scholarly journals Cloning and characterization of the gene encoding the OmpU outer membrane protein of Vibrio cholerae.

1996 ◽  
Vol 64 (12) ◽  
pp. 5406-5409 ◽  
Author(s):  
V Sperandio ◽  
C Bailey ◽  
J A Girón ◽  
V J DiRita ◽  
W D Silveira ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Vibrio Cholerae ◽  
Outer Membrane Protein ◽  
Gene Encoding

scholarly journals Molecular cloning, sequencing and characterization of omp48, the gene encoding for an antigenic outer membrane protein from Aeromonas veronii

2003 ◽  
Vol 94 (5) ◽  
pp. 908-918 ◽  
Author(s):  
R.C. Vazquez-Juarez ◽  
H.A. Barrera-Saldana ◽  
N.Y. Hernandez-Saavedra ◽  
M. Gomez-Chiarri ◽  
F. Ascencio
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Molecular Cloning ◽  
Outer Membrane Protein ◽  
Gene Encoding ◽  
Aeromonas Veronii

scholarly journals Characterization of Outer Membrane Protein OmpU of Vibrio cholerae O1

1998 ◽  
Vol 66 (10) ◽  
pp. 4726-4728 ◽  
Author(s):  
Noboru Nakasone ◽  
Masaaki Iwanaga
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Vibrio Cholerae ◽  
Outer Membrane Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Rabbit Small Intestine ◽  
Vibrio Cholerae O1

ABSTRACT The outer membrane protein OmpU of Vibrio cholerae O1 strain 86B3 was characterized with reference to colonization of the intestine by the organism. The purified OmpU exhibited a pI of 3.6. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, it migrated to 38, 32, and 110 kDa when the sample was heated at 100°C for 2 min, 50°C for 15 min, and room temperature for 30 min, respectively. The purified OmpU was not hemagglutinative. Anti-OmpU serum did not agglutinate strain 86B3 or other V. cholerae organisms. OmpU adhered to the brush border of the rabbit small intestine; adhesion of the organisms to the intestine treated in advance with OmpU was not inhibited. Treating the organisms in advance with anti-OmpU Fab did not inhibit adhesion to the intestine. These results obtained in vitro suggest that OmpU is not involved in the adhesion of V. cholerae to the intestinal epithelium.

scholarly journals Molecular Characterization of an Outer Membrane Protein ofActinobacillus actinomycetemcomitans Belonging to the OmpA Family

1998 ◽  
Vol 66 (1) ◽  
pp. 369-372 ◽  
Author(s):  
Peter A. White ◽  
Sean P. Nair ◽  
Mi-Jurng Kim ◽  
Michael Wilson ◽  
Brian Henderson
Keyword(s):  
Membrane Protein ◽  
Molecular Mass ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Genomic Library ◽  
Mature Protein ◽  
Gene Encoding ◽  
Localized Juvenile Periodontitis ◽  
Cloned Gene

ABSTRACT The major outer membrane protein (OMP) of Actinobacillus actinomycetemcomitans is an OmpA homolog that demonstrates electrophoretic heat modifiability. The gene encoding this protein was isolated from a genomic library of A. actinomycetemcomitansNCTC 9710 by immunoscreening with serum from a patient with localized juvenile periodontitis. Expression of the cloned gene inEscherichia coli and subsequent Western blot analysis revealed a protein with an approximate molecular mass of 34 kDa. The amino acid sequence predicted from the cloned gene demonstrated that the mature protein had a molecular mass of 34,911 Da and significant identity to members of the OmpA family of proteins. We have named the major OMP of A. actinomycetemcomitans Omp34, and its corresponding gene has been named omp34.

Cloning and Characterization of the Gene Encoding for OMP-PD Porin: The Major Photobacterium damsela Outer Membrane Protein

2004 ◽  
Vol 48 (3) ◽  
pp. 167-174 ◽  
Author(s):  
Anna Gribun ◽  
Don J. Katcoff ◽  
Gitit Hershkovits ◽  
Izabella Pechatnikov ◽  
Yeshayahu Nitzan
Keyword(s):  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Gene Encoding
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