scholarly journals Muscle Proteome Analysis for the Effect of Panax Ginseng Extracts in Chicken: Identification of Proteins Using Peptide Mass Fingerprinting

2005 ◽  
Vol 18 (7) ◽  
pp. 922-926 ◽  
Author(s):  
K. C. Jung ◽  
S. L. Yu ◽  
Y. J. Lee ◽  
K. D. Choi ◽  
J. S. Choi ◽  
...  
Keyword(s):  
Panax Ginseng ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Peptide Mass ◽  
Muscle Proteome

scholarly journals Hypoxic Response of Mycobacterium tuberculosis Studied by Metabolic Labeling and Proteome Analysis of Cellular and Extracellular Proteins

2002 ◽  
Vol 184 (13) ◽  
pp. 3485-3491 ◽  
Author(s):  
Ida Rosenkrands ◽  
Richard A. Slayden ◽  
Janne Crawford ◽  
Claus Aagaard ◽  
Clifton E. Barry ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Extracellular Proteins ◽  
Metabolic Labeling ◽  
Low Oxygen ◽  
Hypoxic Response ◽  
Peptide Mass ◽  
Oxygen Conditions

ABSTRACT The events involved in the establishment of a latent infection with Mycobacterium tuberculosis are not fully understood, but hypoxic conditions are generally believed to be the environment encountered by the pathogen in the central part of the granuloma. The present study was undertaken to provide insight into M. tuberculosis protein expression in in vitro latency models where oxygen is depleted. The response of M. tuberculosis to low-oxygen conditions was investigated in both cellular and extracellular proteins by metabolic labeling, two-dimensional electrophoresis, and protein signature peptide analysis by liquid chromatography-mass spectrometry. By peptide mass fingerprinting and immunodetection, five proteins more abundant under low-oxygen conditions were identified from several lysates of M. tuberculosis: Rv0569, Rv2031c (HspX), Rv2623, Rv2626c, and Rv3841 (BfrB). In M. tuberculosis culture filtrates, two additional proteins, Rv0363c (Fba) and Rv2780 (Ald), were found in increased amounts under oxygen limitation. These results extend our understanding of the hypoxic response in M. tuberculosis and potentially provide important insights into the physiology of the latent bacilli.

scholarly journals Functional Genomic Analysis of Global Regulator NolR in Sinorhizobium meliloti

2005 ◽  
Vol 18 (12) ◽  
pp. 1340-1352 ◽  
Author(s):  
Hancai Chen ◽  
Ke Gao ◽  
Eva Kondorosi ◽  
Adam Kondorosi ◽  
Barry G. Rolfe
Keyword(s):  
Sinorhizobium Meliloti ◽  
Regulatory Protein ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Nucleotide Metabolism ◽  
Conjugative Transfer ◽  
Environmental Stimuli ◽  
Peptide Mass ◽  
Functional Genomic Analysis ◽  
Associated Proteins

NolR is a regulator of nodulation genes present in species belonging to the genera Rhizobium and Sinorhizobium. The expression of the nolR gene in Sinorhizobium meliloti AK631 was investigated in relation to stage of growth, availability of nutrients, and different environmental stimuli using the nolR::lacZ fusion report system. It has been shown that the nolR gene is regulated in a population-density-dependent fashion and influenced by a number of environmental stimuli, including nutrients, pH, and oxygen. Exploration of the physiological functions of NolR under various laboratory conditions has shown that NolR is required for the optimal growth of the bacteria on solid media, optimal survival of the bacteria in carbon-starved minimal medium, and after heat shock challenge. NolR also is involved in recipient-induced conjugative transfer of a plasmid. Proteome analysis of strain AK631 and its Tn5-induced nolR-deficient mutant EK698 revealed that a functional NolR induced significant differences in the accumulation of 20 polypeptides in peptide mass fingerprinting early-log-phase cultures and 48 polypeptides in stationary-phase cultures. NolR acted mainly as a repressor in the early-log-phase cultures, whereas it acted as both repressor and activator in the stationaryphase cultures. The NolR protein and 59 NolR-associated proteins have been identified by peptide mass fingerprinting. The NolR protein was differentially expressed only in the NolR+ wild-type strain AK631 but not in its NolR- derivative EK698, confirming that no functional NolR was produced in the mutant. The NolR-associated proteins have diverse functions in amino acid metabolism, carbohydrate metabolism, lipid metabolism, nucleotide metabolism, energy metabolism, metabolism of Co-factors, and cellular adaptation and transportation. These results further support our previous proposal that the NolR is a global regulatory protein which is required for the optimization of nodulation, bacterial growth and survival, and conjugative transfer of a plasmid.

