi.org/10.3390/proteomes9010008 - 1 Feb 2021

Cited by 23 | Viewed by 5914

Abstract

Cardiovascular diseases (CVDs) are widely recognized as the leading cause of mortality worldwide. Despite the advances in clinical management over the past decades, the underlying pathological mechanisms remain largely unknown. Exosomes have drawn the attention of researchers for their relevance in intercellular communication [...] Read more.

Cardiovascular diseases (CVDs) are widely recognized as the leading cause of mortality worldwide. Despite the advances in clinical management over the past decades, the underlying pathological mechanisms remain largely unknown. Exosomes have drawn the attention of researchers for their relevance in intercellular communication under both physiological and pathological conditions. These vesicles are suggested as complementary prospective biomarkers of CVDs; however, the role of exosomes in CVDs is still not fully elucidated. Here, we performed a literature search on exosomal biogenesis, characteristics, and functions, as well as the different available exosomal isolation techniques. Moreover, aiming to give new insights into the interaction between exosomes and CVDs, network analysis on the role of exosome-derived mediators in coronary artery disease (CAD) and heart failure (HF) was also performed to incorporate the different sources of information. The upregulated exosomal miRNAs miR-133a, miR-208a, miR-1, miR-499-5p, and miR-30a were described for the early diagnosis of acute myocardial infarction, while the exosome-derived miR-192, miR-194, miR-146a, and miR-92b-5p were considered as potential biomarkers for HF development. In CAD patients, upregulated exosomal proteins, including fibrinogen beta/gamma chain, inter-alpha-trypsin inhibitor heavy chain, and alpha-1 antichymotrypsin, were assessed as putative protein biomarkers. From downregulated proteins in CAD patients, albumin, clusterin, and vitamin D-binding protein were considered relevant to assess prognosis. The Vesiclepedia database included miR-133a of exosomal origin upregulated in patients with CAD and the exosomal miR-192, miR-194, and miR-146a upregulated in patients with HF. Additionally, Vesiclepedia included 5 upregulated and 13 downregulated exosomal proteins in patients in CAD. The non-included miRNAs and proteins have not yet been identified in exosomes and can be proposed for further research. This report highlights the need for further studies focusing on the identification and validation of miRNAs and proteins of exosomal origin as biomarkers of CAD and HF, which will enable, using exosomal biomarkers, the guiding of diagnosis/prognosis in CVDs. Full article

(This article belongs to the Special Issue Functional Proteomics 2020)

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18 pages, 329 KiB

Open AccessReview

Insights into Mycobacterium leprae Proteomics and Biomarkers—An Overview

by Sakshi Gautam, Devesh Sharma, Anjana Goel, Shripad A. Patil and Deepa Bisht

Proteomes 2021, 9(1), 7; https://doi.org/10.3390/proteomes9010007 - 29 Jan 2021

Cited by 14 | Viewed by 4154

Abstract

Although leprosy is curable, the identification of biomarkers for the early diagnosis of leprosy would play a pivotal role in reducing transmission and the overall prevalence of the disease. Leprosy-specific biomarkers for diagnosis, particularly for the paucibacillary disease, are not well defined. Therefore, [...] Read more.

Although leprosy is curable, the identification of biomarkers for the early diagnosis of leprosy would play a pivotal role in reducing transmission and the overall prevalence of the disease. Leprosy-specific biomarkers for diagnosis, particularly for the paucibacillary disease, are not well defined. Therefore, the identification of new biomarkers for leprosy is one of the prime themes of leprosy research. Studying Mycobacterium leprae, the causative agent of leprosy, at the proteomic level may facilitate the identification, quantification, and characterization of proteins that could be potential diagnostics or targets for drugs and can help in better understanding the pathogenesis. This review aims to shed light on the knowledge gained to understand leprosy or its pathogen employing proteomics and its role in diagnosis. Full article

19 pages, 3383 KiB

Open AccessArticle

In-Depth Analysis of the Plasma Proteome in ME/CFS Exposes Disrupted Ephrin-Eph and Immune System Signaling

by Arnaud Germain, Susan M. Levine and Maureen R. Hanson

Proteomes 2021, 9(1), 6; https://doi.org/10.3390/proteomes9010006 - 29 Jan 2021

Cited by 12 | Viewed by 12451

Abstract

Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS) is a disabling disease with worldwide prevalence and limited therapies exclusively aimed at treating symptoms. To gain insights into the molecular disruptions in ME/CFS, we utilized an aptamer-based technology that quantified 4790 unique human proteins, allowing us to [...] Read more.

Myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS) is a disabling disease with worldwide prevalence and limited therapies exclusively aimed at treating symptoms. To gain insights into the molecular disruptions in ME/CFS, we utilized an aptamer-based technology that quantified 4790 unique human proteins, allowing us to obtain the largest proteomics dataset yet available for this disease, detecting highly abundant proteins as well as rare proteins over a nine-log dynamic range. We report a pilot study of 20 ME/CFS patients and 20 controls, all females. Significant differences in the levels of 19 proteins between cohorts implicate pathways related to the extracellular matrix, the immune system and cell–cell communication. Outputs of pathway and cluster analyses robustly highlight the ephrin pathway, which is involved in cell–cell signaling and regulation of an expansive variety of biological processes, including axon guidance, angiogenesis, epithelial cell migration, and immune response. Receiver Operating Characteristic (ROC) curve analyses distinguish the plasma proteomes of ME/CFS patients from controls with a high degree of accuracy (Area Under the Curve (AUC) > 0.85), and even higher when using protein ratios (AUC up to 0.95), that include some protein pairs with established biological relevance. Our results illustrate the promise of plasma proteomics for diagnosing and deciphering the molecular basis of ME/CFS. Full article

(This article belongs to the Special Issue Functional Proteomics 2020)

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2 pages, 155 KiB

Open AccessEditorial

Acknowledgment to Reviewers of Proteomes in 2020

by Proteomes Editorial Office

Proteomes 2021, 9(1), 5; https://doi.org/10.3390/proteomes9010005 - 28 Jan 2021

Viewed by 1605

Abstract

Peer review is the driving force of journal development, and reviewers are gatekeepers who ensure that Proteomes maintains its standards for the high quality of its published papers [...] Full article

17 pages, 4747 KiB

Open AccessArticle

Targeted Quantification of the Lysosomal Proteome in Complex Samples

by Peter Mosen, Anne Sanner, Jasjot Singh and Dominic Winter

Proteomes 2021, 9(1), 4; https://doi.org/10.3390/proteomes9010004 - 26 Jan 2021

Cited by 16 | Viewed by 6447

Abstract

In eukaryotic cells, lysosomes play a crucial role in the breakdown of a variety of components ranging from small molecules to complex structures, ascertaining the continuous turnover of cellular building blocks. Furthermore, they act as a regulatory hub for metabolism, being crucially involved [...] Read more.

In eukaryotic cells, lysosomes play a crucial role in the breakdown of a variety of components ranging from small molecules to complex structures, ascertaining the continuous turnover of cellular building blocks. Furthermore, they act as a regulatory hub for metabolism, being crucially involved in the regulation of major signaling pathways. Currently, ~450 lysosomal proteins can be reproducibly identified in a single cell line by mass spectrometry, most of which are low-abundant, restricting their unbiased proteomic analysis to lysosome-enriched fractions. In the current study, we applied two strategies for the targeted investigation of the lysosomal proteome in complex samples: data-independent acquisition (DIA) and parallel reaction monitoring (PRM). Using a lysosome-enriched fraction, mouse embryonic fibroblast whole cell lysate, and mouse liver whole tissue lysate, we investigated the capabilities of DIA and PRM to investigate the lysosomal proteome. While both approaches identified and quantified lysosomal proteins in all sample types, and their data largely correlated, DIA identified on average more proteins, especially for lower complex samples and longer chromatographic gradients. For the highly complex tissue sample and shorter gradients, however, PRM delivered a better performance regarding both identification and quantification of lysosomal proteins. All data are available via ProteomeXchange with identifier PXDD023278. Full article

(This article belongs to the Special Issue Targeted Analyses of Proteomes)

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8 pages, 506 KiB

Open AccessArticle

Proteomics-Based Regression Model for Assessing the Development of Chronic Lymphocytic Leukemia

by Varvara I. Bakhtina, Dmitry V. Veprintsev, Tatiana N. Zamay, Irina V. Demko, Gleb G. Mironov, Maxim V. Berezovski, Marina M. Petrova, Anna S. Kichkailo and Yury E. Glazyrin

Proteomes 2021, 9(1), 3; https://doi.org/10.3390/proteomes9010003 - 23 Jan 2021

Cited by 1 | Viewed by 2801

Abstract

The clinical course of chronic lymphocytic leukemia (CLL) is very ambiguous, showing either an indolent nature of the disease or having latent dangerous progression, which, if diagnosed, will require an urgent therapy. The prognosis of the course of the disease and the estimation [...] Read more.

