scholarly journals Outer Membrane Proteome Analysis of Indian Strain ofPasteurella multocidaSerotype B:2 by MALDI-TOF/MS Analysis

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
A. Prasannavadhana ◽  
Santosh Kumar ◽  
Prasad Thomas ◽  
Laxmi Narayan Sarangi ◽  
Santosh Kumar Gupta ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Maldi Tof Ms ◽  
Limited Condition ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Serotype B ◽  
Tof Ms

Identification of outer membrane proteins (OMPs) is important to understand the bacteria structure and function, host-pathogen interaction, development of novel vaccine candidates, and diagnostic antigens. But till now the key antigens ofP. multocidaB:2 isolate causing haemorrhagic septicaemia (HS) in animals are not clearly defined. In this study, P52 strain ofP. multocidaserotype B:2 was grownin vitrounder iron-rich and iron-limited condition. The OMPs were extracted by sarkosyl method followed by SDS-PAGE and the proteins were identified by MALDI-TOF/MS analysis. In total, 22 proteins were identified, of which 7 were observed exclusively under iron-limited condition. Most of the high molecular weight proteins (TbpA, HgbA, HgbB, HasR, IroA, and HemR) identified in this study were involved in iron acquisition. Some hypothetical proteins (HP-KCU-10206, HP and AAUPMB 08244, HP AAUPMB 21592, HP AAUPMB 19766, AAUPMB 11295) were observed for the first time in this study which could be unique to serotype B:2. Further functionalin vivostudy of the proteins identified are required to explore the utility of these proteins in developing diagnostics and vaccine against HS.

Detection of the antibacterial effect of essential oils on outer membrane proteins ofPseudomonas aeruginosaby lab-on-a-chip and MALDI-TOF/MS

2013 ◽  
Vol 28 (6) ◽  
pp. 367-372 ◽  
Author(s):  
Péter Felső ◽  
Györgyi Horváth ◽  
Tímea Bencsik ◽  
Roland Godányi ◽  
Éva Lemberkovics ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Essential Oils ◽  
Outer Membrane ◽  
Antibacterial Effect ◽  
Outer Membrane Proteins ◽  
Lab On A Chip ◽  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Tof Ms

scholarly journals Thermus thermophilus L11 Methyltransferase, PrmA, Is Dispensable for Growth and Preferentially Modifies Free Ribosomal Protein L11 Prior to Ribosome Assembly

2004 ◽  
Vol 186 (17) ◽  
pp. 5819-5825 ◽  
Author(s):  
Dale M. Cameron ◽  
Steven T. Gregory ◽  
Jill Thompson ◽  
Moo-Jin Suh ◽  
Patrick A. Limbach ◽  
...  
Keyword(s):  
Ribosomal Protein ◽  
Thermus Thermophilus ◽  
Methyl Groups ◽  
Maldi Tof Ms ◽  
E Coli ◽  
Maldi Tof ◽  
Ribosomal Protein L11 ◽  
Tof Ms

ABSTRACT The ribosomal protein L11 in bacteria is posttranslationally trimethylated at multiple amino acid positions by the L11 methyltransferase PrmA, the product of the prmA gene. The role of L11 methylation in ribosome function or assembly has yet to be determined, although the deletion of Escherichia coli prmA has no apparent phenotype. We have constructed a mutant of the extreme thermophile Thermus thermophilus in which the prmA gene has been disrupted with the htk gene encoding a heat-stable kanamycin adenyltransferase. This mutant shows no growth defects, indicating that T. thermophilus PrmA, like its E. coli homolog, is dispensable. Ribosomes prepared from this mutant contain unmethylated L11, as determined by matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), and are effective substrates for in vitro methylation by cloned and purified T. thermophilus PrmA. MALDI-TOF MS also revealed that T. thermophilus L11 contains a total of 12 methyl groups, in contrast to the 9 methyl groups found in E. coli L11. Finally, we found that, as with the E. coli methyltransferase, the ribosomal protein L11 dissociated from ribosomes is a more efficient substrate for in vitro methylation by PrmA than intact 70S ribosomes, suggesting that methylation in vivo occurs on free L11 prior to its incorporation into ribosomes.

