Molecular Cloning of the Pasteurella haemolytica pomA Gene and Identification of Bovine Antibodies against PomA Surface Domains

ABSTRACT The gene (pomA) encoding PomA, an OmpA-like major outer membrane protein of the bovine respiratory pathogen Pasteurella haemolytica, was cloned, and its nucleotide sequence was determined. The deduced amino acid sequence of PomA has significant identity with the sequences of other OmpA family proteins. Absorption of three different bovine immune sera with whole P. haemolytica cells resulted in a reduction of bovine immunoglobulin G reactivity with recombinant PomA in Western immunoblots, suggesting the presence of antibodies against PomA surface domains.

Download Full-text

The nucleotide and deduced amino acid sequence of the cationic 19 kDa outer membrane protein OmpH of Yersinia pseudotuberculosis

Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression ◽

10.1016/0167-4781(91)90226-c ◽

1991 ◽

Vol 1129 (1) ◽

pp. 124-126 ◽

Cited By ~ 5

Author(s):

Riita Vuorio ◽

Laura Hirvas ◽

Richard B. Raybourne ◽

David T.Y. Yu ◽

M. Vaara

Keyword(s):

Amino Acid ◽

Membrane Protein ◽

Amino Acid Sequence ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Yersinia Pseudotuberculosis

Download Full-text

Cloning of the Gene Encoding the Actinobacillus actinomycetemcomitans Serotype b OmpA-Like Outer Membrane Protein

Infection and Immunity ◽

10.1128/iai.67.2.942-945.1999 ◽

1999 ◽

Vol 67 (2) ◽

pp. 942-945 ◽

Cited By ~ 23

Author(s):

Hitoshi Komatsuzawa ◽

Toshihisa Kawai ◽

Mark E. Wilson ◽

Martin A. Taubman ◽

Motoyuki Sugai ◽

...

Keyword(s):

Monoclonal Antibody ◽

Amino Acid ◽

Membrane Protein ◽

Amino Acid Sequence ◽

Molecular Mass ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Actinobacillus Actinomycetemcomitans ◽

Gene Encoding ◽

Serotype B

ABSTRACT The gene encoding an outer membrane protein A (OmpA)-like, heat-modifiable Omp of Actinobacillus actinomycetemcomitans ATCC 43718 (strain Y4, serotype b) was cloned by a PCR cloning procedure. DNA sequence analysis revealed that the gene encodes a protein of 346 amino acid residues with a molecular mass of 36.9 kDa. The protein expressed by the cloned gene reacted with a monoclonal antibody to the previously described 29-kDa Omp (Omp29) of strain Y4. This monoclonal antibody reacted specifically with Omp29 of A. actinomycetemcomitans (serotype b), but not with any Omp of Escherichia coli, including OmpA. This protein exhibited characteristic heat modifiability on sodium dodecyl sulfate-polyacrylamide gels, showing an apparent molecular mass of 29 kDa when unheated and a mass of 34 kDa when heated. The N-terminal amino acid sequence of the protein expressed inE. coli perfectly matched those deduced from the purified Omp29 of strain Y4. The deduced amino acid sequence of the gene coding for Omp29 from serotype b matched completely (except for valine at position 321) that of a recently reported omp34gene described for A. actinomycetemcomitans serotype c (NCTC 9710). Because of the conserved nature of the gene within these serotypes, we designated the gene described herein from serotype b asomp34.

Download Full-text

Molecular Cloning, Sequencing, and Expression ofomp-40, the Gene Coding for the Major Outer Membrane Protein from the Acidophilic Bacterium Thiobacillus ferrooxidans

Applied and Environmental Microbiology ◽

10.1128/aem.66.6.2318-2324.2000 ◽

2000 ◽

Vol 66 (6) ◽

pp. 2318-2324 ◽

Cited By ~ 37

Author(s):

Nicolas Guiliani ◽

Carlos A. Jerez

Keyword(s):

Amino Acid ◽

Membrane Protein ◽

Amino Acid Sequence ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Thiobacillus Ferrooxidans ◽