The clinical course of chronic lymphocytic leukemia (CLL) is very ambiguous, showing either an indolent nature of the disease or having latent dangerous progression, which, if diagnosed, will require an urgent therapy. The prognosis of the course of the disease and the estimation of the time of therapy initiation are crucial for the selection of a successful treatment strategy. A reliable estimating index is needed to assign newly diagnosed CLL patients to the prognostic groups. In this work, we evaluated the comparative expressions of proteins in CLL blood cells using a label-free quantification by mass spectrometry and calculated the integrated proteomic indexes for a group of patients who received therapy after the blood sampling over different periods of time. Using a two-factor linear regression analysis based on these data, we propose a new pipeline for evaluating model development for estimation of the moment of therapy initiation for newly diagnosed CLL patients. Full article

(This article belongs to the Special Issue Proteomics in Cancer and Personalized Medicine)

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20 pages, 1318 KiB

Open AccessReview

Misincorporation Proteomics Technologies: A Review

by Joel R. Steele, Carly J. Italiano, Connor R. Phillips, Jake P. Violi, Lisa Pu, Kenneth J. Rodgers and Matthew P. Padula

Proteomes 2021, 9(1), 2; https://doi.org/10.3390/proteomes9010002 - 21 Jan 2021

Cited by 5 | Viewed by 5081 | Correction

Abstract

Proteinopathies are diseases caused by factors that affect proteoform conformation. As such, a prevalent hypothesis is that the misincorporation of noncanonical amino acids into a proteoform results in detrimental structures. However, this hypothesis is missing proteomic evidence, specifically the detection of a noncanonical [...] Read more.

Proteinopathies are diseases caused by factors that affect proteoform conformation. As such, a prevalent hypothesis is that the misincorporation of noncanonical amino acids into a proteoform results in detrimental structures. However, this hypothesis is missing proteomic evidence, specifically the detection of a noncanonical amino acid in a peptide sequence. This review aims to outline the current state of technology that can be used to investigate mistranslations and misincorporations whilst framing the pursuit as Misincorporation Proteomics (MiP). The current availability of technologies explored herein is mass spectrometry, sample enrichment/preparation, data analysis techniques, and the hyphenation of approaches. While many of these technologies show potential, our review reveals a need for further development and refinement of approaches is still required. Full article

(This article belongs to the Special Issue Proteomics: Technologies and Their Applications)

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21 pages, 1885 KiB

Open AccessArticle

Secretome Analysis of Clavibacter nebraskensis Strains Treated with Natural Xylem Sap In Vitro Predicts Involvement of Glycosyl Hydrolases and Proteases in Bacterial Aggressiveness

by Atta Soliman, Christof Rampitsch, James T. Tambong and Fouad Daayf

Proteomes 2021, 9(1), 1; https://doi.org/10.3390/proteomes9010001 - 9 Jan 2021

Cited by 8 | Viewed by 3184

Abstract

The Gram-positive bacterium Clavibacter nebraskensis (Cn) causes Goss’s wilt and leaf blight on corn in the North American Central Plains with yield losses as high as 30%. Cn strains vary in aggressiveness on corn, with highly aggressive strains causing much more serious symptoms [...] Read more.

The Gram-positive bacterium Clavibacter nebraskensis (Cn) causes Goss’s wilt and leaf blight on corn in the North American Central Plains with yield losses as high as 30%. Cn strains vary in aggressiveness on corn, with highly aggressive strains causing much more serious symptoms and damage to crops. Since Cn inhabits the host xylem, we investigated differences in the secreted proteomes of Cn strains to determine whether these could account for phenotypic differences in aggressiveness. Highly and a weakly aggressive Cn strains (Cn14-15-1 and DOAB232, respectively) were cultured, in vitro, in the xylem sap of corn (CXS; host) and tomato (TXS; non-host). The secretome of the Cn strains were extracted and processed, and a comparative bottom-up proteomics approach with liquid chromatography–tandem mass spectrometry (LC–MS/MS) was used to determine their identities and concentration. Relative quantitation of peptides was based on precursor ion intensities to measure protein abundances. In total, 745 proteins were identified in xylem sap media. In CXS, a total of 658 and 396 proteins were identified in strains Cn14-5-1 and DOAB232, respectively. The unique and the differentially abundant proteins in the secretome of strain Cn14-5-1 were higher in either sap medium compared to DOAB232. These proteins were sorted using BLAST2GO and assigned to 12 cellular functional processes. Virulence factors, e.g., cellulase, β-glucosidase, β-galactosidase, chitinase, β-1,4-xylanase, and proteases were generally higher in abundance in the aggressive Cn isolate. This was corroborated by enzymatic activity assays of cellulase and protease in CXS. These proteins were either not detected or detected at significantly lower abundance levels in Cn strains grown in non-host xylem sap (tomato), suggesting potential factors involved in Cn–host (corn) interactions. Full article

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