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

1991 ◽  
Vol 1129 (1) ◽  
pp. 124-126 ◽  
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

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

1999 ◽  
Vol 67 (2) ◽  
pp. 942-945 ◽  
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.

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

2000 ◽  
Vol 66 (6) ◽  
pp. 2318-2324 ◽  
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.

scholarly journals Sequence Polymorphism, Predicted Secondary Structures, and Surface-Exposed Conformational Epitopes of Campylobacter Major Outer Membrane Protein

2000 ◽  
Vol 68 (10) ◽  
pp. 5679-5689 ◽  
Author(s):  
Qijing Zhang ◽  
Jerrel C. Meitzler ◽  
Shouxiong Huang ◽  
Teresa Morishita
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Outer Membrane Proteins ◽  
Major Outer Membrane Protein ◽  
Amino Acid Sequences ◽  
Variable Regions ◽  
Conserved Sequences ◽  
Conformational Epitopes

ABSTRACT The major outer membrane protein (MOMP), a putative porin and a multifunction surface protein of Campylobacter jejuni, may play an important role in the adaptation of the organism to various host environments. To begin to dissect the biological functions and antigenic features of this protein, the gene (designatedcmp) encoding MOMP was identified and characterized from 22 strains of C. jejuni and one strain of C. coli. It was shown that the single-copy cmp locus encoded a protein with characteristics of bacterial outer membrane proteins. Prediction from deduced amino acid sequences suggested that each MOMP subunit consisted of 18 β-strands connected by short periplasmic turns and long irregular external loops. Alignment of the amino acid sequences of MOMP from different strains indicated that there were seven localized variable regions dispersed among highly conserved sequences. The variable regions were located in the putative external loop structures, while the predicted β-strands were formed by conserved sequences. The sequence homology of cmp appeared to reflect the phylogenetic proximity of C. jejuni strains, since strains with identical cmp sequences had indistinguishable or closely related macrorestriction fragment patterns. Using recombinant MOMP and antibodies recognizing linear or conformational epitopes of the protein, it was demonstrated that the surface-exposed epitopes of MOMP were predominantly conformational in nature. These findings are instrumental in the design of MOMP-based diagnostic tools and vaccines.

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

1999 ◽  
Vol 67 (9) ◽  
pp. 4968-4973 ◽  
Author(s):  
Hui Zeng ◽  
Karamjeet Pandher ◽  
George L. Murphy
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Membrane Protein ◽  
Amino Acid Sequence ◽  
Outer Membrane Protein ◽  
Immunoglobulin G ◽  
Pasteurella Haemolytica ◽  
Respiratory Pathogen ◽  
Surface Domains ◽  
Bovine Immunoglobulin

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.

scholarly journals High-resolution mapping of serovar-specific and common antigenic determinants of the major outer membrane protein of Chlamydia trachomatis.

1988 ◽  
Vol 167 (3) ◽  
pp. 817-831 ◽  
Author(s):  
R S Stephens ◽  
E A Wagar ◽  
G K Schoolnik
Keyword(s):  
Amino Acid ◽  
Chlamydia Trachomatis ◽  
Membrane Protein ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Antigenic Determinants ◽  
Amino Acid Peptide ◽  
Antigenic Domains ◽  
Species Specific ◽  
Specific Determinant

The principal surface protein antigen of Chlamydia trachomatis is the major outer membrane protein (MOMP). The MOMP is antigenically complex. Among the 15 serovars of C. trachomatis, mAbs define serovar-, subspecies-, and species-specific determinants on MOMP. The molecular basis of the antigenic diversity of these proteins is reflected in amino acid variable sequence domains. We have mapped the dominant topographic antigenic determinants of MOMP that are defined by mAbs. Using recombinant DNA approaches we have identified the linear distribution of two antigenic domains. One domain contains a serovar-specific determinant and the other contains subspecies- and species-specific determinants. These antigenic domains correspond to two amino acid sequence variable domains. Synthetic peptides were immunogenic and these resolved the serovar-specific determinant within a 14-amino acid peptide. The subspecies- and species-specific determinants were overlapping within a 16-amino acid peptide.

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