Comparative proteome analysis of drought-sensitive and drought-tolerant maize leaves under osmotic stress

2019 ◽  
Vol 99 (4) ◽  
pp. 467-479
Author(s):  
Yuhe Pei ◽  
Jianfen Bai ◽  
Xinmei Guo ◽  
Meiai Zhao ◽  
Qingmei Ma ◽  
...  
Keyword(s):  
Osmotic Stress ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Inbred Lines ◽  
Limiting Factor ◽  
Two Dimensional Gel Electrophoresis ◽  
Maize Production ◽  
Drought Tolerant ◽  
Maize Inbred Lines ◽  
Peptide Mass

Drought is a major yield-limiting factor in maize production. Osmotic stress was applied to two maize inbred lines with polyethylene glycol 6000 treatments. Proteins from the leaves were analyzed by two-dimensional gel electrophoresis and peptide mass fingerprinting at two time points, 24 and 48 h after osmotic stress. Thirty-five proteins were differentially expressed between control and treatment groups in the two maize inbred lines. In ‘Qi319’, a drought-tolerant inbred line, there were five up-regulated proteins at 24 h and 13 up-regulated and one down-regulated protein at 48 h. In drought-sensitive line ‘Zheng58’, 10 proteins were up-regulated at 24 h, while six proteins were up-regulated at 48 h. The 35 proteins were subjected to mass spectrometry and 17 proteins were successfully identified. These proteins were classified into six categories: photosynthesis-related, energy and metabolism, signaling pathways, protein synthesis, defense-related, and unclassified.

scholarly journals Proteomic Analysis of Wild-Type Sinorhizobium meliloti Responses to N-Acyl Homoserine Lactone Quorum-Sensing Signals and the Transition to Stationary Phase

2003 ◽  
Vol 185 (17) ◽  
pp. 5029-5036 ◽  
Author(s):  
Hancai Chen ◽  
Max Teplitski ◽  
Jayne B. Robinson ◽  
Barry G. Rolfe ◽  
Wolfgang D. Bauer
Keyword(s):  
Quorum Sensing ◽  
Stationary Phase ◽  
Proteomic Analysis ◽  
Sinorhizobium Meliloti ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Homoserine Lactone ◽  
Wild Type ◽  
Carbon And Nitrogen ◽  
Peptide Mass

ABSTRACT Proteome analysis revealed that two long-chain N-acyl homoserine lactones (AHLs) produced by Sinorhizobium meliloti 1021 induced significant differences in the accumulation of more than 100 polypeptides in early-log-phase cultures of the wild type. Fifty-six of the corresponding proteins have been identified by peptide mass fingerprinting. The proteins affected by addition of these two AHLs had diverse functions in carbon and nitrogen metabolism, energy cycles, metabolite transport, DNA synthesis, and protein turnover. Two hours of exposure to 3-oxo-C16:1-homoserine lactone (3-oxo-C16:1-HL) affected the accumulation of 40 of the 56 identified proteins, whereas comparable exposure to C14-HL affected 13 of the 56 proteins. Levels of four proteins were affected by both AHLs. Exposure to 3-oxo-C16:1-HL for 8 h affected the accumulation of 17 proteins, 12 of which had reduced accumulation. Of the 80 proteins identified as differing in accumulation between early-log- and early-stationary-phase cultures, only 13 were affected by exposure to 3-oxo-C16:1-HL or C14-HL. These results provide a foundation for future studies of the functions regulated by AHL quorum sensing in S. meliloti and help to establish proteomic analysis as a powerful global approach to the identification of quorum-sensing regulatory patterns in wild-type bacteria.

