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MOLECULAR AND CELLULAR PATHOGENESIS

A Major Secreted Elastase Is Essential for Pathogenicity of Aeromonas hydrophila

Alberto Cascón, Javier Yugueros, Alejandro Temprano, María Sánchez, Carmen Hernanz, José María Luengo, Germán Naharro
Alberto Cascón
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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Javier Yugueros
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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Alejandro Temprano
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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María Sánchez
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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Carmen Hernanz
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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José María Luengo
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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Germán Naharro
Departamento de Sanidad Animal, Microbiologı́a e Inmunologı́a, Facultad de Veterinaria, Universidad de León, 24071 León, Spain
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DOI: 10.1128/IAI.68.6.3233-3241.2000
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ABSTRACT

Aeromonas hydrophila is an opportunistic pathogen and the leading cause of fatal hemorrhagic septicemia in rainbow trout. A gene encoding an elastolytic activity, ahyB, was cloned from Aeromonas hydrophila AG2 into pUC18 and expressed inEscherichia coli and in the nonproteolytic speciesAeromonas salmonicida subsp. masoucida. Nucleotide sequence analysis of the ahyB gene revealed an open reading frame of 1,764 nucleotides with coding capacity for a 588-amino-acid protein with a molecular weight of 62,728. The first 13 N-terminal amino acids of the purified protease completely match those deduced from DNA sequence starting at AAG (Lys-184). This finding indicated that AhyB is synthesized as a preproprotein with a 19-amino-acid signal peptide, a 164-amino-acid N-terminal propeptide, and a 405-amino-acid intermediate which is further processed into a mature protease and a C-terminal propeptide. The protease hydrolyzed casein and elastin and showed a high sequence similarity to other metalloproteases, especially with the mature form of thePseudomonas aeruginosa elastase (52% identity),Helicobacter pylori zinc metalloprotease (61% identity), or proteases from several species of Vibrio (52 to 53% identity). The gene ahyB was insertionally inactivated, and the construct was used to create an isogenic ahyB mutant ofA. hydrophila. These first reports of a defined mutation in an extracellular protease of A. hydrophila demonstrate an important role in pathogenesis.

  • Copyright © 2000 American Society for Microbiology
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A Major Secreted Elastase Is Essential for Pathogenicity of Aeromonas hydrophila
Alberto Cascón, Javier Yugueros, Alejandro Temprano, María Sánchez, Carmen Hernanz, José María Luengo, Germán Naharro
Infection and Immunity Jun 2000, 68 (6) 3233-3241; DOI: 10.1128/IAI.68.6.3233-3241.2000

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A Major Secreted Elastase Is Essential for Pathogenicity of Aeromonas hydrophila
Alberto Cascón, Javier Yugueros, Alejandro Temprano, María Sánchez, Carmen Hernanz, José María Luengo, Germán Naharro
Infection and Immunity Jun 2000, 68 (6) 3233-3241; DOI: 10.1128/IAI.68.6.3233-3241.2000
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KEYWORDS

Aeromonas hydrophila
Bacterial Proteins
Fish Diseases
Gram-Negative Bacterial Infections
Oncorhynchus mykiss
Pancreatic Elastase

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