scholarly journals Isolation and Characterization of Major Outer Membrane Proteins of Edwardsiella tarda.

1998 ◽  
Vol 33 (5) ◽  
pp. 481-487 ◽  
Author(s):  
Xiaolin Tu ◽  
Kenji Kawai
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Edwardsiella Tarda ◽  
Isolation And Characterization

Isolation and characterization of outer membrane proteins of Edwardsiella tarda and its application in immunoassays

Aquaculture ◽  
2007 ◽  
Vol 272 (1-4) ◽  
pp. 98-104 ◽  
Author(s):  
Gokhlesh Kumar ◽  
Gaurav Rathore ◽  
U. Sengupta ◽  
V. Singh ◽  
D. Kapoor ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Edwardsiella Tarda ◽  
Isolation And Characterization

scholarly journals Isolation and characterization of outer membrane proteins (OMPs) from Salmonella Gallinarum in chicken and antibiogram of the isolates

2016 ◽  
Vol 8 (4) ◽  
pp. 2292-2297
Author(s):  
Asma Ul Husna ◽  
Shabir Ahmad Mir ◽  
Rusheeba Manzoor ◽  
Farhat Pandit ◽  
Shakil Ahmad Wani ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Antimicrobial Agents ◽  
Outer Membrane Proteins ◽  
Specific Detection ◽  
Salmonella Gallinarum ◽  
Isolation And Characterization ◽  
Faecal Samples

Salmonella isolates should be distinguished as it may assist in tracing the source of an outbreak and monitoring trends in antimicrobial resistance associated with a particular type. The specific detection of these Salmonella serotypes is therefore extremely important in order to attribute an isolate to a previously known epidemic outbreak. The present investigation was to isolate and identify S. Gallinarum, to study variation in the profile of outer membrane proteins (OMPs) and to determine in vitro antibiogram of S. Gallinarum in poultry. A total of 228 faecal samples and 22 visceral samples suspected for Salmonellosis were collected, of these 15 samples (6.0%) were found positive for S. Gallinarum. In the present study, rfbS gene sequence was helpful in the serotype-specific detection of S. Gallinarum giving a 187 bp product. Salmonella Gallinarum crude protein extracts determined by SDSPAGE showed migration of OMPs as several bands at approximate moleculer weights of appx. 45 kDa, 55 kDa, 64 kDa, 65 kDa, 74 kDa, 110 kDa, 120 kDa, 135 kDa, 150 kDa,155 kDa, 200 kDa and above 200 kDa. The study indicated a definite variation in the profile of OMPs of various Salmonella Gallinarum strains with major OMPs in the range of appx 80-100 kDa which could be the target for vaccine production. All the isolates tested against 14 antimicrobial agents showed variable susceptibility pattern with highest resistance to nalidixic acid, ampicillin and sulphadiazine and sensitivity to chloramphenicol, gentamicin and enrofloxacin.

Bacteriocin 28b fromSerratia marcescensN28b: identification ofEscherichia colisurface components involved in bacteriocin binding and translocation

1996 ◽  
Vol 42 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Josefina Enfedaque ◽  
Santiago Ferrer ◽  
Joan Francesc Guasch ◽  
Miguel Regué ◽  
Joan Tomás
Keyword(s):  
Membrane Proteins ◽  
Serratia Marcescens ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Binding Ability ◽  
E Coli ◽  
The Core ◽  
Isolation And Characterization ◽  
Sensitivity Tests

Serratia marcescens N28b produces bacteriocin 28b, active against Escherichia coli. Bacteriocin sensitivity tests performed on a collection of E. coli envelope mutants, and isolation and characterization of E. coli bacteriocin-28b-insensitive mutants, showed that the core lipopolysaccharide, outer membrane proteins OmpA and OmpF, and TolQ, TolA, and TolB proteins are involved in bacteriocin 28b lethal activity. These mutants were assayed for bacteriocin 28b sensitivity under normal and bypass conditions, and their bacteriocin-binding ability was determined. The results obtained suggest that the core lipopolysaccaride and outer membrane proteins OmpA and OmpF are involved in bacteriocin 28b binding. Furthermore, bacteriocin 28b translocation requires proteins TolA, TolB, and TolQ.Key words: bacteriocin, receptors, translocation, Serratia marcescens.

scholarly journals Isolation and Characterization of Vibrio tubiashii Outer Membrane Proteins and Determination of a toxR Homolog

2007 ◽  
Vol 74 (3) ◽  
pp. 907-911 ◽  
Author(s):  
J. Jean-Gilles Beaubrun ◽  
M. H. Kothary ◽  
S. K. Curtis ◽  
N. C. Flores ◽  
B. E. Eribo ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Growth Conditions ◽  
Isolation And Characterization ◽  
Vibrio Tubiashii

ABSTRACT Outer membrane proteins (OMPs) expressed by Vibrio tubiashii under different environmental growth conditions were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, N-terminal amino acid sequencing, and PCR analyses. Results showed the presence of a 38- to 40-kDa OmpU-like protein and ompU gene, a maltoporin-like protein, several novel OMPs, and a regulatory toxR homolog.

scholarly journals Isolation and Characterization of the Outer Membrane ofBorrelia hermsii

1998 ◽  
Vol 66 (3) ◽  
pp. 1082-1091 ◽  
Author(s):  
Ellen S. Shang ◽  
Jonathan T. Skare ◽  
Maurice M. Exner ◽  
David R. Blanco ◽  
Bruce L. Kagan ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Gradient Centrifugation ◽  
Outer Membrane Proteins ◽  
Freeze Fracture ◽  
Outer Membrane Vesicles ◽  
Proteinase K ◽  
Blue Staining ◽  
Isolation And Characterization

ABSTRACT The outer membrane of Borrelia hermsii has been shown by freeze-fracture analysis to contain a low density of membrane-spanning outer membrane proteins which have not yet been isolated or identified. In this study, we report the purification of outer membrane vesicles (OMV) from B. hermsii HS-1 and the subsequent identification of their constituent outer membrane proteins. The B. hermsii outer membranes were released by vigorous vortexing of whole organisms in low-pH, hypotonic citrate buffer and isolated by isopycnic sucrose gradient centrifugation. The isolated OMV exhibited porin activities ranging from 0.2 to 7.2 nS, consistent with their outer membrane origin. Purified OMV were shown to be relatively free of inner membrane contamination by the absence of measurable β-NADH oxidase activity and the absence of protoplasmic cylinder-associated proteins observed by Coomassie blue staining. Approximately 60 protein spots (some of which are putative isoelectric isomers) with 25 distinct molecular weights were identified as constituents of the OMV enrichment. The majority of these proteins were also shown to be antigenic with sera from B. hermsii-infected mice. Seven of these antigenic proteins were labeled with [3H]palmitate, including the surface-exposed glycerophosphodiester phosphodiesterase, the variable major proteins 7 and 33, and proteins of 15, 17, 38, 42, and 67 kDa, indicating that they are lipoprotein constituents of the outer membrane. In addition, immunoblot analysis of the OMV probed with antiserum to the Borrelia garinii surface-exposed p66/Oms66 porin protein demonstrated the presence of a p66 (Oms66) outer membrane homolog. Treatment of intact B. hermsii with proteinase K resulted in the partial proteolysis of the Oms66/p66 homolog, indicating that it is surface exposed. This identification and characterization of the OMV proteins should aid in further studies of pathogenesis and immunity of tick-borne relapsing fever.

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