The suitability of different DHB isomers as matrices for the MALDI-TOF MS analysis of phospholipids: which isomer for what purpose?

2006 ◽  
Vol 36 (4-5) ◽  
pp. 517-527 ◽  
Author(s):  
Jürgen Schiller ◽  
Rosmarie Süß ◽  
Beate Fuchs ◽  
Matthias Müller ◽  
Marijana Petković ◽  
...  
Keyword(s):  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Tof Ms

NMR, HPLC-ESI-MS, and MALDI-TOF MS Analysis of Condensed Tannins from Delonix regia (Bojer ex Hook.) Raf. and Their Bioactivities

2012 ◽  
Vol 60 (19) ◽  
pp. 5013-5022 ◽  
Author(s):  
Wei-Ming Chai ◽  
Yan Shi ◽  
Hui-Ling Feng ◽  
Ling Qiu ◽  
Hai-Chao Zhou ◽  
...  
Keyword(s):  
Condensed Tannins ◽  
Maldi Tof Ms ◽  
Esi Ms ◽  
Delonix Regia ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Tof Ms

Identification of Lice Stored in Alcohol Using MALDI-TOF MS

2020 ◽  
Author(s):  
Hanene Benyahia ◽  
Basma Ouarti ◽  
Adama Zan Diarra ◽  
Mehdi Boucheikhchoukh ◽  
Mohamed Nadir Meguini ◽  
...  
Keyword(s):  
Economic Consequences ◽  
Correct Identification ◽  
Protein Profiles ◽  
Innovative Strategy ◽  
Maldi Tof Ms ◽  
Pediculus Humanus ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Storage Methods ◽  
Tof Ms

Abstract Lice pose major public and veterinary health problems with economic consequences. Their identification is essential and requires the development of an innovative strategy. MALDI-TOF MS has recently been proposed as a quick, inexpensive, and accurate tool for the identification of arthropods. Alcohol is one of the most frequently used storage methods and makes it possible to store samples for long periods at room temperature. Several recent studies have reported that alcohol alters protein profiles resulting from MS analysis. After preliminary studies on frozen lice, the purpose of this research was to evaluate the influence of alcohol preservation on the accuracy of lice identification by MALDI-TOF MS. To this end, lice stored in alcohol for variable periods were submitted for MS analysis and sample preparation protocols were optimized. The reproducibility and specificity of the MS spectra obtained on both these arthropod families allowed us to implement the reference MS spectra database (DB) with protein profiles of seven lice species stored in alcohol. Blind tests revealed a correct identification of 93.9% of Pediculus humanus corporis (Linnaeus, 1758) and 98.4% of the other lice species collected in the field. This study demonstrated that MALDI-TOF MS could be successfully used for the identification of lice stored in alcohol for different lengths of time.

Identification of Arcanobacterium hippocoleae by MALDI-TOF MS analysis and by various genotypical properties

2017 ◽  
Vol 115 ◽  
pp. 10-12 ◽  
Author(s):  
J.-P. Wickhorst ◽  
O. Sammra ◽  
A.A. Hassan ◽  
M. Alssashen ◽  
C. Lämmler ◽  
...  
Keyword(s):  
Maldi Tof Ms ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Tof Ms

Development of magnetic LuPO4 microspheres for highly selective enrichment and identification of phosphopeptides for MALDI-TOF MS analysis

2015 ◽  
Vol 3 (48) ◽  
pp. 9330-9339 ◽  
Author(s):  
Xing-yu Long ◽  
Qun Song ◽  
Hong-zhen Lian
Keyword(s):  
Core Shell ◽  
Maldi Tof Ms ◽  
Selective Enrichment ◽  
Maldi Tof ◽  
Ms Analysis ◽  
Tof Ms

Lichee-like core–shell structured magnetic lutetium phosphate (Fe3O4@LuPO4) affinity microspheres were synthesized, characterized and successfully applied to enrich phosphopeptides.

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