Sodium Dodecyl ◽

Major Outer Membrane Protein ◽

Gene Coding ◽

Chemolithoautotrophic Bacteria

ABSTRACT Thiobacillus ferrooxidans is one of the chemolithoautotrophic bacteria important in industrial biomining operations. Some of the surface components of this microorganism are probably involved in adaptation to their acidic environment and in bacterium-mineral interactions. We have isolated and characterizedomp40, the gene coding for the major outer membrane protein from T. ferrooxidans. The deduced amino acid sequence of the Omp40 protein has 382 amino acids and a calculated molecular weight of 40,095.7. Omp40 forms an oligomeric structure of about 120 kDa that dissociates into the monomer (40 kDa) by heating in the presence of sodium dodecyl sulfate. The degree of identity of Omp40 amino acid sequence to porins from enterobacteria was only 22%. Nevertheless, multiple alignments of this sequence with those from several OmpC porins showed several important features conserved in the T. ferrooxidans surface protein, such as the approximate locations of 16 transmembrane beta strands, eight loops, including a large external L3 loop, and eight turns which allowed us to propose a putative 16-stranded beta-barrel porin structure for the protein. These results together with the previously known capacity of Omp40 to form ion channels in planar lipid bilayers strongly support its role as a porin in this chemolithoautotrophic acidophilic microorganism. Some characteristics of the Omp40 protein, such as the presence of a putative L3 loop with an estimated isoelectric point of 7.21 allow us to speculate that this can be the result of an adaptation of the acidophilic T. ferrooxidans to prevent free movement of protons across its outer membrane.

Download Full-text

Amino acid sequence of the signal peptide of OmpF, a major outer membrane protein ofEscherichia coli

FEBS Letters ◽

10.1016/0014-5793(82)80341-4 ◽

1982 ◽

Vol 137 (2) ◽

pp. 171-174 ◽

Cited By ~ 24

Author(s):

Norihiro Mutoh ◽

Kaoru Inokuchi ◽

Shoji Mizushima

Keyword(s):

Amino Acid ◽

Membrane Protein ◽

Amino Acid Sequence ◽

Outer Membrane ◽

Signal Peptide ◽

Outer Membrane Protein ◽

Major Outer Membrane Protein ◽

Ofescherichia Coli

Download Full-text

Partial amino acid sequence and molecular cloning of the encoding gene for the major outer membrane protein of Chlamydia trachomatis.

Infection and Immunity ◽

10.1128/iai.48.2.372-377.1985 ◽

1985 ◽

Vol 48 (2) ◽

pp. 372-377 ◽

Cited By ~ 5

Author(s):

F E Nano ◽

P A Barstad ◽

L W Mayer ◽

J E Coligan ◽

H D Caldwell

Keyword(s):

Amino Acid ◽

Chlamydia Trachomatis ◽

Membrane Protein ◽

Amino Acid Sequence ◽

Outer Membrane ◽

Molecular Cloning ◽

Outer Membrane Protein ◽

Major Outer Membrane Protein ◽

Partial Amino Acid Sequence ◽

Encoding Gene

Download Full-text

Comparative studies of two types of bovine immunoglobulin G heavy chains

Biochemical Journal ◽

10.1042/bj1070559 ◽

1968 ◽

Vol 107 (4) ◽

pp. 559-564 ◽

Cited By ~ 45

Author(s):

C. P. Milstein ◽

A. Feinstein

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Amino Acid Composition ◽

Acid Composition ◽

Immunoglobulin G ◽

Comparative Studies ◽

Cyanogen Bromide ◽

Serum Immunoglobulin ◽

Heavy Chains ◽

Bovine Immunoglobulin

‘Fingerprints’ of bovine colostrum and serum immunoglobulin G1 heavy chains were extremely similar, but different from serum immunoglobin G2 heavy chains. Serum immunoglobulin G1 and immunoglobulin G2 heavy chains were treated with cyanogen bromide. The fractions from the C-terminal end of the heavy chains were isolated and the amino acid sequence of this fraction from immunoglobulin G2 was:His-Glx-Ala-Leu-His-Asx-His-Tyr-Met-Gln-Lys-Ser-Thr-Ser-Lys-Ser-Ala-GlyThe amino acid composition of this fraction from immunoglobulin G1 was the same except for the methionine, which in immunoglobulin G1 was replaced by threonine.

Download Full-text