scholarly journals Heat Shock Proteome Analysis of Wild-Type Corynebacterium glutamicum ATCC 13032 and a Spontaneous Mutant Lacking GroEL1, a Dispensable Chaperone

2005 ◽  
Vol 187 (3) ◽  
pp. 884-889 ◽  
Author(s):  
Carlos Barreiro ◽  
Eva González-Lavado ◽  
Sven Brand ◽  
Andreas Tauch ◽  
Juan F. Martín
Keyword(s):  
Heat Shock ◽  
Corynebacterium Glutamicum ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Start Codon ◽  
Northern Analysis ◽  
Spontaneous Mutant ◽  
Wild Type ◽  
Peptide Mass ◽  
Heat Response

ABSTRACT Proteome analysis of Corynebacterium glutamicum ATCC 13032 showed that levels of several proteins increased drastically in response to heat shock. These proteins were identified as DnaK, GroEL1, GroEL2, ClpB, GrpE, and PoxB, and their heat response was in agreement with previous transcriptomic results. A major heat-induced protein was absent in the proteome of strain 13032B of C. glutamicum, used for genome sequencing in Germany, compared with the wild-type ATCC 13032 strain. The missing protein was identified as GroEL1 by matrix-assisted laser desorption ionization-time of flight peptide mass fingerprinting, and the mutation was found to be due to an insertion sequence, IsCg1, that was integrated at position 327 downstream of the translation start codon of the groEL1 gene, resulting in a truncated transcript of this gene, as shown by Northern analysis. The GroEL1 chaperone is, therefore, dispensable in C. glutamicum. On the other hand, GroEL2 appears to be essential for growth. Based on these results, the role of the duplicate groEL1 and groEL2 genes is analyzed.

Automating proteome analysis: improvements in throughput, quality and accuracy of protein identification by peptide mass fingerprinting

2004 ◽  
Vol 18 (23) ◽  
pp. 2785-2794 ◽  
Author(s):  
Ludovic Canelle ◽  
C�dric Pionneau ◽  
Arul Marie ◽  
Jordane Bousquet ◽  
Jean Bigeard ◽  
...  
Keyword(s):  
Protein Identification ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Peptide Mass

scholarly journals Comparative Proteome Analysis of Brucella melitensis Vaccine Strain Rev 1 and a Virulent Strain, 16M

2002 ◽  
Vol 184 (18) ◽  
pp. 4962-4970 ◽  
Author(s):  
Michel Eschenbrenner ◽  
Mary Ann Wagner ◽  
Troy A. Horn ◽  
Jo Ann Kraycer ◽  
Cesar V. Mujer ◽  
...  
Keyword(s):  
Vaccine Strain ◽  
Brucella Melitensis ◽  
Virulent Strain ◽  
Iron Acquisition ◽  
Proteome Analysis ◽  
Peptide Mass Fingerprinting ◽  
Computer Assisted ◽  
Two Dimensional Gel Electrophoresis ◽  
Peptide Mass ◽  
Amino Acid Binding

ABSTRACT The genus Brucella consists of bacterial pathogens that cause brucellosis, a major zoonotic disease characterized by undulant fever and neurological disorders in humans. Among the different Brucella species, Brucella melitensis is considered the most virulent. Despite successful use in animals, the vaccine strains remain infectious for humans. To understand the mechanism of virulence in B. melitensis, the proteome of vaccine strain Rev 1 was analyzed by two-dimensional gel electrophoresis and compared to that of virulent strain 16M. The two strains were grown under identical laboratory conditions. Computer-assisted analysis of the two B. melitensis proteomes revealed proteins expressed in either 16M or Rev 1, as well as up- or down-regulation of proteins specific for each of these strains. These proteins were identified by peptide mass fingerprinting. It was found that certain metabolic pathways may be deregulated in Rev 1. Expression of an immunogenic 31-kDa outer membrane protein, proteins utilized for iron acquisition, and those that play a role in sugar binding, lipid degradation, and amino acid binding was altered in Rev 1.

