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The Major Aeromonas veronii Outer Membrane Protein: Gene Cloning and Sequence Analysis

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Abstract

The gene encoding the major outer membrane protein (OMP) from Aeromonas veronii, Omp38, was cloned and characterized. Sequence analysis revealed an open reading frame of 1,047 nucleotides coding for a primary protein of 349 amino acids with a 20–amino-acid signal peptide at the N-terminal and the consensus sequence Ala-X-Ala (Ala-Asn-Ala) as the signal peptidase I recognition site. The mature protein is composed of 329 amino acids with a calculated molecular mass of 36,327 Da. The degree of identity of the deduced Omp38 amino acid sequence to porins from enteric bacteria (OmpF, PhoE, and OmpC) was only 30%. Nevertheless, Omp38 possesses typical features of Gram-negative porins, including acidic pI, high glycine and low proline content, no cysteine residues, and a carboxy-terminal Phe. On the basis of PhoE-OmpF three-dimensional structure and the Kyte-Doolittle hydrophobicity analysis, it seems likely that Omp38 secondary structure consists of 16 antiparallel β-strands and 8 loops. Phylogenetic analyses among Omp38 and related porins from Gram-negative bacteria originate well-defined clusters that agree with the taxonomy of the corresponding organisms.

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Acknowledgments

This work was supported by Centro de Investigaciones Biológicas del Noroeste (CIBNOR) and Consejo Nacional de Ciencia y Techología (CONACyT) research grants. R.C.V.J. is grateful to the University of Rhade Island (URI) Foundation for additional funds for travel. We also thank to Dr. Possani and Dr. Egly for peptide sequencing.

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Correspondence to Roberto Carlos Vázquez-Juárez.

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Vázquez-Juárez, R.C., Gómez-Chiarri, M., Barrera-Saldaña, H. et al. The Major Aeromonas veronii Outer Membrane Protein: Gene Cloning and Sequence Analysis. Curr Microbiol 51, 372–378 (2005). https://doi.org/10.1007/s00284-005-0054-6

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  • DOI: https://doi.org/10.1007/s00284-005-0054-6

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