Proteomic Analysis of Medicinal Plant Calotropis Gigantea by insilico Peptide Mass Fingerprinting

2020 ◽  
Vol 16 ◽  
Author(s):  
Saad Ur Rehman ◽  
Muhammad Rizwan ◽  
Sajid Khan ◽  
Azhar Mehmood ◽  
Anum Munir
Keyword(s):  
Medicinal Plant ◽  
Structure Prediction ◽  
3D Structure ◽  
Peptide Mass Fingerprinting ◽  
Protein Docking ◽  
Receptor Protein ◽  
Human Leukemia ◽  
Protein Database ◽  
Calotropis Gigantea ◽  
Peptide Mass

: Medicinal plants are the basic source of medicinal compounds traditionally used for the treatment of human diseases. Calotropis gigantea a medicinal plant belonging to the family of Apocynaceae in the plant kingdom and subfamily Asclepiadaceae usually bearing multiple medicinal properties to cure a variety of diseases. Background: The Peptide Mass Fingerprinting (PMF) identifies the proteins from a reference protein database by comparing the amino acid sequence that is previously stored in a database and identified. Method: The calculation of insilico peptide masses is done through the ExPASy PeptideMass and these masses are used to identify the peptides from MASCOT online server. Anticancer probability is calculated from the iACP server, docking of active peptides is done by CABS-dock the server. Objective: The purpose of the study is to identify the peptides having anti-cancerous properties by in-silico peptide mass fingerprinting. Results : The anti-cancerous peptides are identified with the MASCOT peptide mass fingerprinting server, the identified peptides are screened and only the anti-cancer are selected. De novo peptide structure prediction is used for 3D structure prediction by PEP-FOLD 3 server. The docking results confirm strong bonding with the interacting amino acids of the receptor protein of breast cancer BRCA1 which shows the best peptide binding to the Active chain, the human leukemia protein docking with peptides shows the accurate binding. Conclusion : These peptides are stable and functional and are the best way for the treatment of cancer and many other deadly diseases.

scholarly journals The Fish Pathogen Vibrio ordalii Under Iron Deprivation Produces the Siderophore Piscibactin

2019 ◽  
Vol 7 (9) ◽  
pp. 313 ◽  
Author(s):  
Pamela Ruiz ◽  
Miguel Balado ◽  
Juan Carlos Fuentes-Monteverde ◽  
Alicia E. Toranzo ◽  
Jaime Rodríguez ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Iron Uptake ◽  
Peptide Mass Fingerprinting ◽  
Iron Limitation ◽  
Fish Pathogen ◽  
Fish Pathogens ◽  
Iron Deprivation ◽  
Peptide Mass ◽  
Photobacterium Damselae ◽  
Vibrio Ordalii

Vibrio ordalii is the causative agent of vibriosis, mainly in salmonid fishes, and its virulence mechanisms are still not completely understood. In previous works we demonstrated that V. ordalii possess several iron uptake mechanisms based on heme utilization and siderophore production. The aim of the present work was to confirm the production and utilization of piscibactin as a siderophore by V. ordalii. Using genetic analysis, identification by peptide mass fingerprinting (PMF) of iron-regulated membrane proteins and chemical identification by LC-HRMS, we were able to clearly demonstrate that V. ordalii produces piscibactin under iron limitation. The synthesis and transport of this siderophore is encoded by a chromosomal gene cluster homologous to another one described in V. anguillarum, which also encodes the synthesis of piscibactin. Using β-galactosidase assays we were able to show that two potential promoters regulated by iron control the transcription of this gene cluster in V. ordalii. Moreover, biosynthetic and transport proteins corresponding to piscibactin synthesis and uptake could be identified in membrane fractions of V. ordalii cells grown under iron limitation. The synthesis of piscibactin was previously reported in other fish pathogens like Photobacterium damselae subsp. piscicida and V. anguillarum, which highlights the importance of this siderophore as a key virulence factor in Vibrionaceae bacteria infecting poikilothermic animals.

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